PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31071163-14	2019	In this work, we also found that Dug1p, previously identified as a Cys-Gly dipeptidase, played an essential role in the hydrolysis of the dipeptide VG in yeast cells.	Dipeptides	138-147	metallodipeptidase	Saccharomyces cerevisiae S288C	33-38
25427234-1	2014	Dug1p, a M20 family metallopeptidase and human orthologue of carnosinase, hydrolyzes Cys-Gly dipeptide, the last step of glutathione (GSH) degradation in Saccharomyces cerevisiae.	cysteinylglycine	85-92	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
29636254-5	2018	Sequence analysis showed that the open reading frames of PDC1, DUG1 (Cys-Gly metallo-di-peptidase in the glutathione degradation pathway), and TEF1 (translational elongation factor EF-1 alpha) genes were inserted into the plasmids of 32, 1, and 1 engineered strains, respectively.	Glutathione	105-116	metallodipeptidase	Saccharomyces cerevisiae S288C	63-67
26081279-1	2015	Relative transcriptions of Aspergillus nidulans dug1-3 (orthologes of Saccharomyces cerevisiae DUG - deficient in utilization of glutathione - pathway genes) and ggtA encoding gamma-glutamyl transpeptidase were studied under conditions inducing glutathione degradation.	Glutathione	129-140	metallodipeptidase	Saccharomyces cerevisiae S288C	48-52
26081279-1	2015	Relative transcriptions of Aspergillus nidulans dug1-3 (orthologes of Saccharomyces cerevisiae DUG - deficient in utilization of glutathione - pathway genes) and ggtA encoding gamma-glutamyl transpeptidase were studied under conditions inducing glutathione degradation.	Glutathione	245-256	metallodipeptidase	Saccharomyces cerevisiae S288C	48-52
26081279-3	2015	Although dug2 showed constitutive transcription, dug1 and dug3 were induced by carbon and nitrogen starvation and yeast extract did not caused significant changes in their relative transcription.	Carbon	79-85	metallodipeptidase	Saccharomyces cerevisiae S288C	49-53
26081279-3	2015	Although dug2 showed constitutive transcription, dug1 and dug3 were induced by carbon and nitrogen starvation and yeast extract did not caused significant changes in their relative transcription.	Nitrogen	90-98	metallodipeptidase	Saccharomyces cerevisiae S288C	49-53
25427234-1	2014	Dug1p, a M20 family metallopeptidase and human orthologue of carnosinase, hydrolyzes Cys-Gly dipeptide, the last step of glutathione (GSH) degradation in Saccharomyces cerevisiae.	Dipeptides	93-102	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
25427234-1	2014	Dug1p, a M20 family metallopeptidase and human orthologue of carnosinase, hydrolyzes Cys-Gly dipeptide, the last step of glutathione (GSH) degradation in Saccharomyces cerevisiae.	Glutathione	121-132	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
25427234-1	2014	Dug1p, a M20 family metallopeptidase and human orthologue of carnosinase, hydrolyzes Cys-Gly dipeptide, the last step of glutathione (GSH) degradation in Saccharomyces cerevisiae.	Glutathione	134-137	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
25427234-3	2014	We report the crystal structure of Dug1p at 2.55 A resolution in complex with a Gly-Cys dipeptide and two Zn(2+) ions.	gly-cys dipeptide	80-97	metallodipeptidase	Saccharomyces cerevisiae S288C	35-40
25427234-3	2014	We report the crystal structure of Dug1p at 2.55 A resolution in complex with a Gly-Cys dipeptide and two Zn(2+) ions.	Zinc	106-108	metallodipeptidase	Saccharomyces cerevisiae S288C	35-40
25427234-7	2014	Modeling of tripeptides into the Dug1p active site showed tripeptides fit well.	tripeptides	12-23	metallodipeptidase	Saccharomyces cerevisiae S288C	33-38
25427234-7	2014	Modeling of tripeptides into the Dug1p active site showed tripeptides fit well.	tripeptides	58-69	metallodipeptidase	Saccharomyces cerevisiae S288C	33-38
