PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
23991830-4	2014	H2 S is produced by cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST).	Hydrogen Sulfide	0-4	mercaptopyruvate sulfurtransferase	Homo sapiens	91-127
23581969-3	2014	RECENT ADVANCES: In addition to cystathionine beta-synthase and cystathionine gamma-lyase, 3-mercaptopyruvate sulfurtransferase along with cysteine aminotransferase was recently demonstrated to produce H2S.	Hydrogen Sulfide	202-205	mercaptopyruvate sulfurtransferase	Homo sapiens	91-127
24036365-3	2013	H2S is produced from L-cysteine by enzymes such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase (CAT).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	123-159
24036365-3	2013	H2S is produced from L-cysteine by enzymes such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase (CAT).	Cysteine	21-31	mercaptopyruvate sulfurtransferase	Homo sapiens	123-159
23698001-0	2013	Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase.	Hydrogen Sulfide	34-37	mercaptopyruvate sulfurtransferase	Homo sapiens	58-92
23882260-3	2013	H2S is produced by enzymes from l-cysteine; cystathionine beta-synthase, cystathionine gamma-lyase, and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase.	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	104-140
23728586-7	2013	L-cysteine (L-Cys, a substrate of CBS, CSE and MPST) elicited relaxation in a dose-dependent manner on human bladder strips pre-contracted by acetylcholine chloride.	Cysteine	0-10	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
23728586-7	2013	L-cysteine (L-Cys, a substrate of CBS, CSE and MPST) elicited relaxation in a dose-dependent manner on human bladder strips pre-contracted by acetylcholine chloride.	Cysteine	12-17	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
23728586-7	2013	L-cysteine (L-Cys, a substrate of CBS, CSE and MPST) elicited relaxation in a dose-dependent manner on human bladder strips pre-contracted by acetylcholine chloride.	Acetylcholine	142-164	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
23764732-1	2013	3-Mercaptopyruvate (3-MP) is a metabolite of cysteine present in mammalian tissues and is known to be a substrate of 3-mercaptopyruvate sulfurtransferase (3MST, EC.3.4.1.2).	3-mercaptopyruvic acid	0-18	mercaptopyruvate sulfurtransferase	Homo sapiens	117-153
23764732-1	2013	3-Mercaptopyruvate (3-MP) is a metabolite of cysteine present in mammalian tissues and is known to be a substrate of 3-mercaptopyruvate sulfurtransferase (3MST, EC.3.4.1.2).	Cysteine	45-53	mercaptopyruvate sulfurtransferase	Homo sapiens	117-153
23698001-3	2013	In this study, we have expressed, purified, and crystallized human MST in the presence of the substrate 3-mercaptopyruvate (3-MP).	3-mercaptopyruvic acid	104-122	mercaptopyruvate sulfurtransferase	Homo sapiens	67-70
23698001-3	2013	In this study, we have expressed, purified, and crystallized human MST in the presence of the substrate 3-mercaptopyruvate (3-MP).	3-mercaptopyruvic acid	124-128	mercaptopyruvate sulfurtransferase	Homo sapiens	67-70
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	Hydrogen Sulfide	16-19	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	persulfides	111-121	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-1	2013	Mercaptopyruvate sulfurtransferase (MST) is a source of endogenous H2S, a gaseous signaling molecule implicated in a wide range of physiological processes.	Hydrogen Sulfide	67-70	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	Cysteine	133-141	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-1	2013	Mercaptopyruvate sulfurtransferase (MST) is a source of endogenous H2S, a gaseous signaling molecule implicated in a wide range of physiological processes.	Hydrogen Sulfide	67-70	mercaptopyruvate sulfurtransferase	Homo sapiens	36-39
23340406-2	2013	Hydrogen sulphide is known to be produced from L-cysteine by cystathionine beta-synthase, cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase.	Hydrogen Sulfide	0-17	mercaptopyruvate sulfurtransferase	Homo sapiens	120-156
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	dihydrolipoic acid	143-161	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	Homocysteine	176-188	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-4	2013	The kinetics of H2S production by MST from 3-MP was studied at pH 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glutathione, homocysteine, and thioredoxin, and in the presence of cyanide.	Cyanides	230-237	mercaptopyruvate sulfurtransferase	Homo sapiens	34-37
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	Pyruvic Acid	81-89	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	cysteine persulfide	109-128	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	Cysteine	130-133	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	Disulfides	218-227	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	Cysteine	109-117	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	93-100	mercaptopyruvate sulfurtransferase	Homo sapiens	77-80
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	2-(3,5-dihydroxyphenyl)-6-hydroxybenzothiazole	93-100	mercaptopyruvate sulfurtransferase	Homo sapiens	349-352
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	Serine	101-104	mercaptopyruvate sulfurtransferase	Homo sapiens	77-80
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	Serine	101-104	mercaptopyruvate sulfurtransferase	Homo sapiens	349-352
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	Cysteine	164-172	mercaptopyruvate sulfurtransferase	Homo sapiens	77-80
23698001-6	2013	The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas our kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor for MST.	persulfides	325-335	mercaptopyruvate sulfurtransferase	Homo sapiens	77-80
23537657-1	2013	Recent data show that lower concentrations of hydrogen sulfide (H2S), as well as endogenous, intramitochondrial production of H2S by the 3-mercaptopyruvate (3-MP)/3-mercaptopyruvate sulfurtransferase (3-MST) pathway serves as an electron donor and inorganic source of energy to support mitochondrial electron transport and ATP generation in mammalian cells by donating electrons to Complex II.	Hydrogen Sulfide	46-62	mercaptopyruvate sulfurtransferase	Homo sapiens	163-199
23537657-1	2013	Recent data show that lower concentrations of hydrogen sulfide (H2S), as well as endogenous, intramitochondrial production of H2S by the 3-mercaptopyruvate (3-MP)/3-mercaptopyruvate sulfurtransferase (3-MST) pathway serves as an electron donor and inorganic source of energy to support mitochondrial electron transport and ATP generation in mammalian cells by donating electrons to Complex II.	Hydrogen Sulfide	126-129	mercaptopyruvate sulfurtransferase	Homo sapiens	163-199
23537657-1	2013	Recent data show that lower concentrations of hydrogen sulfide (H2S), as well as endogenous, intramitochondrial production of H2S by the 3-mercaptopyruvate (3-MP)/3-mercaptopyruvate sulfurtransferase (3-MST) pathway serves as an electron donor and inorganic source of energy to support mitochondrial electron transport and ATP generation in mammalian cells by donating electrons to Complex II.	3-mercaptopyruvic acid	137-155	mercaptopyruvate sulfurtransferase	Homo sapiens	163-199
23537657-1	2013	Recent data show that lower concentrations of hydrogen sulfide (H2S), as well as endogenous, intramitochondrial production of H2S by the 3-mercaptopyruvate (3-MP)/3-mercaptopyruvate sulfurtransferase (3-MST) pathway serves as an electron donor and inorganic source of energy to support mitochondrial electron transport and ATP generation in mammalian cells by donating electrons to Complex II.	Adenosine Triphosphate	323-326	mercaptopyruvate sulfurtransferase	Homo sapiens	163-199
23340406-3	2013	Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase.	D-cysteine	95-105	mercaptopyruvate sulfurtransferase	Homo sapiens	116-152
23805308-1	2013	3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain.	Hydrogen Sulfide	88-104	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
23805308-1	2013	3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain.	Hydrogen Sulfide	88-104	mercaptopyruvate sulfurtransferase	Homo sapiens	38-42
23805308-1	2013	3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain.	Hydrogen Sulfide	106-109	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
23805308-1	2013	3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain.	Hydrogen Sulfide	106-109	mercaptopyruvate sulfurtransferase	Homo sapiens	38-42
23104984-0	2013	Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics.	Hydrogen Sulfide	19-35	mercaptopyruvate sulfurtransferase	Homo sapiens	50-86
23104984-6	2013	3-mercaptopyruvate (3-MP), the substrate of the mitochondrial enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) stimulated mitochondrial H(2)S production and enhanced mitochondrial electron transport and cellular bioenergetics at low concentrations (10-100 nM), while at higher concentrations, it inhibited cellular bioenergetics.	3-mercaptopyruvic acid	0-18	mercaptopyruvate sulfurtransferase	Homo sapiens	69-105
23104984-6	2013	3-mercaptopyruvate (3-MP), the substrate of the mitochondrial enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) stimulated mitochondrial H(2)S production and enhanced mitochondrial electron transport and cellular bioenergetics at low concentrations (10-100 nM), while at higher concentrations, it inhibited cellular bioenergetics.	Hydrogen Sulfide	139-144	mercaptopyruvate sulfurtransferase	Homo sapiens	69-105
23340406-2	2013	Hydrogen sulphide is known to be produced from L-cysteine by cystathionine beta-synthase, cystathionine gamma-lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase.	Cysteine	47-57	mercaptopyruvate sulfurtransferase	Homo sapiens	120-156
23340406-3	2013	Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase.	Hydrogen Sulfide	72-89	mercaptopyruvate sulfurtransferase	Homo sapiens	116-152
22517358-0	2012	Increased endogenous H2S generation by CBS, CSE, and 3MST gene therapy improves ex vivo renovascular relaxation in hyperhomocysteinemia.	Hydrogen Sulfide	21-24	mercaptopyruvate sulfurtransferase	Homo sapiens	53-57
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Homocysteine	65-68	mercaptopyruvate sulfurtransferase	Homo sapiens	145-181
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Homocysteine	65-68	mercaptopyruvate sulfurtransferase	Homo sapiens	183-187
22517358-5	2012	Ex vivo renal artery culture with CBS, CSE, and 3MST triple gene therapy generated more H(2)S in the presence of Hcy, and these arteries were more responsive to endothelial-dependent vasodilation compared with nontransfected arteries treated with high Hcy.	Hydrogen Sulfide	88-93	mercaptopyruvate sulfurtransferase	Homo sapiens	48-52
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	14-19	mercaptopyruvate sulfurtransferase	Homo sapiens	145-181
22517358-5	2012	Ex vivo renal artery culture with CBS, CSE, and 3MST triple gene therapy generated more H(2)S in the presence of Hcy, and these arteries were more responsive to endothelial-dependent vasodilation compared with nontransfected arteries treated with high Hcy.	Homocysteine	113-116	mercaptopyruvate sulfurtransferase	Homo sapiens	48-52
22517358-11	2012	We conclude that conversion of Hcy to H(2)S by CBS, CSE, or 3MST triple gene therapy improves renovascular function in HHcy.	Homocysteine	31-34	mercaptopyruvate sulfurtransferase	Homo sapiens	60-64
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	14-19	mercaptopyruvate sulfurtransferase	Homo sapiens	183-187
22517358-11	2012	We conclude that conversion of Hcy to H(2)S by CBS, CSE, or 3MST triple gene therapy improves renovascular function in HHcy.	Hydrogen Sulfide	38-43	mercaptopyruvate sulfurtransferase	Homo sapiens	60-64
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Homocysteine	51-63	mercaptopyruvate sulfurtransferase	Homo sapiens	145-181
22517358-2	2012	Endogenously, H(2)S is produced as a metabolite of homocysteine (Hcy) by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST).	Homocysteine	51-63	mercaptopyruvate sulfurtransferase	Homo sapiens	183-187
21275894-2	2011	H(2)S is generated by three enzymes, cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	0-5	mercaptopyruvate sulfurtransferase	Homo sapiens	108-144
21937432-3	2011	We recently demonstrated that 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase (CAT) produces H(2)S in the brain and in vascular endothelium.	Hydrogen Sulfide	126-131	mercaptopyruvate sulfurtransferase	Homo sapiens	30-66
21732914-0	2011	Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide.	dihydrolipoic acid	16-34	mercaptopyruvate sulfurtransferase	Homo sapiens	52-88
21732914-0	2011	Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide.	Hydrogen Sulfide	100-116	mercaptopyruvate sulfurtransferase	Homo sapiens	52-88
21732914-2	2011	We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate).	Hydrogen Sulfide	83-86	mercaptopyruvate sulfurtransferase	Homo sapiens	36-72
