PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
32179647-2	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	
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	
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	
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	
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	
23698001-6	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