25427234-8	2014	Guided by the structure and modeling, we examined the ability of Dug1p to hydrolyze tripeptides, and results show that Dug1p hydrolyzes tripeptides selectively.	tripeptides	84-95	metallodipeptidase	Saccharomyces cerevisiae S288C	65-70
25427234-8	2014	Guided by the structure and modeling, we examined the ability of Dug1p to hydrolyze tripeptides, and results show that Dug1p hydrolyzes tripeptides selectively.	tripeptides	84-95	metallodipeptidase	Saccharomyces cerevisiae S288C	119-124
25427234-8	2014	Guided by the structure and modeling, we examined the ability of Dug1p to hydrolyze tripeptides, and results show that Dug1p hydrolyzes tripeptides selectively.	tripeptides	136-147	metallodipeptidase	Saccharomyces cerevisiae S288C	65-70
25427234-8	2014	Guided by the structure and modeling, we examined the ability of Dug1p to hydrolyze tripeptides, and results show that Dug1p hydrolyzes tripeptides selectively.	tripeptides	136-147	metallodipeptidase	Saccharomyces cerevisiae S288C	119-124
19346245-5	2009	Dug1p had previously been identified as part of the Dug1p-Dug2p-Dug3p complex that operates as an alternate GSH degradation pathway and has also been suggested to function as a possible di- or tripeptidase based on genetic studies.	Glutathione	108-111	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
22170048-6	2012	Whatever the condition tested, GSH is degraded by the cytosolic Dug complex (composed of the three subunits Dug1, Dug2, and Dug3) but not by the gamma-glutamyl-transpeptidase, raising the question of the role of this enzyme.	Glutathione	31-34	metallodipeptidase	Saccharomyces cerevisiae S288C	108-112
20868722-0	2011	Cys-Gly specific dipeptidase Dug1p from S. cerevisiae binds promiscuously to di-, tri-, and tetra-peptides: Peptide-protein interaction, homology modeling, and activity studies reveal a latent promiscuity in substrate recognition.	Cysteine	0-3	metallodipeptidase	Saccharomyces cerevisiae S288C	29-34
20868722-1	2011	Dug1p is a recently identified novel dipeptidase and plays an important role in glutathione (GSH) degradation.	Glutathione	80-91	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-1	2011	Dug1p is a recently identified novel dipeptidase and plays an important role in glutathione (GSH) degradation.	Glutathione	93-96	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-6	2011	Three-dimensional model of Dug1p is constructed and docking of peptides to the modeled structure suggests that hydrogen bonding to active site residues (E172, E171, and D137) lock the N-terminal of the peptide into the binding site.	Hydrogen	111-119	metallodipeptidase	Saccharomyces cerevisiae S288C	27-32
20868722-7	2011	Dug1p recognizes peptides in a metal independent manner and peptide binding is not sensitive to salts (dlogK/dlog[salt] ~ 0) over a range of [NaCl] (0.02-0.5 M), [ZnCl(2)], and [MnCl(2)] (0-0.5 mM).	Metals	31-36	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-7	2011	Dug1p recognizes peptides in a metal independent manner and peptide binding is not sensitive to salts (dlogK/dlog[salt] ~ 0) over a range of [NaCl] (0.02-0.5 M), [ZnCl(2)], and [MnCl(2)] (0-0.5 mM).	Sodium Chloride	142-146	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-7	2011	Dug1p recognizes peptides in a metal independent manner and peptide binding is not sensitive to salts (dlogK/dlog[salt] ~ 0) over a range of [NaCl] (0.02-0.5 M), [ZnCl(2)], and [MnCl(2)] (0-0.5 mM).	zncl	163-167	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-7	2011	Dug1p recognizes peptides in a metal independent manner and peptide binding is not sensitive to salts (dlogK/dlog[salt] ~ 0) over a range of [NaCl] (0.02-0.5 M), [ZnCl(2)], and [MnCl(2)] (0-0.5 mM).	