21527544-7	2011	We recently demonstrated that a third H(2)S-producing enzyme, 3-mercaptopyruvate sulfurtransferase (3MST), is expressed in neurons and vascular endothelium.	Hydrogen Sulfide	38-43	mercaptopyruvate sulfurtransferase	Homo sapiens	62-98
20414692-3	2011	It also affects the activity of two sulfurtransferases, 3-mercaptopyruvate sulfurtransferase and rhodanese, involved in the metabolism of sulfane sulfur-containing compounds and in consequence exerts an effect on the level of sulfane sulfur.	Hydrogen Sulfide	138-145	mercaptopyruvate sulfurtransferase	Homo sapiens	56-92
20414692-3	2011	It also affects the activity of two sulfurtransferases, 3-mercaptopyruvate sulfurtransferase and rhodanese, involved in the metabolism of sulfane sulfur-containing compounds and in consequence exerts an effect on the level of sulfane sulfur.	Sulfur	36-42	mercaptopyruvate sulfurtransferase	Homo sapiens	56-92
20414692-3	2011	It also affects the activity of two sulfurtransferases, 3-mercaptopyruvate sulfurtransferase and rhodanese, involved in the metabolism of sulfane sulfur-containing compounds and in consequence exerts an effect on the level of sulfane sulfur.	sulfane sulfur	138-152	mercaptopyruvate sulfurtransferase	Homo sapiens	56-92
20414692-4	2011	Under conditions, in which the raised level of sulfane sulfur was accompanied by an elevated activity of 3-mercaptopyruvate sulfurtransferase, the proliferation of the human astrocytome U373 line was decreased.	Hydrogen Sulfide	47-54	mercaptopyruvate sulfurtransferase	Homo sapiens	105-141
20414692-4	2011	Under conditions, in which the raised level of sulfane sulfur was accompanied by an elevated activity of 3-mercaptopyruvate sulfurtransferase, the proliferation of the human astrocytome U373 line was decreased.	Sulfur	55-61	mercaptopyruvate sulfurtransferase	Homo sapiens	105-141
20446008-5	2011	In all the investigated cell lines, the activity of MPST was higher than that of CST, which suggests that in these cells, the main pathway of sulfane sulfur formation is the MPST-catalyzed reaction.	sulfane sulfur	142-156	mercaptopyruvate sulfurtransferase	Homo sapiens	52-56
19605461-3	2009	Here we show that 3-mercaptopyruvate sulfurtransferase (3MST) and cysteine aminotransferase (CAT) are localized to vascular endothelium in the thoracic aorta and produce H(2)S.	Hydrogen Sulfide	170-175	mercaptopyruvate sulfurtransferase	Homo sapiens	18-54
19803743-6	2010	We recently demonstrated that the third H(2)S-producing enzyme, 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase (CAT) produces H(2)S in the brain as well as in vascular endothelium.	Hydrogen Sulfide	40-45	mercaptopyruvate sulfurtransferase	Homo sapiens	64-100
19803743-6	2010	We recently demonstrated that the third H(2)S-producing enzyme, 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase (CAT) produces H(2)S in the brain as well as in vascular endothelium.	Hydrogen Sulfide	160-165	mercaptopyruvate sulfurtransferase	Homo sapiens	64-100
18537713-1	2008	An intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase (MST, EC.2.8.1.2).	Disulfides	18-27	mercaptopyruvate sulfurtransferase	Homo sapiens	136-172
17520087-1	2007	The non-cytotoxic concentration (20 microM) of menadione (2-methyl-1,4-naphthoquinone), after 1 h of incubation, leads to loss of the activity of rhodanese by 33%, 3-mercaptopyruvate sulfurtransferase by 20%, as well as the level of sulfane sulfur by about 23% and glutathione by 12%, in the culture of U373 cells, in comparison with the control culture.	Vitamin K 3	47-56	mercaptopyruvate sulfurtransferase	Homo sapiens	164-200
18520135-2	2008	Reduced sulfur is also produced via the desulfuration of cysteine by several sulfurtransferases present in mammalian tissues; these enzymes include gamma-cystathionase (gamma-CST), and 3-mercaptopyruvate sulfurtransferase (3-MST).	Cysteine	57-65	mercaptopyruvate sulfurtransferase	Homo sapiens	185-221
18520135-2	2008	Reduced sulfur is also produced via the desulfuration of cysteine by several sulfurtransferases present in mammalian tissues; these enzymes include gamma-cystathionase (gamma-CST), and 3-mercaptopyruvate sulfurtransferase (3-MST).	Sulfur	8-14	mercaptopyruvate sulfurtransferase	Homo sapiens	185-221
17520087-1	2007	The non-cytotoxic concentration (20 microM) of menadione (2-methyl-1,4-naphthoquinone), after 1 h of incubation, leads to loss of the activity of rhodanese by 33%, 3-mercaptopyruvate sulfurtransferase by 20%, as well as the level of sulfane sulfur by about 23% and glutathione by 12%, in the culture of U373 cells, in comparison with the control culture.	Vitamin K 3	58-85	mercaptopyruvate sulfurtransferase	Homo sapiens	164-200
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	sulfane sulfur	0-14	mercaptopyruvate sulfurtransferase	Homo sapiens	143-179
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cysteine	71-79	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cysteine	71-79	mercaptopyruvate sulfurtransferase	Homo sapiens	36-40
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cyanides	96-103	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
16545926-1	2006	Mercaptopyruvate sulfurtransferase (MPST) plays a central role in both cysteine degradation and cyanide detoxification.	Cyanides	96-103	mercaptopyruvate sulfurtransferase	Homo sapiens	36-40
16740749-9	2006	In vitro, the TuM1 module is down-regulated in ER+ MCF7 cells upon treatment with tamoxifen, suggesting that TuM1 expression may be dependent on active signaling by ER.	Tamoxifen	82-91	mercaptopyruvate sulfurtransferase	Homo sapiens	14-18
16740749-9	2006	In vitro, the TuM1 module is down-regulated in ER+ MCF7 cells upon treatment with tamoxifen, suggesting that TuM1 expression may be dependent on active signaling by ER.	Tamoxifen	82-91	mercaptopyruvate sulfurtransferase	Homo sapiens	109-113
15886420-6	2005	Slight but significant cyanide-induced rise in MpST activity was observed only in the liver, which indicates a possibility of enhancement of its detoxification in reaction with mercapropyruvate in this organ.	Cyanides	23-30	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
15886420-6	2005	Slight but significant cyanide-induced rise in MpST activity was observed only in the liver, which indicates a possibility of enhancement of its detoxification in reaction with mercapropyruvate in this organ.	mercapropyruvate	177-193	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
16500920-3	2006	Rhodanese can detoxify H2S and is comprised of two isoenzymes: thiosulfate sulfurtransferase (TST) and mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	23-26	mercaptopyruvate sulfurtransferase	Homo sapiens	103-137
16500920-3	2006	Rhodanese can detoxify H2S and is comprised of two isoenzymes: thiosulfate sulfurtransferase (TST) and mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	23-26	mercaptopyruvate sulfurtransferase	Homo sapiens	139-142
16500920-4	2006	Using specific antisera to discriminate TST from MST, we found that only TST could detoxify H2S.	Hydrogen Sulfide	92-95	mercaptopyruvate sulfurtransferase	Homo sapiens	49-52
16719781-0	2006	The mercaptopyruvate pathway in cysteine catabolism: a physiologic role and related disease of the multifunctional 3-mercaptopyruvate sulfurtransferase.	3-mercaptopyruvic acid	4-20	mercaptopyruvate sulfurtransferase	Homo sapiens	115-151
16719781-4	2006	The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox.	3-mercaptopyruvic acid	4-20	mercaptopyruvate sulfurtransferase	Homo sapiens	148-184
16719781-4	2006	The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox.	Cysteine	39-47	mercaptopyruvate sulfurtransferase	Homo sapiens	148-184
16719781-4	2006	The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox.	Cysteine	108-116	mercaptopyruvate sulfurtransferase	Homo sapiens	148-184
16719781-4	2006	The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox.	Pyruvic Acid	12-20	mercaptopyruvate sulfurtransferase	Homo sapiens	148-184
16719781-5	2006	3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide, it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine.	Hydrogen Peroxide	139-156	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-5	2006	3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide, it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine.	sulfenate	205-214	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-5	2006	3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide, it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine.	Cysteine	237-245	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	Cyanides	53-60	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	persulfides	96-106	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	Cysteine	129-137	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-7	2006	3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction.	Cyanides	180-187	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
16719781-9	2006	These facts suggest that 3-mercaptopyruvate sulfurtransferase has physiologic roles as an antioxidant and a cyanide antidote; is essential for neural function, and participates in cysteine degradation.	Cyanides	108-115	mercaptopyruvate sulfurtransferase	Homo sapiens	25-61
16719781-9	2006	These facts suggest that 3-mercaptopyruvate sulfurtransferase has physiologic roles as an antioxidant and a cyanide antidote; is essential for neural function, and participates in cysteine degradation.	Cysteine	180-188	mercaptopyruvate sulfurtransferase	Homo sapiens	25-61
15653770-6	2005	3-Mercaptopyruvate sulfurtransferase (3-MST; EC 2.8.1.2) and GAPDH also bound selenium supplied as selenodiglutathione formed from SeO3(2-) and glutathione.	Selenium	78-86	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
15653770-6	2005	3-Mercaptopyruvate sulfurtransferase (3-MST; EC 2.8.1.2) and GAPDH also bound selenium supplied as selenodiglutathione formed from SeO3(2-) and glutathione.	seo3	131-135	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
12871026-0	2003	Do antidotes for acute cyanide poisoning act on mercaptopyruvate sulfurtransferase to facilitate detoxification?	Cyanides	23-30	mercaptopyruvate sulfurtransferase	Homo sapiens	48-82
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	sulfane sulfur	0-14	mercaptopyruvate sulfurtransferase	Homo sapiens	181-185
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	Cysteine	53-61	mercaptopyruvate sulfurtransferase	Homo sapiens	143-179
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	Cysteine	53-61	mercaptopyruvate sulfurtransferase	Homo sapiens	181-185
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	Sulfur	8-14	mercaptopyruvate sulfurtransferase	Homo sapiens	143-179
11785922-5	2001	Sulfane sulfur compounds are formed in the anaerobic cysteine sulfur metabolism with the participation of such enzymes as cystathionase (CST), 3-mercaptopyruvate sulfurtransferase (MpST) and rhodanese (thiosulfate: cyanide sulfurtransferase).	Sulfur	8-14	mercaptopyruvate sulfurtransferase	Homo sapiens	181-185
10788459-7	2000	Enzymatic characterization showed that, of the twelve mutated M-PSTs, mutations at residues Asp-86, Glu-89, and Glu-146 resulted in a dramatic decrease in V(max)/K(m) with dopamine as substrate, being greater than 450 times for the D86A/E89I/E146A mutated M-PST.	Aspartic Acid	92-95	mercaptopyruvate sulfurtransferase	Homo sapiens	62-67
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Alanine	65-68	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-7	2000	Enzymatic characterization showed that, of the twelve mutated M-PSTs, mutations at residues Asp-86, Glu-89, and Glu-146 resulted in a dramatic decrease in V(max)/K(m) with dopamine as substrate, being greater than 450 times for the D86A/E89I/E146A mutated M-PST.	Glutamic Acid	100-103	mercaptopyruvate sulfurtransferase	Homo sapiens	62-67
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Alanine	65-68	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Isoleucine	73-76	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Isoleucine	73-76	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Alanine	85-88	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-12	2000	These results indicated that, in contrast to M-PST, mutations at Ala-86, Ile-89, and Ala-146 to the corresponding residues in M-PST are not sufficient for rendering the change of P-PST substrate phenotype to that of M-PST.	Alanine	85-88	mercaptopyruvate sulfurtransferase	Homo sapiens	126-131
10788459-7	2000	Enzymatic characterization showed that, of the twelve mutated M-PSTs, mutations at residues Asp-86, Glu-89, and Glu-146 resulted in a dramatic decrease in V(max)/K(m) with dopamine as substrate, being greater than 450 times for the D86A/E89I/E146A mutated M-PST.	Glutamic Acid	112-115	mercaptopyruvate sulfurtransferase	Homo sapiens	62-67
10788459-7	2000	Enzymatic characterization showed that, of the twelve mutated M-PSTs, mutations at residues Asp-86, Glu-89, and Glu-146 resulted in a dramatic decrease in V(max)/K(m) with dopamine as substrate, being greater than 450 times for the D86A/E89I/E146A mutated M-PST.	Dopamine	172-180	mercaptopyruvate sulfurtransferase	Homo sapiens	62-67
