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5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
?
L-glutamylhydrazine + methylamine
gamma-L-glutamylmethylamide + hydrazine
recombinant enzyme, method optimmization and evaluation, overview
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + ethylamine
theanine + 4-nitroaniline
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
-
-
-
?
7-(N-gamma-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + ?
-
-
-
-
?
D-Gln + Ala
D-Glu-Ala + NH3
-
6.2% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Cys
D-Glu-Cys + NH3
-
19.3% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Glu
D-Glu-Glu + NH3
-
8.1% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Gly
D-Glu-Gly + NH3
-
20.1% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Gly-Gly
Glu-Gly-Gly + NH3
-
-
-
-
?
D-Gln + His
D-Glu-His + NH3
-
116% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + L-Val
D-Glu-Val + NH3
-
8.1% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Met
D-Glu-Met + NH3
-
352% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Phe
D-Glu-Phe + NH3
-
144% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + taurine
D-Glu-taurine + NH3
-
422% of the activity with D-Gln and Gly-Gly
-
-
?
D-Gln + Trp
D-Glu-Trp + NH3
-
558% of the activity with D-Gln and Gly-Gly
-
-
?
glutamic acid gamma methyl ester + ethylamine
theanine + ethanol
-
-
-
-
ir
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
acceptor: amino acids
-
-
?
L-Gln + taurine
gamma-glutamyltaurine + NH3
-
-
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
-
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: hydrolase reaction with H2O as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: hydrolase reaction with H2O as acceptor
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Glu-donor is 5-L-Glu-4-nitroanilide
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
acceptors are amino acids or dipeptides
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
isozyme A prefers basic and aromatic amino acids as acceptors
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: autotranspeptidation with another donor molecule as acceptor
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reaction: autotranspeptidation with another donor molecule as acceptor
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
Glu-donor is GSH
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor specificity, overview
-
?
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2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop, weak inhibition, structure-activity relationship, Escherichia coli enzyme GGT in complex with the inhibitor, Lys562 is the probable residue for the recognition of negative charge at C-terminal of GGsTop
1-chloro-3-tosylamido-7-amino-2-heptanone
-
weak
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 610/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 120/per mol * s
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
-
second-order rate constant for enzyme inactivation is 19/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 80/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 12000/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 24/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 16000/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 35000/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 2900/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 150/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 210/per mol * s
6-diazo-5-oxo-L-norleucine
-
-
Cu2+
-
1 mM, strong inhibition
L- or D-Serine/borate
-
L-serine/borate, not D-serine/borate
-
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
L-1-tosylamido-2-phenylethylchloromethylketone
-
-
Ni2+
-
1 mM, strong inhibition
p-chloromercuribenzoate
-
no inhibition
Zn2+
-
1 mM, strong inhibition
Hg2+
-
1 mM, strong inhibition
Hg2+
-
hydrolase, not transferase reaction
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
i.e. AT-125
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
-
strong, irreversible, 1 mM
additional information
no inhibition of recombinant enzyme by 200 mM L-glutamylhydrazine
-
additional information
-
-
-
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S463D
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
S463K
complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391
S463T
40% decrease in ratio kcat/KM
T391A
mutant protein without intramolecular autocatalytic processing activity
D433N
-
mutation enables gamma-glutamyltranspeptidase to deacylate glutaryl-7-aminocepha-losporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins
additional information
construction of truncation mutants lacking 11, 17, 18, 20 and 26 amino acids at the N-terminus. Mutants lacking 11 and 17 amino acids show about 10% reduction in specific activity, mutants lacking 18 or more amino acids show a complete loss of activity
additional information
-
construction of truncation mutants lacking 11, 17, 18, 20 and 26 amino acids at the N-terminus. Mutants lacking 11 and 17 amino acids show about 10% reduction in specific activity, mutants lacking 18 or more amino acids show a complete loss of activity
additional information
immobilization of recombinant enzyme on 3% sodium alginates inpresence of 2% CaCl2, immobilized recombinant gamma-glutamyltranspeptidase cells exhibit favourable operational stability for enzymatic synthesis of gamma-glutamylmethylamide from L-glutamylhydrazine and methylamine, usage of L-glutamylhydrazine as an economical substrate, immobilized gamma-glutamyltranspeptidase cells are used for 10 reaction cycles, and the average conversion ratio from L-glutamylhydrazine to gamma-glutamylmethylamide reaches 93.2%. No inhibition by 200 mM L-glutamylhydrazine
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Suzuki, H.; Kumagai, H.; Tochikura, T.
gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties
J. Bacteriol.
168
1325-1331
1986
Escherichia coli
brenda
Suzuki, H.; Kumagai, H.; Tochikura, T.
gamma-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization
J. Bacteriol.
168
1332-1335
1986
Escherichia coli
brenda
Suzuki, H.; Izuka, S.; Minami, H.; Miyakawa, N.; Ishihara, S.; Kumagai, H.
Use of bacterial gamma-glutamyltranspeptidase for enzymatic synthesis of gamma-D-glutamyl compounds
Appl. Environ. Microbiol.
69
6399-6404
2003
Escherichia coli
brenda
Suzuki, H.; Miwa, C.; Ishihara, S.; Kumagai, H.
A single amino acid substitution converts gamma-glutamyltranspeptidase to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase)
Appl. Environ. Microbiol.
70
6324-6328
2004
Escherichia coli
brenda
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), Escherichia coli
brenda
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), Escherichia coli
brenda
Yao, Y.F.; Weng, Y.M.; Hu, H.Y.; Ku, K.L.; Lin, L.L.
Expression optimization and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Escherichia coli novablue
Protein J.
25
431-441
2006
Escherichia coli, Escherichia coli Novablue
brenda
Han, L.; Hiratake, J.; Kamiyama, A.; Sakata, K.
Design, synthesis, and evaluation of gamma-phosphono diester analogues of glutamate as highly potent inhibitors and active site probes of gamma-glutamyl transpeptidase
Biochemistry
46
1432-1447
2007
Escherichia coli, Homo sapiens
brenda
Hsu, W.H.; Ong, P.L.; Chen, S.C.; Lin, L.L.
Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase
Indian J. Biochem. Biophys.
46
281-288
2009
Escherichia coli (P18956), Escherichia coli
brenda
Lo, H.F.; Chou, W.M.; Chen, P.J.; Lin, L.L.
Influence of signal-peptide truncations on the functional expression of Escherichia coli gamma -glutamyltranspeptidase
J. Basic Microbiol.
48
260-268
2008
Escherichia coli (P18956), Escherichia coli
brenda
Wada, K.; Hiratake, J.; Irie, M.; Okada, T.; Yamada, C.; Kumagai, H.; Suzuki, H.; Fukuyama, K.
Crystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists
J. Mol. Biol.
380
361-372
2008
Escherichia coli (P18956), Escherichia coli
brenda
Zhang, F.; Zheng, Q.Z.; Jiao, Q.C.; Liu, J.Z.; Zhao, G.H.
Synthesis of theanine from glutamic acid gamma-methyl ester and ethylamine catalyzed by Escherichia coli having gamma-glutamyltranspeptidase activity
Biotechnol. Lett.
32
1147-1150
2010
Escherichia coli
brenda
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, Homo sapiens (P19440), Homo sapiens
brenda
Lisheng, X.; Guizhen, G.; Xingtao, Z.; Mengting, W.
Enzymatic synthesis of gamma-glutamylmethylamide from L-glutamylhydrazine and methylamine catalysed by immobilized recombinant gamma-glutamyltranspeptidase
Biocatal. Biotransform.
37
86-91
2019
Escherichia coli (P18956)
-
brenda