mncl	178-182	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-10	2011	Dug1p activity towards Cys-Gly peptide is significantly reduced (~ 70%) in the presence of Glu-Cys-Gly.	cys-gly peptide	23-38	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-10	2011	Dug1p activity towards Cys-Gly peptide is significantly reduced (~ 70%) in the presence of Glu-Cys-Gly.	gamma-glutamylcysteine	91-98	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-10	2011	Dug1p activity towards Cys-Gly peptide is significantly reduced (~ 70%) in the presence of Glu-Cys-Gly.	Glycine	27-30	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
20868722-11	2011	Therefore, Dug1p can recognize a variety of oligopeptides, but has evolved with post-binding screening potential to hydrolyze Cys-Gly peptides selectively.	Cysteine	126-129	metallodipeptidase	Saccharomyces cerevisiae S288C	11-16
20868722-11	2011	Therefore, Dug1p can recognize a variety of oligopeptides, but has evolved with post-binding screening potential to hydrolyze Cys-Gly peptides selectively.	Glycine	130-133	metallodipeptidase	Saccharomyces cerevisiae S288C	11-16
22277648-1	2012	The recently identified, fungi-specific alternative pathway of glutathione degradation requires the participation of three genes, DUG1, DUG2, and DUG3.	Glutathione	63-74	metallodipeptidase	Saccharomyces cerevisiae S288C	130-134
22277648-12	2012	Dug1p activity in glutathione degradation was found to be restricted to its Cys-Gly peptidase activity, which functioned downstream of the (Dug2p-Dug3p)(2) GATase.	Glutathione	18-29	metallodipeptidase	Saccharomyces cerevisiae S288C	0-5
19346245-5	2009	Dug1p had previously been identified as part of the Dug1p-Dug2p-Dug3p complex that operates as an alternate GSH degradation pathway and has also been suggested to function as a possible di- or tripeptidase based on genetic studies.	Glutathione	108-111	metallodipeptidase	Saccharomyces cerevisiae S288C	52-57
19346245-6	2009	We show here that Dug1p is a homodimer that can also function in a Dug2-Dug3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides in vitro.	cysteinylglycine	139-146	metallodipeptidase	Saccharomyces cerevisiae S288C	18-23
19346245-8	2009	Yeast cells lacking Dug1p (dug1Delta) accumulate Cys-Gly.	cysteinylglycine	49-56	metallodipeptidase	Saccharomyces cerevisiae S288C	20-25
17179087-4	2007	These genes have been named DUG1 (YFR044c), DUG2 (YBR281c), and DUG3 (YNL191w) (defective in utilization of glutathione).	Glutathione	108-119	metallodipeptidase	Saccharomyces cerevisiae S288C	28-32
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	Dipeptides	9-19	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	tripeptides	24-35	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	cysteinylglycine	71-78	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	Glu-Cys-Gly	82-93	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	Dipeptides	9-18	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	gamma-glutamylcysteine	283-296	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-5	2007	Although dipeptides and tripeptides with a normal peptide bond such as cys-gly or glu-cys-gly required the presence of only a functional DUG1 gene that encoded a protein belonging to the M20A metallohydrolase family, the presence of an unusual peptide bond such as in the dipeptide, gamma-glu-cys, or in GSH, required the participation of the DUG2 and DUG3 gene products as well.	Glutathione	304-307	metallodipeptidase	Saccharomyces cerevisiae S288C	137-141
17179087-8	2007	A model is proposed for the functioning of the Dug1p/Dug2p/Dug3p proteins as a specific GSH degradosomal complex.	Glutathione	88-91	metallodipeptidase	Saccharomyces cerevisiae S288C	47-52