10788459-8	2000	With p-nitrophenol as substrate, the V(max)/K(m) determined for the D86A/E89I/E146A-mutated M-PST increased more than 25 times and approached that determined for the wild-type P-PST.	4-nitrophenol	5-18	mercaptopyruvate sulfurtransferase	Homo sapiens	92-97
10460806-11	1999	P-PST-1 sulfates 3-OH-PPX, 3-OH-ropi, and 4-OH-xyl; M-PST and EST conjugate 3-OH-PPX, 3-OH-ropi, and 4-OH-ropi whereas ST1B2 sulfates only 4-OH-xyl.	3-OH-ropivacaine	86-95	mercaptopyruvate sulfurtransferase	Homo sapiens	52-57
10608851-2	1999	Humans are one of the few species that produce large amounts of catecholamine sulfates, and they have evolved a specific sulfotransferase, SULT1A3 (M-PST), to catalyze the formation of these conjugates.	catecholamine sulfates	64-86	mercaptopyruvate sulfurtransferase	Homo sapiens	148-153
10460806-11	1999	P-PST-1 sulfates 3-OH-PPX, 3-OH-ropi, and 4-OH-xyl; M-PST and EST conjugate 3-OH-PPX, 3-OH-ropi, and 4-OH-ropi whereas ST1B2 sulfates only 4-OH-xyl.	4-oh-ropi	101-110	mercaptopyruvate sulfurtransferase	Homo sapiens	52-57
10657971-0	2000	Human phenol sulfotransferases hP-PST and hM-PST activate propane 2-nitronate to a genotoxicant.	propane-2-nitronate	58-77	mercaptopyruvate sulfurtransferase	Homo sapiens	42-48
10460806-11	1999	P-PST-1 sulfates 3-OH-PPX, 3-OH-ropi, and 4-OH-xyl; M-PST and EST conjugate 3-OH-PPX, 3-OH-ropi, and 4-OH-ropi whereas ST1B2 sulfates only 4-OH-xyl.	4-oh-xyl	139-147	mercaptopyruvate sulfurtransferase	Homo sapiens	52-57
9325148-11	1997	P-PST prefers p-nitrophenol as substrate, is sensitive to inhibition by DCNP, and is thermostable; in contrast, M-PST prefers monoamines as substrate, is not sensitive to DCNP, and is thermolabile.	monoamines	126-136	mercaptopyruvate sulfurtransferase	Homo sapiens	112-117
9839429-6	1998	For isoproterenol, the Km,app for M-PST was 6.1 times higher for the active (R)- than for the inactive (S)-enantiomer.	Isoproterenol	4-17	mercaptopyruvate sulfurtransferase	Homo sapiens	34-39
8093002-14	1994	COS-expressed HAST1 and HAST3 displayed inhibition profiles with the ST inhibitor 2,6-dichloro-4-nitrophenol (DCNP), identical with human liver cytosolic P-PST and M-PST activities respectively.	carbonyl sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	164-169
8806051-0	1996	The effect of three alpha-keto acids on 3-mercaptopyruvate sulfurtransferase activity.	alpha-keto acids	20-36	mercaptopyruvate sulfurtransferase	Homo sapiens	40-76
8806051-1	1996	3-Mercaptopyruvate sulfurtransferase catalyzes the transfer of sulfur from 3-mercaptopyruvate to several possible acceptor molecules, one of which is cyanide.	3-mercaptopyruvic acid	75-93	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
8806051-1	1996	3-Mercaptopyruvate sulfurtransferase catalyzes the transfer of sulfur from 3-mercaptopyruvate to several possible acceptor molecules, one of which is cyanide.	Cyanides	150-157	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
8806051-2	1996	Because the transsulfuration of cyanide is the primary in vivo mechanism of detoxification, 3-mercaptopyruvate sulfurtransferase may function in the enzymatic detoxification of cyanide in vivo.	Cyanides	177-184	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
8806051-5	1996	Thus, the effect of these three alpha-keto acids on the enzyme 3-mercaptopyruvate sulfurtransferase was examined.	alpha-keto acids	32-48	mercaptopyruvate sulfurtransferase	Homo sapiens	63-99
8806051-6	1996	All three alpha-keto acids inhibited 3-mercaptopyruvate sulfurtransferase in a concentration-dependent manner and were determined to be uncompetitive inhibitors of MST with respect to 3-mercaptopyruvate.	alpha-keto acids	10-26	mercaptopyruvate sulfurtransferase	Homo sapiens	37-73
8565785-1	1995	The cDNA for the human monoamine-sulfating form of phenol sulfotransferase (hM-PST) was isolated from a T47D human breast carcinoma lambda gt10 cDNA library, and the active enzyme was expressed in Escherichia coli.	monoamine	23-32	mercaptopyruvate sulfurtransferase	Homo sapiens	76-82
8565785-5	1995	Monoamine neurotransmittors, such as epinephrine and dopamine, were maximally conjugated at lower concentrations by expressed hM-PST (2 and 20 microM, respectively) than by hP-PST (1 and 1 mM, respectively).	monoamine	0-9	mercaptopyruvate sulfurtransferase	Homo sapiens	126-132
8565785-5	1995	Monoamine neurotransmittors, such as epinephrine and dopamine, were maximally conjugated at lower concentrations by expressed hM-PST (2 and 20 microM, respectively) than by hP-PST (1 and 1 mM, respectively).	Epinephrine	37-48	mercaptopyruvate sulfurtransferase	Homo sapiens	126-132
8565785-5	1995	Monoamine neurotransmittors, such as epinephrine and dopamine, were maximally conjugated at lower concentrations by expressed hM-PST (2 and 20 microM, respectively) than by hP-PST (1 and 1 mM, respectively).	Dopamine	53-61	mercaptopyruvate sulfurtransferase	Homo sapiens	126-132
8093002-18	1994	This report on the functional characterization of P-PST and M-PST cDNAs provides important information on the structural as well as functional relationships of human PSTs, which sulphate a vast array of exogenous and endogenous compounds.	Sulfates	178-186	mercaptopyruvate sulfurtransferase	Homo sapiens	60-65
2327787-2	1990	During the purification procedure, P-PST was resolved from the monoamine-sulfating form of phenol sulfotransferase (M-PST) and dehydroepiandrosterone sulfotransferase, which are also present in human liver cytosol.	monoamine	63-72	mercaptopyruvate sulfurtransferase	Homo sapiens	116-121
20732163-0	1992	The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese.	picrylsulphonic acid	14-34	mercaptopyruvate sulfurtransferase	Homo sapiens	87-124
20732163-0	1992	The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese.	Cyanides	61-68	mercaptopyruvate sulfurtransferase	Homo sapiens	87-124
20732163-0	1992	The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese.	thiocyanate	72-83	mercaptopyruvate sulfurtransferase	Homo sapiens	87-124
20732163-1	1992	This study indicates that 3-mercaptopyruvate sulphurtransferase (MPST; EC 2.8.1.2) activity may serve as a useful in vitro indicator for the analysis of cyanide detoxification to thiocyanate.	thiocyanate	179-190	mercaptopyruvate sulfurtransferase	Homo sapiens	26-63
20732163-1	1992	This study indicates that 3-mercaptopyruvate sulphurtransferase (MPST; EC 2.8.1.2) activity may serve as a useful in vitro indicator for the analysis of cyanide detoxification to thiocyanate.	thiocyanate	179-190	mercaptopyruvate sulfurtransferase	Homo sapiens	65-69
20732163-2	1992	The time course and capacity of MPST to detoxify cyanide was equal to or exceeded that of rhodanese.	Cyanides	49-56	mercaptopyruvate sulfurtransferase	Homo sapiens	32-36
20732163-3	1992	Picrylsulphonic acid strongly inhibited purified rhodanese, but in the presence of mercaptopyruvate, it could increase the formation of thiocyanate catalysed by MPST.	picrylsulphonic acid	0-20	mercaptopyruvate sulfurtransferase	Homo sapiens	161-165
20732163-3	1992	Picrylsulphonic acid strongly inhibited purified rhodanese, but in the presence of mercaptopyruvate, it could increase the formation of thiocyanate catalysed by MPST.	3-mercaptopyruvic acid	83-99	mercaptopyruvate sulfurtransferase	Homo sapiens	161-165
20732163-3	1992	Picrylsulphonic acid strongly inhibited purified rhodanese, but in the presence of mercaptopyruvate, it could increase the formation of thiocyanate catalysed by MPST.	thiocyanate	136-147	mercaptopyruvate sulfurtransferase	Homo sapiens	161-165
20732163-4	1992	Formation of thiocyanate by MPST followed a linear time course and had a linear relation to enzyme level.	thiocyanate	13-24	mercaptopyruvate sulfurtransferase	Homo sapiens	28-32
34458274-6	2021	Cysteine degradation depends on the action of the H2S-synthesizing enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and/or 3-mercaptopyruvate sulfurtransferase (MpST; together with cysteine aminotransferase, CAT).	Cysteine	0-8	mercaptopyruvate sulfurtransferase	Homo sapiens	150-186
32860641-3	2020	On the other hand, 3-mercaptopyruvate sulfurtransferase transfers sulfur from a substrate 3-mercaptopyruvate to the cysteine residues of acceptor proteins.	Cysteine	116-124	mercaptopyruvate sulfurtransferase	Homo sapiens	21-55
34458274-6	2021	Cysteine degradation depends on the action of the H2S-synthesizing enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and/or 3-mercaptopyruvate sulfurtransferase (MpST; together with cysteine aminotransferase, CAT).	Cysteine	0-8	mercaptopyruvate sulfurtransferase	Homo sapiens	188-192
34458274-9	2021	However, the relative contributions of each of these enzymes (CBS/CSE/MpST) on cysteine-derived ATP synthesis under hypoxia remains unclear, due to the lack of specific inhibitors.	Cysteine	79-87	mercaptopyruvate sulfurtransferase	Homo sapiens	70-74
34458274-6	2021	Cysteine degradation depends on the action of the H2S-synthesizing enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and/or 3-mercaptopyruvate sulfurtransferase (MpST; together with cysteine aminotransferase, CAT).	Deuterium	50-53	mercaptopyruvate sulfurtransferase	Homo sapiens	150-186
34458274-6	2021	Cysteine degradation depends on the action of the H2S-synthesizing enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and/or 3-mercaptopyruvate sulfurtransferase (MpST; together with cysteine aminotransferase, CAT).	Deuterium	50-53	mercaptopyruvate sulfurtransferase	Homo sapiens	188-192
34458274-7	2021	In normoxia, CBS and CSE inhibition had a mild impact on cysteine-sustained ATP production, pointing out the relevance of CAT + MpST pathway.	Cysteine	57-65	mercaptopyruvate sulfurtransferase	Homo sapiens	128-132
34458274-7	2021	In normoxia, CBS and CSE inhibition had a mild impact on cysteine-sustained ATP production, pointing out the relevance of CAT + MpST pathway.	Adenosine Triphosphate	76-79	mercaptopyruvate sulfurtransferase	Homo sapiens	128-132
33554726-2	2021	RESULTS: Experiments in human adipose tissue explants and in isolated preadipocytes demonstrated that exogenous H2S or the activation of endogenous H2S biosynthesis resulted in increased adipogenesis, insulin action, sirtuin deacetylase and PPARgamma transcriptional activity, whereas chemical inhibition and gene knockdown of each enzyme generating H2S (CTH, CBS, MPST) led to altered adipocyte differentiation, cellular senescence and increased inflammation.	Deuterium	112-115	mercaptopyruvate sulfurtransferase	Homo sapiens	365-369
34208749-8	2021	Two additional pathways for the production of H2S with 3-mercaptopyruvate sulfurtransferase (3MST) from l- and d-cysteine have been identified.	Deuterium	46-49	mercaptopyruvate sulfurtransferase	Homo sapiens	55-91
34208749-8	2021	Two additional pathways for the production of H2S with 3-mercaptopyruvate sulfurtransferase (3MST) from l- and d-cysteine have been identified.	l- and d-cysteine	104-121	mercaptopyruvate sulfurtransferase	Homo sapiens	55-91
35023928-8	2022	Micronutrients increased 3-mercaptopyruvate (P = .03), reporting on the activity of CAT that provides the substrate for H2S release within mitochondria by 3MPST, decreased lanthionine (P = .024), reporting the release of H2S from CBS, and had no significant effect of H2S release from CSE.	3-mercaptopyruvic acid	25-43	mercaptopyruvate sulfurtransferase	Homo sapiens	156-160
35023928-8	2022	Micronutrients increased 3-mercaptopyruvate (P = .03), reporting on the activity of CAT that provides the substrate for H2S release within mitochondria by 3MPST, decreased lanthionine (P = .024), reporting the release of H2S from CBS, and had no significant effect of H2S release from CSE.	Deuterium	120-123	mercaptopyruvate sulfurtransferase	Homo sapiens	156-160
3469673-1	1987	Sulfhydryl modification of 22 human erythrocyte enzymes was achieved by exposing intact erythrocytes, hemolysates, and partially purified enzymes to persulfides (RSSH) generated nonenzymatically from cystine in the presence of pyridoxal phosphate and mercaptopyruvate, which donates its sulfur to suitable acceptors with the mediation of the carrier enzyme, mercaptopyruvate sulfurtransferase (EC 2.8.1.2).	Sulfhydryl Compounds	0-10	mercaptopyruvate sulfurtransferase	Homo sapiens	358-392
4370594-0	1974	Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin.	Iron	69-73	mercaptopyruvate sulfurtransferase	Homo sapiens	8-44
33856792-1	2021	The enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) is one of the more recently identified mammalian sources of H2S.	Deuterium	116-119	mercaptopyruvate sulfurtransferase	Homo sapiens	11-47
34302686-1	2021	Hydrogen sulfide, a small molecule, produced by endogenous enzymes, such as CTH, CBS, and MPST using L-cysteine as substrates, has been reported to have numerous protective effects.	Hydrogen Sulfide	0-16	mercaptopyruvate sulfurtransferase	Homo sapiens	90-94
34302686-1	2021	Hydrogen sulfide, a small molecule, produced by endogenous enzymes, such as CTH, CBS, and MPST using L-cysteine as substrates, has been reported to have numerous protective effects.	Cysteine	101-111	mercaptopyruvate sulfurtransferase	Homo sapiens	90-94
