3.4.19.13: glutathione gamma-glutamate hydrolase
This is an abbreviated version!
For detailed information about glutathione gamma-glutamate hydrolase, go to the full flat file.
Word Map on EC 3.4.19.13
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3.4.19.13
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medicine
-
hydroxyacyl
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halide
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alpha-globin
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formyl
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dihalomethanes
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methanes
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phosphoglycolate
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monoxide
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decomposes
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diverted
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halogenated
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formaldehyde
- 3.4.19.13
- medicine
-
hydroxyacyl
- halide
-
alpha-globin
-
formyl
-
dihalomethanes
- methanes
- phosphoglycolate
-
monoxide
-
decomposes
-
diverted
-
halogenated
- formaldehyde
Reaction
Synonyms
At4g29210, BaGGT42, BaGGT469, BlGGT13, BsGGT168, gamma-glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gamma-GT, GGT, GGT-1, GGT1, GGT3, GGT4, GGT5, hp1118, More
ECTree
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Reference on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mehdi, K.; Thierie, J.; Penninckx, M.J.
gamma-Glutamyl transpeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione
Biochem. J.
359
631-637
2001
Saccharomyces cerevisiae
Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism
J. Biol. Chem.
282
2433-2439
2007
Escherichia coli (P18956)
Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate
Proc. Natl. Acad. Sci. USA
103
6471-6476
2006
Escherichia coli (P18956)
Grzam, A.; Martin, M.N.; Hell, R.; Meyer, A.J.
gamma-Glutamyl transpeptidase GGT4 initiates vacuolar degradation of glutathione S-conjugates in Arabidopsis
FEBS Lett.
581
3131-3138
2007
Arabidopsis thaliana (Q9M0G0)
Ohkama-Ohtsu, N.; Oikawa, A.; Zhao, P.; Xiang, C.; Saito, K.; Oliver, D.J.
A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis
Plant Physiol.
148
1603-1613
2008
Arabidopsis thaliana (Q9M0G0)
Grillo, M.P.; Hua, F.; March, K.L.; Benet, L.Z.; Knutson, C.G.; Ware, J.A.
Gamma-glutamyltranspeptidase-mediated degradation of diclofenac-S-acyl-glutathione in vitro and in vivo in rat
Chem. Res. Toxicol.
21
1933-1938
2008
Bos taurus, Rattus norvegicus
Wickham, S.; West, M.; Cook, P.; Hanigan, M.
Gamma-glutamyl compounds: Substrate specificity of gamma-glutamyl transpeptidase enzymes
Anal. Biochem.
414
208-214
2011
Homo sapiens (P19440), Homo sapiens (P36269)
Enoiu, M.; Herber, R.; Wennig, R.; Marson, C.; Bodaud, H.; Leroy, P.; Mitrea, N.; Siest, G.; Wellman, M.
gamma-Glutamyltranspeptidase-dependent metabolism of 4-hydroxynonenal-glutathione conjugate
Arch. Biochem. Biophys.
397
18-27
2002
Homo sapiens
Accaoui, M.; Enoiu, M.; Mergny, M.; Masson, C.; Dominici, S.; Wellman, M.; Visvikis, A.
Gamma-glutamyltranspeptidase-dependent glutathione catabolism results in activation of NF-kB
Biochem. Biophys. Res. Commun.
276
1062-1067
2000
Homo sapiens
Hanigan, M.; Ricketts, W.
Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyl transpeptidase
Biochemistry
32
6302-6306
1993
Homo sapiens
Hultberg, M.; Hultberg, B.
Glutathione turnover in human cell lines in the presence of agents with glutathione influencing potential with and without acivicin inhibition of gamma-glutamyltranspeptidase
Biochim. Biophys. Acta
1726
42-47
2005
Homo sapiens
Stark, A.; Zeiger, E.; Pagano, D.
Glutathione mutagenesis in Salmonella typhimurium is a gamma-glutamyltranspeptidase-enhanced process involving active oxygen species
Carcinogenesis
9
771-777
1988
Salmonella enterica subsp. enterica serovar Typhimurium
Grillo, M.; Benet, L.
Interaction of gamma-glutamyltranspeptidase with clofibryl-S-acyl-glutathione in vitro and in vivo in rat
Chem. Res. Toxicol.
14
1033-1040
2001
Rattus norvegicus
Minami, H.; Suzuki, H.; Kumagai, H.
gamma-Glutamyltranspeptidase, but not YwrD, is important in utilization of extracellular glutathione as a sulfur source in Bacillus subtilis
J. Bacteriol.
186
1213-1214
2004
Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
Meredith, M.; Williams, G.
