Reference on EC 3.4.19.13 - glutathione gamma-glutamate hydrolase and Organism(s) Homo sapiens
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AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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 anthracis (Q51693), Bacillus subtilis, Bacillus subtilis BEST7613, Escherichia coli (P18956), Escherichia coli K12 (P18956), Halalkalibacterium halodurans, Helicobacter pylori (Q9F5N9), Homo sapiens (P19440), Saccharomyces cerevisiae (Q05902), Saccharomyces cerevisiae ATCC 204508 (Q05902), Thermoplasma acidophilum (Q9HJH4), 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), Escherichia coli K12 (P18956), Homo sapiens (P19440)
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)