35174476-2	2022	H2S is synthesized by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (MST).	Deuterium	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	94-130
2718769-1	1989	The isoelectric point (pI) value of 3-mercaptopyruvate sulfurtransferase (MST) from human erythrocytes was determined to be 6.3 at 10 degrees C by isoelectric focusing in horizontal slab polyacrylamide gel containing 2% carrier ampholyte (pH 3-10).	polyacrylamide	187-201	mercaptopyruvate sulfurtransferase	Homo sapiens	36-72
2718769-1	1989	The isoelectric point (pI) value of 3-mercaptopyruvate sulfurtransferase (MST) from human erythrocytes was determined to be 6.3 at 10 degrees C by isoelectric focusing in horizontal slab polyacrylamide gel containing 2% carrier ampholyte (pH 3-10).	polyacrylamide	187-201	mercaptopyruvate sulfurtransferase	Homo sapiens	74-77
3860259-1	1985	The kinetic and biochemical properties of a purified, monoamine-sulfating form of phenol sulfotransferase (M-PST) from human brain are described.	monoamine	54-63	mercaptopyruvate sulfurtransferase	Homo sapiens	107-112
3860259-2	1985	M-PST activity was separated and purified from phenol-sulfating activity by anion-exchange chromatography on DEAE-cellulose and subsequently purified on AffiGel Blue and Sephacryl S-200, routinely giving a final purification of over 20 000-fold, with approximately a 3% yield.	Phenol	47-53	mercaptopyruvate sulfurtransferase	Homo sapiens	0-5
3860259-2	1985	M-PST activity was separated and purified from phenol-sulfating activity by anion-exchange chromatography on DEAE-cellulose and subsequently purified on AffiGel Blue and Sephacryl S-200, routinely giving a final purification of over 20 000-fold, with approximately a 3% yield.	DEAE-Cellulose	109-123	mercaptopyruvate sulfurtransferase	Homo sapiens	0-5
3860259-2	1985	M-PST activity was separated and purified from phenol-sulfating activity by anion-exchange chromatography on DEAE-cellulose and subsequently purified on AffiGel Blue and Sephacryl S-200, routinely giving a final purification of over 20 000-fold, with approximately a 3% yield.	sephacryl S 200	170-185	mercaptopyruvate sulfurtransferase	Homo sapiens	0-5
3860259-6	1985	Kinetic analysis demonstrated that sulfation by M-PST proceeds via an ordered, bisubstrate reaction mechanism, where 3"-phosphoadenosine 5"-phosphosulfate (PAPS) is the leading substrate.	Phosphoadenosine Phosphosulfate	117-154	mercaptopyruvate sulfurtransferase	Homo sapiens	48-53
3860259-6	1985	Kinetic analysis demonstrated that sulfation by M-PST proceeds via an ordered, bisubstrate reaction mechanism, where 3"-phosphoadenosine 5"-phosphosulfate (PAPS) is the leading substrate.	Phosphoadenosine Phosphosulfate	156-160	mercaptopyruvate sulfurtransferase	Homo sapiens	48-53
7045223-4	1982	In contrast, concomitant administration of 2 X 10(7) thioglycollate-stimulated peritoneal exudate adherent cells plus 10(8) alloimmune syngeneic spleen cells produced acute allograft rejection in 50% of B recipients within 10 to 12 days, while in every instance grafts underwent acute rejection (MST +/- SD = 10.0 +/- 1.4 days) in B recipients treated with interleukin 2 (IL 2) rich conditioned supernatant plus sensitized cells.	Thioglycolates	53-67	mercaptopyruvate sulfurtransferase	Homo sapiens	296-299
6928374-0	1980	3-Mercaptopyruvate sulfurtransferase: rapid equilibrium-ordered mechanism with cyanide as the acceptor substrate.	Cyanides	79-86	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
6928374-1	1980	A steady-state kinetic analysis of 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) using cyanide as the sulfur-acceptor substrate was performed.	Cyanides	91-98	mercaptopyruvate sulfurtransferase	Homo sapiens	35-71
33554726-2	2021	RESULTS: Experiments in human adipose tissue explants and in isolated preadipocytes demonstrated that exogenous H2S or the activation of endogenous H2S biosynthesis resulted in increased adipogenesis, insulin action, sirtuin deacetylase and PPARgamma transcriptional activity, whereas chemical inhibition and gene knockdown of each enzyme generating H2S (CTH, CBS, MPST) led to altered adipocyte differentiation, cellular senescence and increased inflammation.	Deuterium	148-151	mercaptopyruvate sulfurtransferase	Homo sapiens	365-369
33554726-2	2021	RESULTS: Experiments in human adipose tissue explants and in isolated preadipocytes demonstrated that exogenous H2S or the activation of endogenous H2S biosynthesis resulted in increased adipogenesis, insulin action, sirtuin deacetylase and PPARgamma transcriptional activity, whereas chemical inhibition and gene knockdown of each enzyme generating H2S (CTH, CBS, MPST) led to altered adipocyte differentiation, cellular senescence and increased inflammation.	Deuterium	148-151	mercaptopyruvate sulfurtransferase	Homo sapiens	365-369
32417499-3	2020	Three enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercaptopyruvate-sulfurtransferase (MPST), are mainly responsible for H2S production.	Deuterium	159-162	mercaptopyruvate sulfurtransferase	Homo sapiens	87-123
33338600-5	2021	In a hyperoxia-based animal model of BPD, oxygen exposure deregulated MPST expression during post-natal lung development, where MPST was localized to the smooth muscle layer of the pulmonary vessels in developing lungs.	Oxygen	42-48	mercaptopyruvate sulfurtransferase	Homo sapiens	70-74
33338600-5	2021	In a hyperoxia-based animal model of BPD, oxygen exposure deregulated MPST expression during post-natal lung development, where MPST was localized to the smooth muscle layer of the pulmonary vessels in developing lungs.	Oxygen	42-48	mercaptopyruvate sulfurtransferase	Homo sapiens	128-132
33352938-4	2020	Herein, we explored the potential role of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide (H2S) system in the regulation of the endoplasmic reticulum (ER) stress and of its downstream processes in the immortalized hepatic cell line HepG2 in vitro.	Deuterium	101-104	mercaptopyruvate sulfurtransferase	Homo sapiens	46-82
33352938-6	2020	Genetic silencing of 3-MST or pharmacological inhibition of the key enzymes involved in hepatocyte H2S biosynthesis exacerbated many readouts related to ER-stress or its downstream functional responses.	Deuterium	99-102	mercaptopyruvate sulfurtransferase	Homo sapiens	23-26
33352938-7	2020	Our findings implicate the 3-MST/H2S system in the intracellular network that governs proteostasis and ER-stress adaptability in hepatocytes and reinforce the therapeutic potential of pharmacological H2S supplementation.	Deuterium	33-36	mercaptopyruvate sulfurtransferase	Homo sapiens	29-32
33352938-7	2020	Our findings implicate the 3-MST/H2S system in the intracellular network that governs proteostasis and ER-stress adaptability in hepatocytes and reinforce the therapeutic potential of pharmacological H2S supplementation.	Deuterium	200-203	mercaptopyruvate sulfurtransferase	Homo sapiens	29-32
33296712-5	2021	Rare potentially damaging TST p.Arg206Cys (rs61742280) and MPST p.His317Tyr (rs1038542246) heterozygous variants were identified but with no impact on subject phenotypes.	his317tyr	66-75	mercaptopyruvate sulfurtransferase	Homo sapiens	59-63
32897507-7	2020	Results suggest, tocopherol is more inductive to monoamine-SULT (MPST) and Dehydroepiandrosterone-SULT (DHEAST) compared to that of tocotrienol (inconsistent change in PPST, phenol sulfotransferase/MPST/EST, estrogen sulfotransferase).	Tocopherols	17-27	mercaptopyruvate sulfurtransferase	Homo sapiens	65-69
32897507-7	2020	Results suggest, tocopherol is more inductive to monoamine-SULT (MPST) and Dehydroepiandrosterone-SULT (DHEAST) compared to that of tocotrienol (inconsistent change in PPST, phenol sulfotransferase/MPST/EST, estrogen sulfotransferase).	Tocopherols	17-27	mercaptopyruvate sulfurtransferase	Homo sapiens	198-202
33055309-0	2021	3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking.	sulfane sulfur	69-83	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	3-mercaptopyruvic acid	107-125	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	3-mercaptopyruvic acid	107-125	mercaptopyruvate sulfurtransferase	Homo sapiens	38-42
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	3-mercaptopyruvic acid	127-130	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	3-mercaptopyruvic acid	127-130	mercaptopyruvate sulfurtransferase	Homo sapiens	38-42
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	hydropersulfide	160-175	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
33055309-1	2021	3-Mercaptopyruvate sulfurtransferase (MPST, also annotated as 3-MST or MST) catalyzes the desulfuration of 3-mercaptopyruvate (3MP) to generate an enzyme-bound hydropersulfide.	hydropersulfide	160-175	mercaptopyruvate sulfurtransferase	Homo sapiens	38-42
33055309-2	2021	Subsequently, MPST transfers the persulfide"s outer sulfur atom to proteins or small molecule acceptors.	persulfides	33-43	mercaptopyruvate sulfurtransferase	Homo sapiens	14-18
33055309-2	2021	Subsequently, MPST transfers the persulfide"s outer sulfur atom to proteins or small molecule acceptors.	Sulfur	52-58	mercaptopyruvate sulfurtransferase	Homo sapiens	14-18
33055309-3	2021	MPST activity is known to be involved in hydrogen sulfide (H2S) generation, tRNA thiolation, protein urmylation and cyanide detoxification.	Hydrogen Sulfide	41-57	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
33055309-3	2021	MPST activity is known to be involved in hydrogen sulfide (H2S) generation, tRNA thiolation, protein urmylation and cyanide detoxification.	Deuterium	59-62	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
33055309-3	2021	MPST activity is known to be involved in hydrogen sulfide (H2S) generation, tRNA thiolation, protein urmylation and cyanide detoxification.	thiolation	81-91	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
33055309-3	2021	MPST activity is known to be involved in hydrogen sulfide (H2S) generation, tRNA thiolation, protein urmylation and cyanide detoxification.	Cyanides	116-123	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
33055309-5	2021	Deletion and overexpression experiments suggest that MPST contributes to oxidative stress resistance, mitochondrial respiratory function and the regulation of fatty acid metabolism.	Fatty Acids	159-169	mercaptopyruvate sulfurtransferase	Homo sapiens	53-57
32417499-3	2020	Three enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercaptopyruvate-sulfurtransferase (MPST), are mainly responsible for H2S production.	Deuterium	159-162	mercaptopyruvate sulfurtransferase	Homo sapiens	125-129
32871814-4	2020	H2S is endogenously produced by three enzymes: Cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (MPST).	Deuterium	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	119-155
32871814-4	2020	H2S is endogenously produced by three enzymes: Cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (MPST).	Deuterium	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	157-161
30500457-0	2020	Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.	Hydrogen Sulfide	67-83	mercaptopyruvate sulfurtransferase	Homo sapiens	22-58
30500457-0	2020	Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.	Hydrogen Sulfide	85-88	mercaptopyruvate sulfurtransferase	Homo sapiens	60-65
30500457-5	2020	However, until recently, less attention has been paid to the third enzymatic source of H2S, 3-mercaptopyruvate sulfurtransferase (3-MST), even though several of its biological and biochemical features - e.g. its partial mitochondrial localization, its ability to produce polysulfides, which, in turn, can induce functionally relevant posttranslational protein modifications - makes it a potential candidate.	Hydrogen Sulfide	87-90	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
32664399-4	2020	Interestingly, the peripheral blood mononuclear cells obtained from the MS patients had a lower expression of the H2S-producing enzyme, 3-mercaptopyruvate-sulfurtransferase (MPST), in comparison to those obtained from healthy donors.	Deuterium	114-117	mercaptopyruvate sulfurtransferase	Homo sapiens	136-172
32664399-4	2020	Interestingly, the peripheral blood mononuclear cells obtained from the MS patients had a lower expression of the H2S-producing enzyme, 3-mercaptopyruvate-sulfurtransferase (MPST), in comparison to those obtained from healthy donors.	Deuterium	114-117	mercaptopyruvate sulfurtransferase	Homo sapiens	174-178
31734816-13	2020	The current results suggest that reduced levels of the mitochondrial enzyme 3-MPST in OA cartilage might be, at least in part, responsible for a reduction in H2S biosynthesis in this tissue and that impaired H2S biosynthesis in the joint might be a contributing factor to OA.	hydrogen sulfite	158-161	mercaptopyruvate sulfurtransferase	Homo sapiens	78-82
31734816-13	2020	The current results suggest that reduced levels of the mitochondrial enzyme 3-MPST in OA cartilage might be, at least in part, responsible for a reduction in H2S biosynthesis in this tissue and that impaired H2S biosynthesis in the joint might be a contributing factor to OA.	hydrogen sulfite	208-211	mercaptopyruvate sulfurtransferase	Homo sapiens	78-82