Intracellular glutathione cycling by gamma-glutamyl transpeptidase in tumorigenic and nontumorigenic cultured rat liver cells
J. Biol. Chem.
261
4986-4992
1986
Rattus norvegicus
Suzuki, H.; Kumagai, H.
Autocatalytic processing of gamma-glutamyltranspeptidase
J. Biol. Chem.
277
43536-43543
2002
Escherichia coli (P18956)
Boanca, G.; Sand, A.; Okada, T.; Suzuki, H.; Kumagai, H.; Fukuyama, K.; Barycki, J.J.
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad
J. Biol. Chem.
282
534-541
2007
Helicobacter pylori (O25743)
Shibayama, K.; Wachino, J.; Arakawa, Y.; Saidijam, M.; Rutherford, N.; Henderson, P.
Metabolism of glutamine and glutathione via gamma-glutamyltranspeptidase and glutamate transport in Helicobacter pylori: Possible significance in the pathophysiology of the organism
Mol. Microbiol.
64
396-406
2007
Helicobacter pylori (O25743)
Ida, T.; Suzuki, H.; Fukuyama, K.; Hiratake, J.; Wada, K.
Structure of Bacillus subtilis ?-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue.
Acta Crystallogr. Sect. D
70
607-614
2014
Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
Kushwaha, N.; Srivastava, S.
Gamma-glutamyl transpeptidase from two plant growth promoting rhizosphere fluorescent pseudomonads
Antonie van Leeuwenhoek
105
45-56
2014
Pseudomonas protegens (L7Z147), Pseudomonas fluorescens (Q4KIM5), Pseudomonas fluorescens Pf-5 (Q4KIM5), Pseudomonas protegens PfT-1 (L7Z147)
Chi, M.C.; Lo, Y.H.; Chen, Y.Y.; Lin, L.L.; Merlino, A.
gamma-Glutamyl transpeptidase architecture: Effect of extra sequence deletion on autoprocessing, structure and stability of the protein from Bacillus licheniformis
Biochim. Biophys. Acta
1844
2290-2297
2014
Bacillus licheniformis (A9YTT0)
Nakajima, M.; Watanabe, B.; Han, L.; Shimizu, B.; Wada, K.; Fukuyama, K.; Suzuki, H.; Hiratake, J.
Glutathione-analogous peptidyl phosphorus esters as mechanism-based inhibitors of gamma-glutamyl transpeptidase for probing cysteinyl-glycine binding site
Bioorg. Med. Chem.
22
1176-1194
2014
Escherichia coli, Homo sapiens
Ito, R.; Ihara, H.; Okada, T.; Ikeda, Y.
1alpha,25-Dihydroxyvitamin D3 enhances gamma-glutamyl transpeptidase activity in LLC-PK1 porcine kidney epithelial cells
Mol. Med. Rep.
10
2111-2115
2014
Sus scrofa
Li, M.; Liang, X.; Rollins, J.
Sclerotinia sclerotiorum gamma-glutamyl transpeptidase (Ss-Ggt1) is required for regulating glutathione accumulation and development of sclerotia and compound appressoria
Mol. Plant Microbe Interact.
25
412-420
2012
Sclerotinia sclerotiorum
Zhang, G.; Ducatelle, R.; Pasmans, F.; DHerde, K.; Huang, L.; Smet, A.; Haesebrouck, F.; Flahou, B.
Effects of Helicobacter suis gamma-glutamyl transpeptidase on lymphocytes: modulation by glutamine and glutathione supplementation and outer membrane vesicles as a putative delivery route of the enzyme
PLoS ONE
8
e77966
2013
Helicobacter suis (D5LUP7)
Zhou, L.; Kang, Q.; Hu, O.; Yu, L.
Ultrasensitive detection of glutathione based on liquid crystals in the presence of gamma-glutamyl transpeptidase
Anal. Chim. Acta
1040
187-195
2018
Homo sapiens (P19440)
Verma, V.V.; Gupta, R.; Goel, M.