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	3-mercaptopyruvic acid	76-94	mercaptopyruvate sulfurtransferase	Homo sapiens	0-37
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	3-mercaptopyruvic acid	76-94	mercaptopyruvate sulfurtransferase	Homo sapiens	39-43
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	sulfane sulfur	116-130	mercaptopyruvate sulfurtransferase	Homo sapiens	0-37
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	sulfane sulfur	116-130	mercaptopyruvate sulfurtransferase	Homo sapiens	39-43
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	persulfides	152-162	mercaptopyruvate sulfurtransferase	Homo sapiens	0-37
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	persulfides	152-162	mercaptopyruvate sulfurtransferase	Homo sapiens	39-43
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	Cysteine	224-232	mercaptopyruvate sulfurtransferase	Homo sapiens	0-37
32179647-1	2020	3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine.	Cysteine	224-232	mercaptopyruvate sulfurtransferase	Homo sapiens	39-43
32179647-2	2020	Hydrogen sulfide (H2S), a signaling molecule implicated in many physiological processes, can be released from the persulfide product of the MPST reaction.	Hydrogen Sulfide	0-16	mercaptopyruvate sulfurtransferase	Homo sapiens	140-144
32179647-2	2020	Hydrogen sulfide (H2S), a signaling molecule implicated in many physiological processes, can be released from the persulfide product of the MPST reaction.	Deuterium	18-21	mercaptopyruvate sulfurtransferase	Homo sapiens	140-144
32179647-2	2020	Hydrogen sulfide (H2S), a signaling molecule implicated in many physiological processes, can be released from the persulfide product of the MPST reaction.	persulfides	114-124	mercaptopyruvate sulfurtransferase	Homo sapiens	140-144
32179647-6	2020	We also show that N-acetylcysteine, a widely-used antioxidant, is a poor substrate for MPST and is unlikely to function as a thiophilic acceptor.	Acetylcysteine	18-34	mercaptopyruvate sulfurtransferase	Homo sapiens	87-91
32179647-8	2020	Kinetic simulations at physiologically-relevant substrate concentrations predicted that the proportion of sulfur transfer to thioredoxin increases ~3.5-fold as its concentration decreases from 10 to 1 mum, whereas the total MPST reaction rate increases ~7-fold.	Sulfur	106-112	mercaptopyruvate sulfurtransferase	Homo sapiens	224-228
32179647-9	2020	The simulations also predicted that cysteine is a quantitatively-significant sulfane sulfur acceptor, revealing MPST"s potential to generate low-molecular-weight persulfides.	Cysteine	36-44	mercaptopyruvate sulfurtransferase	Homo sapiens	112-116
32179647-9	2020	The simulations also predicted that cysteine is a quantitatively-significant sulfane sulfur acceptor, revealing MPST"s potential to generate low-molecular-weight persulfides.	Hydrogen Sulfide	77-84	mercaptopyruvate sulfurtransferase	Homo sapiens	112-116
32179647-9	2020	The simulations also predicted that cysteine is a quantitatively-significant sulfane sulfur acceptor, revealing MPST"s potential to generate low-molecular-weight persulfides.	Sulfur	85-91	mercaptopyruvate sulfurtransferase	Homo sapiens	112-116
32179647-9	2020	The simulations also predicted that cysteine is a quantitatively-significant sulfane sulfur acceptor, revealing MPST"s potential to generate low-molecular-weight persulfides.	low-molecular-weight persulfides	141-173	mercaptopyruvate sulfurtransferase	Homo sapiens	112-116
32340322-4	2020	The current study explored the possibility that a second H2S-producing enzyme, 3-mercaptopyruvate sulfurtransferase (3-MST), may also contribute to the development of functional deficits of Down syndrome cells.	Deuterium	57-60	mercaptopyruvate sulfurtransferase	Homo sapiens	79-115
30500457-5	2020	However, until recently, less attention has been paid to the third enzymatic source of H2S, 3-mercaptopyruvate sulfurtransferase (3-MST), even though several of its biological and biochemical features - e.g. its partial mitochondrial localization, its ability to produce polysulfides, which, in turn, can induce functionally relevant posttranslational protein modifications - makes it a potential candidate.	Hydrogen Sulfide	87-90	mercaptopyruvate sulfurtransferase	Homo sapiens	130-135
30500457-5	2020	However, until recently, less attention has been paid to the third enzymatic source of H2S, 3-mercaptopyruvate sulfurtransferase (3-MST), even though several of its biological and biochemical features - e.g. its partial mitochondrial localization, its ability to produce polysulfides, which, in turn, can induce functionally relevant posttranslational protein modifications - makes it a potential candidate.	polysulfide	271-283	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
30500457-5	2020	However, until recently, less attention has been paid to the third enzymatic source of H2S, 3-mercaptopyruvate sulfurtransferase (3-MST), even though several of its biological and biochemical features - e.g. its partial mitochondrial localization, its ability to produce polysulfides, which, in turn, can induce functionally relevant posttranslational protein modifications - makes it a potential candidate.	polysulfide	271-283	mercaptopyruvate sulfurtransferase	Homo sapiens	130-135
30500457-9	2020	Emerging data with newly discovered pharmacological inhibitors of 3-MST, as well as data using 3-MST silencing approaches suggest that the 3-MST/H2S system plays a role in maintaining cancer cell proliferation; it may also regulate bioenergetic and cell-signaling functions.	Hydrogen Sulfide	145-148	mercaptopyruvate sulfurtransferase	Homo sapiens	66-71
30500457-9	2020	Emerging data with newly discovered pharmacological inhibitors of 3-MST, as well as data using 3-MST silencing approaches suggest that the 3-MST/H2S system plays a role in maintaining cancer cell proliferation; it may also regulate bioenergetic and cell-signaling functions.	Hydrogen Sulfide	145-148	mercaptopyruvate sulfurtransferase	Homo sapiens	95-100
30500457-9	2020	Emerging data with newly discovered pharmacological inhibitors of 3-MST, as well as data using 3-MST silencing approaches suggest that the 3-MST/H2S system plays a role in maintaining cancer cell proliferation; it may also regulate bioenergetic and cell-signaling functions.	Hydrogen Sulfide	145-148	mercaptopyruvate sulfurtransferase	Homo sapiens	95-100
30500457-0	2020	Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.	Hydrogen Sulfide	67-83	mercaptopyruvate sulfurtransferase	Homo sapiens	60-65
30500457-0	2020	Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.	Hydrogen Sulfide	85-88	mercaptopyruvate sulfurtransferase	Homo sapiens	22-58
32041330-0	2020	Effect of S-Allyl -L-Cysteine on MCF-7 Cell Line 3-Mercaptopyruvate Sulfurtransferase/Sulfane Sulfur System, Viability and Apoptosis.	S-allylcysteine	10-29	mercaptopyruvate sulfurtransferase	Homo sapiens	51-85
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	Deuterium	120-123	mercaptopyruvate sulfurtransferase	Homo sapiens	62-96
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	Deuterium	120-123	mercaptopyruvate sulfurtransferase	Homo sapiens	98-102
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Cysteine	59-69	mercaptopyruvate sulfurtransferase	Homo sapiens	268-304
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	sulfane sulfur	124-138	mercaptopyruvate sulfurtransferase	Homo sapiens	62-96
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	sulfane sulfur	124-138	mercaptopyruvate sulfurtransferase	Homo sapiens	98-102
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	Cysteine	165-175	mercaptopyruvate sulfurtransferase	Homo sapiens	62-96
32041330-2	2020	-Cystathionase (CTH), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (MPST) are involved in H2S/sulfane sulfur endogenous formation from L-cysteine.	Cysteine	165-175	mercaptopyruvate sulfurtransferase	Homo sapiens	98-102
32041330-13	2020	Significant decrease in MPST activity at 2245 microM SAC after 24 h and 48 h incubation vs. 1000 microM SAC was associated with decrease in sulfane sulfur levels.	sulfane sulfur	140-154	mercaptopyruvate sulfurtransferase	Homo sapiens	24-28
30644090-3	2020	To date, very little is known about the regulatory role of 3-mercaptopyruvate sulfurtransferase (3-MST), an important H2 S-producing enzyme in ECs.	Hydrogen Sulfide	118-122	mercaptopyruvate sulfurtransferase	Homo sapiens	59-95
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	polysulfide	73-85	mercaptopyruvate sulfurtransferase	Homo sapiens	121-157
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	polysulfide	73-85	mercaptopyruvate sulfurtransferase	Homo sapiens	159-163
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	h2 sn	87-92	mercaptopyruvate sulfurtransferase	Homo sapiens	121-157
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	h2 sn	87-92	mercaptopyruvate sulfurtransferase	Homo sapiens	159-163
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	Hydrogen Sulfide	87-91	mercaptopyruvate sulfurtransferase	Homo sapiens	121-157
30657595-2	2020	Some of these functions have recently been ascribed to its oxidized form polysulfides (H2 Sn ), which can be produced by 3-mercaptopyruvate sulfurtransferase (MPST), also known as a H2 S-producing enzyme.	Hydrogen Sulfide	87-91	mercaptopyruvate sulfurtransferase	Homo sapiens	159-163
30657595-6	2020	MPST also produces redox regulators cysteine persulfide (CysSSH), GSH persulfide (GSSH), and persulfurated proteins.	cysteine persulfide	36-55	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
30657595-6	2020	MPST also produces redox regulators cysteine persulfide (CysSSH), GSH persulfide (GSSH), and persulfurated proteins.	cysssh	57-63	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
30657595-6	2020	MPST also produces redox regulators cysteine persulfide (CysSSH), GSH persulfide (GSSH), and persulfurated proteins.	gsh persulfide	66-80	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	hydrogen sulfite	22-25	mercaptopyruvate sulfurtransferase	Homo sapiens	268-304
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	hydrogen sulfite	22-25	mercaptopyruvate sulfurtransferase	Homo sapiens	306-310
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Cysteine	59-69	mercaptopyruvate sulfurtransferase	Homo sapiens	306-310
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Pyridoxal Phosphate	115-134	mercaptopyruvate sulfurtransferase	Homo sapiens	268-304
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Pyridoxal Phosphate	115-134	mercaptopyruvate sulfurtransferase	Homo sapiens	306-310
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Cysteine	61-69	mercaptopyruvate sulfurtransferase	Homo sapiens	268-304
31893496-2	2019	In mammalian tissues, H2S is synthesized endogenously from L-cysteine in regulated enzymatic pathways catalyzed by pyridoxal phosphate-dependent enzymes: cystathionine beta - synthase (CBS), gamma - cystathionase (CTH) and cysteine aminotransferase (CAT) coupled with 3-mercaptopyruvate sulfurtransferase (MPST).	Cysteine	61-69	mercaptopyruvate sulfurtransferase	Homo sapiens	306-310
31634482-4	2019	We have found that expression and activity of 3-mercaptopyruvate sulfurtransferase (MPST), one of three enzymes that hat regulates H2S biosynthesis, is significantly lower in MSC as compared with lineage-restricted dermal fibroblasts.	Deuterium	131-134	mercaptopyruvate sulfurtransferase	Homo sapiens	46-82
31634482-4	2019	We have found that expression and activity of 3-mercaptopyruvate sulfurtransferase (MPST), one of three enzymes that hat regulates H2S biosynthesis, is significantly lower in MSC as compared with lineage-restricted dermal fibroblasts.	Deuterium	131-134	mercaptopyruvate sulfurtransferase	Homo sapiens	84-88
31634482-6	2019	Inactivation of MPST with phenylpyruvate (PP) or by siRNA silencing led to diminished H2S production associated with increased production of reactive oxygen species (ROS) and lactic acid.	phenylpyruvic acid	26-40	mercaptopyruvate sulfurtransferase	Homo sapiens	16-20
31634482-6	2019	Inactivation of MPST with phenylpyruvate (PP) or by siRNA silencing led to diminished H2S production associated with increased production of reactive oxygen species (ROS) and lactic acid.	Deuterium	86-89	mercaptopyruvate sulfurtransferase	Homo sapiens	16-20
31634482-6	2019	Inactivation of MPST with phenylpyruvate (PP) or by siRNA silencing led to diminished H2S production associated with increased production of reactive oxygen species (ROS) and lactic acid.	Reactive Oxygen Species	141-164	mercaptopyruvate sulfurtransferase	Homo sapiens	16-20
31634482-6	2019	Inactivation of MPST with phenylpyruvate (PP) or by siRNA silencing led to diminished H2S production associated with increased production of reactive oxygen species (ROS) and lactic acid.	Reactive Oxygen Species	166-169	mercaptopyruvate sulfurtransferase	Homo sapiens	16-20
31634482-6	2019	Inactivation of MPST with phenylpyruvate (PP) or by siRNA silencing led to diminished H2S production associated with increased production of reactive oxygen species (ROS) and lactic acid.	Lactic Acid	175-186	mercaptopyruvate sulfurtransferase	Homo sapiens	16-20
31634482-8	2019	Suppression of TET1 gene and inhibition of glycolysis with glucose analog, 2-desoxy-d-glucose, or hexokinase II inhibitor significantly reduced expression of pluripotency genes following MPST inactivation or knockdown.	Glucose	59-66	mercaptopyruvate sulfurtransferase	Homo sapiens	187-191
31634482-8	2019	Suppression of TET1 gene and inhibition of glycolysis with glucose analog, 2-desoxy-d-glucose, or hexokinase II inhibitor significantly reduced expression of pluripotency genes following MPST inactivation or knockdown.	Glucose	86-93	mercaptopyruvate sulfurtransferase	Homo sapiens	187-191
31634482-9	2019	MPST disruption promoted the conversion of fibroblasts into adipocytes as evidenced by a significant increase in expression of adipocyte-specific genes, PPARgamma, and UCP1, and intracellular accumulation of oil Red-O positive fat droplets.	oil red O	208-217	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
31449969-6	2019	RESULTS: Proteomic analysis of fibroblasts identified upregulation of multiple proteins involved in serine synthesis and thiol metabolism including: phosphoserine amino transferase (PSAT1), cystathionine beta synthase (CBS), and mercaptopyruvate sulfurtransferase (MPST).	Serine	100-106	mercaptopyruvate sulfurtransferase	Homo sapiens	229-263
31449969-6	2019	RESULTS: Proteomic analysis of fibroblasts identified upregulation of multiple proteins involved in serine synthesis and thiol metabolism including: phosphoserine amino transferase (PSAT1), cystathionine beta synthase (CBS), and mercaptopyruvate sulfurtransferase (MPST).	Serine	100-106	mercaptopyruvate sulfurtransferase	Homo sapiens	265-269
31382676-0	2019	N-Acetylcysteine Serves as Substrate of 3-Mercaptopyruvate Sulfurtransferase and Stimulates Sulfide Metabolism in Colon Cancer Cells.	Acetylcysteine	0-16	mercaptopyruvate sulfurtransferase	Homo sapiens	40-76
31443288-6	2019	Pre-treatment of H2S also decreased H2O2-induced suppression of endogenous H2S production enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercapto-pyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	17-20	mercaptopyruvate sulfurtransferase	Homo sapiens	171-208
31443288-6	2019	Pre-treatment of H2S also decreased H2O2-induced suppression of endogenous H2S production enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercapto-pyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	17-20	mercaptopyruvate sulfurtransferase	Homo sapiens	210-214
31443288-6	2019	Pre-treatment of H2S also decreased H2O2-induced suppression of endogenous H2S production enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercapto-pyruvate sulfurtransferase (MPST).	Hydrogen Peroxide	36-40	mercaptopyruvate sulfurtransferase	Homo sapiens	171-208
31443288-6	2019	Pre-treatment of H2S also decreased H2O2-induced suppression of endogenous H2S production enzymes, cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE), and 3-mercapto-pyruvate sulfurtransferase (MPST).	Hydrogen Peroxide	36-40	mercaptopyruvate sulfurtransferase	Homo sapiens	210-214
31382676-2	2019	The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects.	Deuterium	247-250	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
31382676-2	2019	The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects.	sulfane sulfur	261-275	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
31382676-2	2019	The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects.	persulfides	292-303	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
31382676-2	2019	The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects.	polysulfide	308-320	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
31382676-2	2019	The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), besides being respectively involved in the synthesis and catabolism of H2S, generate sulfane sulfur species such as persulfides and polysulfides, currently recognized as mediating some of the H2S biological effects.	Deuterium	368-371	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
30862476-3	2019	Therefore we assessed the expressional kinetics of potential H2S-producing enzymes during undisturbed skin repair: the cystathionine-gamma-lyase (CSE), the cystathionine-beta-synthase (CBS) and the 3-mercaptopyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	61-64	mercaptopyruvate sulfurtransferase	Homo sapiens	236-240
29790379-3	2019	Recent Advances: The three H2S-producing enzymes, namely cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (3MST), have been found to be highly expressed in numerous types of cancer.	Hydrogen Sulfide	27-30	mercaptopyruvate sulfurtransferase	Homo sapiens	129-165
30928641-2	2019	Multiple enzymes such as cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) and 3-Mercaptopyruvate sulfurtransferase (MST) produce endogenous H2S, and these are differentially expressed in the various tissue systems including the skeletal system.	Hydrogen Sulfide	158-161	mercaptopyruvate sulfurtransferase	Homo sapiens	96-132
30849397-3	2019	Cystathionine beta-synthetase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) are known as H2S-producing enzymes.	Hydrogen Sulfide	131-134	mercaptopyruvate sulfurtransferase	Homo sapiens	74-110
30862476-3	2019	Therefore we assessed the expressional kinetics of potential H2S-producing enzymes during undisturbed skin repair: the cystathionine-gamma-lyase (CSE), the cystathionine-beta-synthase (CBS) and the 3-mercaptopyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	61-64	mercaptopyruvate sulfurtransferase	Homo sapiens	198-234
31527361-0	2019	[Development of fluorescent probes for detecting reactive sulfur species and their application to development of inhibitors for 3MST].	reactive sulfur species	49-72	mercaptopyruvate sulfurtransferase	Homo sapiens	129-132
30679627-1	2019	Biosynthesis of hydrogen sulfide (H2S), a key signalling molecule in human (patho)physiology, is mostly accomplished by the human enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	16-32	mercaptopyruvate sulfurtransferase	Homo sapiens	209-245
30679627-1	2019	Biosynthesis of hydrogen sulfide (H2S), a key signalling molecule in human (patho)physiology, is mostly accomplished by the human enzymes cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	34-37	mercaptopyruvate sulfurtransferase	Homo sapiens	209-245
31527361-9	2019	Further, we applied HSip-1 to the high-throughput screening (HTS) for the inhibitors of 3-mercaptopyruvate sulfurtransferase (3MST), one of the reactive sulfur species (RSS)-generating enzymes.	RSS	169-172	mercaptopyruvate sulfurtransferase	Homo sapiens	88-124
28877979-0	2018	Fatty acids promote fatty liver disease via the dysregulation of 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway.	Fatty Acids	0-11	mercaptopyruvate sulfurtransferase	Homo sapiens	65-101
28877979-0	2018	Fatty acids promote fatty liver disease via the dysregulation of 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway.	Hydrogen Sulfide	102-118	mercaptopyruvate sulfurtransferase	Homo sapiens	65-101
28877979-9	2018	Intriguingly, inhibition of MPST significantly enhanced rather than decreased H2S production, whereas MPST overexpression markedly inhibited H2S production.	Hydrogen Sulfide	78-81	mercaptopyruvate sulfurtransferase	Homo sapiens	28-32
28877979-2	2018	This study aimed to investigate the underlying mechanisms by which FFA contributes to the pathogenesis of NAFLD via the regulation of 3-mercaptopyruvate sulfurtransferase (MPST), a key enzyme that regulates endogenous hydrogen sulfide (H2S) biosynthesis.	Hydrogen Sulfide	218-234	mercaptopyruvate sulfurtransferase	Homo sapiens	134-170
28877979-9	2018	Intriguingly, inhibition of MPST significantly enhanced rather than decreased H2S production, whereas MPST overexpression markedly inhibited H2S production.	Hydrogen Sulfide	141-144	mercaptopyruvate sulfurtransferase	Homo sapiens	102-106
28877979-10	2018	Co-immunoprecipitation experiments showed that MPST directly interacted with and negatively regulated cystathionine gamma-lyase (CSE), a major source of H2S production in the liver.	Hydrogen Sulfide	153-156	mercaptopyruvate sulfurtransferase	Homo sapiens	47-51
28877979-2	2018	This study aimed to investigate the underlying mechanisms by which FFA contributes to the pathogenesis of NAFLD via the regulation of 3-mercaptopyruvate sulfurtransferase (MPST), a key enzyme that regulates endogenous hydrogen sulfide (H2S) biosynthesis.	Hydrogen Sulfide	218-234	mercaptopyruvate sulfurtransferase	Homo sapiens	172-176
28877979-11	2018	Mechanistically, MPST promoted steatosis via inhibition of CSE/H2S and subsequent upregulation of the sterol regulatory element-binding protein 1c pathway, C-Jun N-terminal kinase phosphorylation and hepatic oxidative stress.	Hydrogen Sulfide	63-66	mercaptopyruvate sulfurtransferase	Homo sapiens	17-21
28877979-2	2018	This study aimed to investigate the underlying mechanisms by which FFA contributes to the pathogenesis of NAFLD via the regulation of 3-mercaptopyruvate sulfurtransferase (MPST), a key enzyme that regulates endogenous hydrogen sulfide (H2S) biosynthesis.	Hydrogen Sulfide	236-239	mercaptopyruvate sulfurtransferase	Homo sapiens	134-170
28877979-2	2018	This study aimed to investigate the underlying mechanisms by which FFA contributes to the pathogenesis of NAFLD via the regulation of 3-mercaptopyruvate sulfurtransferase (MPST), a key enzyme that regulates endogenous hydrogen sulfide (H2S) biosynthesis.	Hydrogen Sulfide	236-239	mercaptopyruvate sulfurtransferase	Homo sapiens	172-176
30274149-2	2018	Three enzymes mediate the endogenous production of H2S: cystathione beta-synthase (CBS), cystathione gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST).	Hydrogen Sulfide	51-54	mercaptopyruvate sulfurtransferase	Homo sapiens	123-159
30283315-4	2018	Since recent studies have demonstrated that several human tumors overexpress the hydrogen sulfide (H2S)-synthesizing enzymes cystathionine-beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST), and also show dysregulated H2S levels, we examined these biomarkers in the oral ACC and compared the results to those of adjacent benign oral epithelium.	Hydrogen Sulfide	81-97	mercaptopyruvate sulfurtransferase	Homo sapiens	197-233
30283315-4	2018	Since recent studies have demonstrated that several human tumors overexpress the hydrogen sulfide (H2S)-synthesizing enzymes cystathionine-beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST), and also show dysregulated H2S levels, we examined these biomarkers in the oral ACC and compared the results to those of adjacent benign oral epithelium.	Hydrogen Sulfide	81-97	mercaptopyruvate sulfurtransferase	Homo sapiens	235-240
30283315-4	2018	Since recent studies have demonstrated that several human tumors overexpress the hydrogen sulfide (H2S)-synthesizing enzymes cystathionine-beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST), and also show dysregulated H2S levels, we examined these biomarkers in the oral ACC and compared the results to those of adjacent benign oral epithelium.	Hydrogen Sulfide	99-102	mercaptopyruvate sulfurtransferase	Homo sapiens	197-233
30283315-4	2018	Since recent studies have demonstrated that several human tumors overexpress the hydrogen sulfide (H2S)-synthesizing enzymes cystathionine-beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST), and also show dysregulated H2S levels, we examined these biomarkers in the oral ACC and compared the results to those of adjacent benign oral epithelium.	Hydrogen Sulfide	99-102	mercaptopyruvate sulfurtransferase	Homo sapiens	235-240
29793450-1	2018	BACKGROUND: Knowledge about the expression and thus a role of enzymes that produce endogenous H2S - cystathionine-beta-synthase, cystathionine gamma-lyase and mercaptopyruvate sulfurtransferase - in renal tumors is still controversial.	Hydrogen Sulfide	94-97	mercaptopyruvate sulfurtransferase	Homo sapiens	159-193
29928321-1	2018	H2S, synthesized by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST), functions as a signalling molecule in mammalian cells.	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	91-127
29928321-1	2018	H2S, synthesized by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST), functions as a signalling molecule in mammalian cells.	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	129-133
29779029-11	2018	The mRNA levels of cystathionine beta-synthase and cystathionine gamma-lyase, 2 catalytic enzymes of H2S formation, were significantly lower in blood mononuclear cells of CKD patients with respect to controls; however, the mRNA level of 3-mercaptopyruvate sulfurtransferase, as another H2S-producing enzyme, was significantly higher in CKD patients.	Deuterium	101-104	mercaptopyruvate sulfurtransferase	Homo sapiens	237-273
29429900-5	2018	We provide evidence suggesting the possibility that sulfane sulfur species produced by 3-mercaptopyruvate sulfurtransferase and sulfide:quinone oxidoreductase are the actual mediators of the immediate antioxidative and cytoprotective effects provided by NAC.	sulfane sulfur	52-66	mercaptopyruvate sulfurtransferase	Homo sapiens	87-123