Phylogenetic and evolutionary analysis of functional divergence among Gamma glutamyl transpeptidase (GGT) subfamilies
Biol. Direct
10
49
2015
Bacillus subtilis, Halalkalibacterium halodurans, Escherichia coli (P18956), Homo sapiens (P19440), Saccharomyces cerevisiae (Q05902), Bacillus anthracis (Q51693), Helicobacter pylori (Q9F5N9), Thermoplasma acidophilum (Q9HJH4), Bacillus subtilis BEST7613, Saccharomyces cerevisiae ATCC 204508 (Q05902), Escherichia coli K12 (P18956), Thermoplasma acidophilum ATCC 25905 (Q9HJH4)
Kamiyama, A.; Nakajima, M.; Han, L.; Wada, K.; Mizutani, M.; Tabuchi, Y.; Kojima-Yuasa, A.; Matsui-Yuasa, I.; Suzuki, H.; Fukuyama, K.; Watanabe, B.; Hiratake, J.
Phosphonate-based irreversible inhibitors of human gamma-glutamyl transpeptidase (GGT). GGsTop is a non-toxic and highly selective inhibitor with critical electrostatic interaction with an active-site residue Lys562 for enhanced inhibitory activity
Bioorg. Med. Chem.
24
5340-5352
2016
Escherichia coli (P18956), Homo sapiens (P19440), Escherichia coli K12 (P18956)
Terzyan, S.S.; Burgett, A.W.; Heroux, A.; Smith, C.A.; Mooers, B.H.; Hanigan, M.H.
Human gamma-glutamyl transpeptidase 1 structures of the free enzyme, inhibitor-bound tetrahedral transition states, and glutamate-bound enzyme reveal novel movement within the active site during catalysis
J. Biol. Chem.
290
17576-17586
2015
Homo sapiens (P19440)
Bindal, S.; Sharma, S.; Singh, T.P.; Gupta, R.
Evolving transpeptidase and hydrolytic variants of gamma-glutamyl transpeptidase from Bacillus licheniformis by targeted mutations of conserved residue Arg109 and their biotechnological relevance
J. Biotechnol.
249
82-90
2017
Bacillus licheniformis (A9YTT0), Bacillus licheniformis ER-15 (A9YTT0)
Spitzmüller, Z.; Gonda, S.; Kiss-Szikszai, A.; Vasas, G.; Pocsi, I.; Emri, T.
Characterization of extracellular gamma-glutamyl transpeptidase from Aspergillus nidulans
Mycoscience
57
400-403
2016
Aspergillus nidulans, Aspergillus nidulans FGSC A26
-
Kumari, S.; Pal, R.K.; Gupta, R.; Goel, M.
High resolution X-ray diffraction dataset for Bacillus licheniformis gamma glutamyl transpeptidase-acivicin complex SUMO-Tag renders high expression and solubility
Protein J.
36
7-16
2017
Bacillus licheniformis (A9YTT0), Bacillus licheniformis ER-15 (A9YTT0)
Wisnewski, A.V.; Liu, J.; Nassar, A.F.
In vitro cleavage of diisocyanate-glutathione conjugates by human gamma-glutamyl transpeptidase-1
Xenobiotica
46
726-732
2016
Homo sapiens (P19440)
Liu, C.; Jia, J.; Wang, H.; Xue, L.; Kong, Y.; Wang, F.
Purification and characterization of a flavor-related enzyme, gamma-glutamyl-transpeptidase, from Toona sinensis leaves
J. Hortic. Sci. Biotechnol.
91
611-618
2016
Toona sinensis
-
Lee, J.; Lee, J.; Nam, G.; Son, B.; Jang, M.; Lee, S.; Hurh, B.; Kim, T.
Heterologous expression and enzymatic characterization of gamma-glutamyltranspeptidase from Bacillus amyloliquefaciens
J. Microbiol.
55
147-152
2017
Bacillus amyloliquefaciens (A0A1S5V3K5), Bacillus velezensis (A7Z5E0), Bacillus subtilis (P54422), Bacillus licheniformis (Q65KZ6), Bacillus subtilis 168 (P54422), Bacillus licheniformis NCIMB 9375 (Q65KZ6), Bacillus licheniformis Gibson 46 (Q65KZ6), Bacillus licheniformis JCM 2505 (Q65KZ6), Bacillus licheniformis NRRL NRS-1264 (Q65KZ6), Bacillus velezensis BGSC 10A6 (A7Z5E0), Bacillus velezensis DSM 23117 (A7Z5E0), Bacillus amyloliquefaciens SMB469 (A0A1S5V3K5), Bacillus licheniformis NBRC 12200 (Q65KZ6), Bacillus licheniformis ATCC 14580 (Q65KZ6), Bacillus velezensis FZB42 (A7Z5E0), Bacillus licheniformis DSM 13 (Q65KZ6)
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