29429900-5	2018	We provide evidence suggesting the possibility that sulfane sulfur species produced by 3-mercaptopyruvate sulfurtransferase and sulfide:quinone oxidoreductase are the actual mediators of the immediate antioxidative and cytoprotective effects provided by NAC.	Acetylcysteine	254-257	mercaptopyruvate sulfurtransferase	Homo sapiens	87-123
29507650-2	2018	H2S is produced from cysteine by enzymes, such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), cysteine aminotransferase (CAT), and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	155-191
29507650-2	2018	H2S is produced from cysteine by enzymes, such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), cysteine aminotransferase (CAT), and 3-mercaptopyruvate sulfurtransferase (3MST).	Cysteine	21-29	mercaptopyruvate sulfurtransferase	Homo sapiens	155-191
29452248-1	2018	Hydrogen sulfide (H2S) is produced by the action of cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) or 3-mercaptopyruvate sulfurtransferase (3-MST).	Hydrogen Sulfide	0-16	mercaptopyruvate sulfurtransferase	Homo sapiens	122-158
29452248-1	2018	Hydrogen sulfide (H2S) is produced by the action of cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) or 3-mercaptopyruvate sulfurtransferase (3-MST).	Hydrogen Sulfide	18-21	mercaptopyruvate sulfurtransferase	Homo sapiens	122-158
29061341-8	2018	Two major H2S-generating enzymes, cystathionine-beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST) were upregulated in the 5-FU-resistant cells.	Hydrogen Sulfide	10-13	mercaptopyruvate sulfurtransferase	Homo sapiens	72-108
28558483-2	2017	Recently, hydrogen polysulfides (H2Sn) have been found to be produced by 3-mercaptopyruvate sulfurtransferase and to regulate the activity of ion channels, tumor suppressers, and protein kinases.	hydrogen polysulfides	10-31	mercaptopyruvate sulfurtransferase	Homo sapiens	73-109
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	Hydrogen Sulfide	57-60	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	3-mercaptopyruvic acid	97-115	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	3-mercaptopyruvic acid	117-120	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	Cysteine	139-149	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	Ketoglutaric Acids	154-173	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
30393252-3	2018	3-Mercaptopyruvate sulfurtransferase (3MST) is the third H2S-producing enzyme, and its substrate 3-mercaptopyruvate (3MP) is provided from l-cysteine and alpha-ketoglutarate (alpha-KG) by a PLP-dependent cysteine aminotransferase (CAT).	Ketoglutaric Acids	175-183	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
28481637-4	2017	The generation of H2S is catalyzed by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3-MST).	Hydrogen Sulfide	18-21	mercaptopyruvate sulfurtransferase	Homo sapiens	110-146
30393252-0	2018	[Production of H2S, H2Sn, and persulfide species (CysSSH and GSSH) by 3-mercaptopyruvate sulfurtransferase].	Hydrogen Sulfide	15-18	mercaptopyruvate sulfurtransferase	Homo sapiens	70-106
30393252-0	2018	[Production of H2S, H2Sn, and persulfide species (CysSSH and GSSH) by 3-mercaptopyruvate sulfurtransferase].	h2sn	20-24	mercaptopyruvate sulfurtransferase	Homo sapiens	70-106
30393252-0	2018	[Production of H2S, H2Sn, and persulfide species (CysSSH and GSSH) by 3-mercaptopyruvate sulfurtransferase].	persulfides	30-40	mercaptopyruvate sulfurtransferase	Homo sapiens	70-106
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Hydrogen Sulfide	165-172	mercaptopyruvate sulfurtransferase	Homo sapiens	82-118
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Hydrogen Sulfide	165-172	mercaptopyruvate sulfurtransferase	Homo sapiens	120-124
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Sulfur	101-107	mercaptopyruvate sulfurtransferase	Homo sapiens	120-124
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Hydrogen Sulfide	165-172	mercaptopyruvate sulfurtransferase	Homo sapiens	82-118
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Hydrogen Sulfide	165-172	mercaptopyruvate sulfurtransferase	Homo sapiens	120-124
28852876-4	2017	In U87MG cells, an increased level of sulfane sulfur and an increased activity of 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese, the enzymes involved in sulfane sulfur generation and transfer, suggest that DATS can function as a donor of sulfane sulfur atom, transferred by sulfurtransferases, to sulfhydryl groups of cysteine residues of Bcl-2 and in this way lower the level of active form of Bcl-2 by S-sulfuration.	Sulfur	101-107	mercaptopyruvate sulfurtransferase	Homo sapiens	120-124
28852876-6	2017	MPST and rhodanese, the level of which is increased in the presence of DATS, can serve as antioxidant proteins.	diallyl trisulfide	71-75	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
28558483-2	2017	Recently, hydrogen polysulfides (H2Sn) have been found to be produced by 3-mercaptopyruvate sulfurtransferase and to regulate the activity of ion channels, tumor suppressers, and protein kinases.	h2sn	33-37	mercaptopyruvate sulfurtransferase	Homo sapiens	73-109
28979207-5	2017	RNA interference was used to block the endogenous generation of hydrogen sulfide by CSE, CBS, or MPST in a vascular endothelial cell migration model in both normoxia and hypoxia.	Hydrogen Sulfide	64-80	mercaptopyruvate sulfurtransferase	Homo sapiens	97-101
28412453-5	2017	Here, we compared the specific activities of mercaptopyruvate sulfurtransferase (MST, required for sulfanegen"s activity), across common laboratory models of cyanide intoxication, and humans.	Cyanides	158-165	mercaptopyruvate sulfurtransferase	Homo sapiens	45-79
28552745-7	2017	The CSE inhibitor dl-propargylglycine (PPG) and aspartate (limits MPST) had no effect alone, but when applied together with AOAA the hypoxic relaxation response was further reduced.	Aspartic Acid	48-57	mercaptopyruvate sulfurtransferase	Homo sapiens	66-70
28804545-2	2017	Recently, hydrogen sulfide (H2S), a gaseous transmitter endogenously generated by cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST), is found to improve mitochondrial function.	Hydrogen Sulfide	10-26	mercaptopyruvate sulfurtransferase	Homo sapiens	153-189
28804545-2	2017	Recently, hydrogen sulfide (H2S), a gaseous transmitter endogenously generated by cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST), is found to improve mitochondrial function.	Hydrogen Sulfide	28-31	mercaptopyruvate sulfurtransferase	Homo sapiens	153-189
29927219-2	2017	Adipocyte endogenously produces H2S by cystathionine beta synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).The endogenous H2S in adipocyte plays an essential role in glucose uptake activity and utilization, lipolysis and adipocyte differentiation, and then takes part in the pathogenesis of obesity, diabetes and cardiovascular diseases.H2S regulates adipocyte energy metabolism by activation activating insulin receptor, peroxisome proliferator activated receptor gamma (PPARgamma) or potassium channel.	Hydrogen Sulfide	32-35	mercaptopyruvate sulfurtransferase	Homo sapiens	148-152
29927219-2	2017	Adipocyte endogenously produces H2S by cystathionine beta synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).The endogenous H2S in adipocyte plays an essential role in glucose uptake activity and utilization, lipolysis and adipocyte differentiation, and then takes part in the pathogenesis of obesity, diabetes and cardiovascular diseases.H2S regulates adipocyte energy metabolism by activation activating insulin receptor, peroxisome proliferator activated receptor gamma (PPARgamma) or potassium channel.	Hydrogen Sulfide	169-172	mercaptopyruvate sulfurtransferase	Homo sapiens	148-152
29927219-2	2017	Adipocyte endogenously produces H2S by cystathionine beta synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).The endogenous H2S in adipocyte plays an essential role in glucose uptake activity and utilization, lipolysis and adipocyte differentiation, and then takes part in the pathogenesis of obesity, diabetes and cardiovascular diseases.H2S regulates adipocyte energy metabolism by activation activating insulin receptor, peroxisome proliferator activated receptor gamma (PPARgamma) or potassium channel.	Glucose	213-220	mercaptopyruvate sulfurtransferase	Homo sapiens	148-152
29927219-2	2017	Adipocyte endogenously produces H2S by cystathionine beta synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).The endogenous H2S in adipocyte plays an essential role in glucose uptake activity and utilization, lipolysis and adipocyte differentiation, and then takes part in the pathogenesis of obesity, diabetes and cardiovascular diseases.H2S regulates adipocyte energy metabolism by activation activating insulin receptor, peroxisome proliferator activated receptor gamma (PPARgamma) or potassium channel.	Hydrogen Sulfide	169-172	mercaptopyruvate sulfurtransferase	Homo sapiens	148-152
28291844-2	2017	The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system.	Hydrogen Sulfide	71-74	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
28079151-0	2017	Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide.	Hydrogen Sulfide	70-73	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
28079151-0	2017	Discovery and Mechanistic Characterization of Selective Inhibitors of H2S-producing Enzyme: 3-Mercaptopyruvate Sulfurtransferase (3MST) Targeting Active-site Cysteine Persulfide.	cysteine persulfide	158-177	mercaptopyruvate sulfurtransferase	Homo sapiens	92-128
28079151-2	2017	3-Mercaptopyruvate sulfurtransferase (3MST), one of three H2S-producing enzymes, was also recently shown to produce sulfane sulfur (H2Sn).	Hydrogen Sulfide	58-61	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
28079151-2	2017	3-Mercaptopyruvate sulfurtransferase (3MST), one of three H2S-producing enzymes, was also recently shown to produce sulfane sulfur (H2Sn).	sulfane sulfur	116-130	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
28079151-2	2017	3-Mercaptopyruvate sulfurtransferase (3MST), one of three H2S-producing enzymes, was also recently shown to produce sulfane sulfur (H2Sn).	h2sn	132-136	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
28291844-2	2017	The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system.	Hydrogen Sulfide	71-74	mercaptopyruvate sulfurtransferase	Homo sapiens	50-54
28291844-2	2017	The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system.	3-Chloro-4-methylaniline hydrochloride	149-152	mercaptopyruvate sulfurtransferase	Homo sapiens	12-48
28291844-2	2017	The role of 3-mercaptopyruvate sulfurtransferase (MPST, EC 2.8.1.2) in H2S generation is also considered; it could be important for tissues with low CTH activity, e.g. cells of the nervous system.	3-Chloro-4-methylaniline hydrochloride	149-152	mercaptopyruvate sulfurtransferase	Homo sapiens	50-54
28291844-4	2017	In both cell lines, the expression and activity of MPST were the highest among the investigated enzymes, suggesting its possible role in the generation of H2S.	Hydrogen Sulfide	155-158	mercaptopyruvate sulfurtransferase	Homo sapiens	51-55
28291844-7	2017	The higher expression and activity of CBS, CTH and MPST in the neuroblastoma cells were associated with more intensive generation of H2S in the presence of 2 mM cysteine.	Hydrogen Sulfide	133-136	mercaptopyruvate sulfurtransferase	Homo sapiens	51-55
28291844-7	2017	The higher expression and activity of CBS, CTH and MPST in the neuroblastoma cells were associated with more intensive generation of H2S in the presence of 2 mM cysteine.	Cysteine	161-169	mercaptopyruvate sulfurtransferase	Homo sapiens	51-55
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	Hydrogen Sulfide	97-113	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	Hydrogen Sulfide	97-113	mercaptopyruvate sulfurtransferase	Homo sapiens	38-41
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	Hydrogen Sulfide	97-113	mercaptopyruvate sulfurtransferase	Homo sapiens	211-214
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	polysulfide	118-130	mercaptopyruvate sulfurtransferase	Homo sapiens	0-36
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	polysulfide	118-130	mercaptopyruvate sulfurtransferase	Homo sapiens	38-41
27973427-1	2016	3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST.	polysulfide	118-130	mercaptopyruvate sulfurtransferase	Homo sapiens	211-214
27440715-9	2016	Pretreatment with the cystathionine-gamma-lyase inhibitor d/l-propargylglycine (PAG) decreased hypoxic inhibition of sodium transport by H441 monolayers, whereas inhibition of cystathionine-beta-synthase (with aminooxy-acetic acid; AOAA) or 3-mercaptopyruvate sulfurtransferase (with aspartate) had no effect.	Deuterium	58-59	mercaptopyruvate sulfurtransferase	Homo sapiens	241-277
27808278-2	2016	Here we show that human lung adenocarcinoma tissue expresses high levels of hydrogen sulfide (H2S) producing enzymes, namely, cystathionine beta-synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST), in comparison to adjacent lung tissue.	Hydrogen Sulfide	76-92	mercaptopyruvate sulfurtransferase	Homo sapiens	197-233
27808278-2	2016	Here we show that human lung adenocarcinoma tissue expresses high levels of hydrogen sulfide (H2S) producing enzymes, namely, cystathionine beta-synthase (CBS), cystathionine gamma lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST), in comparison to adjacent lung tissue.	Hydrogen Sulfide	94-97	mercaptopyruvate sulfurtransferase	Homo sapiens	197-233
27440715-9	2016	Pretreatment with the cystathionine-gamma-lyase inhibitor d/l-propargylglycine (PAG) decreased hypoxic inhibition of sodium transport by H441 monolayers, whereas inhibition of cystathionine-beta-synthase (with aminooxy-acetic acid; AOAA) or 3-mercaptopyruvate sulfurtransferase (with aspartate) had no effect.	propargylglycine	60-78	mercaptopyruvate sulfurtransferase	Homo sapiens	241-277
27484215-4	2016	H2S n is produced by 3-mercaptopyruvate sulfurtransferase (3MST) from 3-mercaptopyruvate (3MP) and is generated by the chemical interaction of H2S with nitric oxide (NO).	h2s n	0-5	mercaptopyruvate sulfurtransferase	Homo sapiens	21-57
27484215-4	2016	H2S n is produced by 3-mercaptopyruvate sulfurtransferase (3MST) from 3-mercaptopyruvate (3MP) and is generated by the chemical interaction of H2S with nitric oxide (NO).	3-mercaptopyruvic acid	90-93	mercaptopyruvate sulfurtransferase	Homo sapiens	21-57
27484215-4	2016	H2S n is produced by 3-mercaptopyruvate sulfurtransferase (3MST) from 3-mercaptopyruvate (3MP) and is generated by the chemical interaction of H2S with nitric oxide (NO).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	21-57
27484215-4	2016	H2S n is produced by 3-mercaptopyruvate sulfurtransferase (3MST) from 3-mercaptopyruvate (3MP) and is generated by the chemical interaction of H2S with nitric oxide (NO).	Nitric Oxide	152-164	mercaptopyruvate sulfurtransferase	Homo sapiens	21-57
27083071-1	2016	Hydrogen sulfide (H2S) is produced in the mammalian body through the enzymatic activities of cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	0-16	mercaptopyruvate sulfurtransferase	Homo sapiens	164-200
27308865-6	2016	To meet this need, our laboratory is developing sulfanegen, a potential antidote for cyanide poisoning with a novel mechanism based on 3-mercaptopyruvate sulfurtransferase (3-MST) for the detoxification of cyanide.	Sulfanegen	48-58	mercaptopyruvate sulfurtransferase	Homo sapiens	135-171
27308865-6	2016	To meet this need, our laboratory is developing sulfanegen, a potential antidote for cyanide poisoning with a novel mechanism based on 3-mercaptopyruvate sulfurtransferase (3-MST) for the detoxification of cyanide.	Cyanides	206-213	mercaptopyruvate sulfurtransferase	Homo sapiens	135-171
27146345-3	2016	Mercaptopyruvate sulfurtransferase (MST, PDB code: 4JGT ) catalyzes sulfur transfer from mercaptopyruvate to sulfur acceptors, and the first step of the reaction is the formation of cysteine (Cys248) persulfide via S-sulfhydration.	3-mercaptopyruvic acid	89-105	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
27146345-3	2016	Mercaptopyruvate sulfurtransferase (MST, PDB code: 4JGT ) catalyzes sulfur transfer from mercaptopyruvate to sulfur acceptors, and the first step of the reaction is the formation of cysteine (Cys248) persulfide via S-sulfhydration.	Sulfur	68-74	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
27146345-3	2016	Mercaptopyruvate sulfurtransferase (MST, PDB code: 4JGT ) catalyzes sulfur transfer from mercaptopyruvate to sulfur acceptors, and the first step of the reaction is the formation of cysteine (Cys248) persulfide via S-sulfhydration.	Cysteine	182-190	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
27146345-3	2016	Mercaptopyruvate sulfurtransferase (MST, PDB code: 4JGT ) catalyzes sulfur transfer from mercaptopyruvate to sulfur acceptors, and the first step of the reaction is the formation of cysteine (Cys248) persulfide via S-sulfhydration.	persulfides	200-210	mercaptopyruvate sulfurtransferase	Homo sapiens	0-34
27083071-1	2016	Hydrogen sulfide (H2S) is produced in the mammalian body through the enzymatic activities of cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST).	Hydrogen Sulfide	18-21	mercaptopyruvate sulfurtransferase	Homo sapiens	164-200
27440715-9	2016	Pretreatment with the cystathionine-gamma-lyase inhibitor d/l-propargylglycine (PAG) decreased hypoxic inhibition of sodium transport by H441 monolayers, whereas inhibition of cystathionine-beta-synthase (with aminooxy-acetic acid; AOAA) or 3-mercaptopyruvate sulfurtransferase (with aspartate) had no effect.	pag	80-83	mercaptopyruvate sulfurtransferase	Homo sapiens	241-277
27080266-11	2016	Expressions of endogenous H2S and its synthases including CBS, CSE and MPST were present in the cytoplasm of chondrocytes.CSE protein expression in Grade 3 (defined by outerbridge grading) cartilage tissues was significantly increased as compared with that of Grade 1 cartilage tissues (1.67+-0.09 vs. 1.26+-0.11, P< 0.05).	Hydrogen Sulfide	26-29	mercaptopyruvate sulfurtransferase	Homo sapiens	71-75
25822632-3	2015	The expression of the H2S-synthesising enzymes, cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST), was increased in a time-dependent manner during 3T3L1 differentiation.	Hydrogen Sulfide	22-25	mercaptopyruvate sulfurtransferase	Homo sapiens	119-155
26069359-8	2015	Recently, the third enzyme, 3-mercaptopyruvate sulfur transferase, along with cysteine aminotransferase, which is similar to aspartate aminotransferase, has been found to produce H2S in the brain.	Hydrogen Sulfide	179-182	mercaptopyruvate sulfurtransferase	Homo sapiens	28-65
24800864-3	2015	H2S is produced from l-cysteine by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase.	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	107-143
24800864-3	2015	H2S is produced from l-cysteine by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) along with cysteine aminotransferase.	Cysteine	21-31	mercaptopyruvate sulfurtransferase	Homo sapiens	107-143
26162829-3	2015	H2S is produced from L-cysteine by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) together with cysteine aminotransferase (CAT).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	107-143
28785645-4	2015	H2S is produced endogenously through several key enzymes, including cystathionine beta-lyase (CBE), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (MST)/cysteine aminotransferase (CAT).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	137-173
25615598-3	2015	H2S is a gaseous signaling molecule and is produced endogenously by the enzymes cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	151-187
25615598-3	2015	H2S is a gaseous signaling molecule and is produced endogenously by the enzymes cystathionine-beta-synthase (CBS), cystathionine-gamma-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	189-193
25278485-5	2015	The molecular events triggered by Nampt include elevated production of NAD(+) and up-regulation of H2S producing enzymes, cystathionine beta synthase (CBS) and cystathionase (CTH) with 3-mercaptopyruvate sulfurtransferase (MST) being detectable only in 3D spheroids.	Hydrogen Sulfide	99-102	mercaptopyruvate sulfurtransferase	Homo sapiens	185-221
26162829-3	2015	H2S is produced from L-cysteine by cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (3MST) together with cysteine aminotransferase (CAT).	Cysteine	21-31	mercaptopyruvate sulfurtransferase	Homo sapiens	107-143
26078818-2	2015	Three enzymes, cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (MST), are involved in enzymatic production of H2S.	Hydrogen Sulfide	171-174	mercaptopyruvate sulfurtransferase	Homo sapiens	87-123
25123509-2	2015	H2 S is produced from substances by three enzymes: cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	0-4	mercaptopyruvate sulfurtransferase	Homo sapiens	123-159
25123509-11	2015	H2 S is produced from cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), and 3-mercaptopyruvate sulfur transferase (MST).	Hydrogen Sulfide	0-4	mercaptopyruvate sulfurtransferase	Homo sapiens	94-131
25725525-1	2015	A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide.	Cystine	2-9	mercaptopyruvate sulfurtransferase	Homo sapiens	31-67
25725525-1	2015	A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide.	Thiosulfates	132-143	mercaptopyruvate sulfurtransferase	Homo sapiens	31-67
25725525-1	2015	A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide.	Sulfhydryl Compounds	147-152	mercaptopyruvate sulfurtransferase	Homo sapiens	31-67
25725525-1	2015	A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide.	Cyanides	177-184	mercaptopyruvate sulfurtransferase	Homo sapiens	31-67
25205294-2	2015	A third enzyme, 3-mercaptopyruvate sulfurtransferase (3-MST), synthesizes H2 S in the presence of the substrate 3-mercaptopyruvate (3-MP).	Hydrogen Sulfide	74-78	mercaptopyruvate sulfurtransferase	Homo sapiens	16-52
25532835-4	2014	The activity of 3-mercaptopyruvate sulfurtransferase was the highest in the thalamus, hypothalamus and subcortical nuclei and essentially the same level of sulfane sulfur was found in all the investigated brain regions.	sulfane sulfur	156-170	mercaptopyruvate sulfurtransferase	Homo sapiens	16-52
25532835-5	2014	The investigations demonstrated that the level of sulfane sulfur in gliomas with the highest grades was high in comparison to various human brain regions, and was correlated with a decreased activity of gamma-cystathionase, 3-mercaptopyruvate sulfurtransferase and rhodanese.	Hydrogen Sulfide	50-57	mercaptopyruvate sulfurtransferase	Homo sapiens	224-260
25532835-5	2014	The investigations demonstrated that the level of sulfane sulfur in gliomas with the highest grades was high in comparison to various human brain regions, and was correlated with a decreased activity of gamma-cystathionase, 3-mercaptopyruvate sulfurtransferase and rhodanese.	Sulfur	58-64	mercaptopyruvate sulfurtransferase	Homo sapiens	224-260
25532835-9	2014	Because of the disappearance of gamma-cystathionase activity in high-grade gliomas, it seems to be possible that 3-mercaptopyruvate sulfurtransferase could participate in hydrogen sulfide production.	Hydrogen Sulfide	171-187	mercaptopyruvate sulfurtransferase	Homo sapiens	113-149
25336638-1	2014	The human tRNA thiouridine modification protein (TUM1), also designated as 3-mercaptopyruvate sulfurtransferase (MPST), has been implicated in a wide range of physiological processes in the cell.	Thiouridine	15-26	mercaptopyruvate sulfurtransferase	Homo sapiens	49-53
25336638-1	2014	The human tRNA thiouridine modification protein (TUM1), also designated as 3-mercaptopyruvate sulfurtransferase (MPST), has been implicated in a wide range of physiological processes in the cell.	Thiouridine	15-26	mercaptopyruvate sulfurtransferase	Homo sapiens	75-111
25336638-1	2014	The human tRNA thiouridine modification protein (TUM1), also designated as 3-mercaptopyruvate sulfurtransferase (MPST), has been implicated in a wide range of physiological processes in the cell.	Thiouridine	15-26	mercaptopyruvate sulfurtransferase	Homo sapiens	113-117
25336638-3	2014	TUM1 is a member of the sulfurtransferase family and catalyzes the conversion of 3-mercaptopyruvate to pyruvate and protein-bound persulfide.	3-mercaptopyruvic acid	81-99	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
25336638-3	2014	TUM1 is a member of the sulfurtransferase family and catalyzes the conversion of 3-mercaptopyruvate to pyruvate and protein-bound persulfide.	Pyruvic Acid	91-99	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
25336638-3	2014	TUM1 is a member of the sulfurtransferase family and catalyzes the conversion of 3-mercaptopyruvate to pyruvate and protein-bound persulfide.	persulfides	130-140	mercaptopyruvate sulfurtransferase	Homo sapiens	0-4
25336638-10	2014	Our studies point to distinct roles of each TUM1 isoform in the sulfur transfer processes in the cell, with different compartmentalization of the two splice variants of TUM1.	Sulfur	64-70	mercaptopyruvate sulfurtransferase	Homo sapiens	44-48
25058799-2	2014	It is synthesized endogenously in mammals from the sulfur-containing amino acid l-cysteine by the action of several distinct enzymes: cystathionine-gamma-lyase (CSE), cystathionine-ss-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (3-MST) along with cysteine aminotransferase (CAT).	Cysteine	80-90	mercaptopyruvate sulfurtransferase	Homo sapiens	204-240
24491257-2	2014	H2S is produced from L-cysteine by enzymes such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), 3-mercaptopyruvate sulfurtransferase (3MST), and cysteine aminotransferase (CAT).	Hydrogen Sulfide	0-3	mercaptopyruvate sulfurtransferase	Homo sapiens	119-155
24491257-2	2014	H2S is produced from L-cysteine by enzymes such as cystathionine beta-synthase (CBS), cystathionine gamma-lyase (CSE), 3-mercaptopyruvate sulfurtransferase (3MST), and cysteine aminotransferase (CAT).	Cysteine	21-31	mercaptopyruvate sulfurtransferase	Homo sapiens	119-155
24582857-2	2014	Enzymatic production of H2S is catalyzed by cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS), and 3-mercaptopyruvate sulfurtransferase (MST).	Hydrogen Sulfide	24-27	mercaptopyruvate sulfurtransferase	Homo sapiens	116-152