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0.12
1-menaphthylglutathione
-
at pH 8.0 and 37°C
0.075
2,4-dinitrophenylglutathione
-
at pH 8.0 and 37°C
0.23
4-methylbiphenylylglutathione
-
at pH 8.0 and 37°C
0.3
4-nitrobenzylglutathione
-
at pH 8.0 and 37°C
0.031
5-D-Glu-4-nitroanilide
-
-
0.137
5-D-glutamyl-4-nitroanilide
-
-
0.65 - 1.09
5-L-glutamyl 3-carboxy-4-nitroanilide
0.0109 - 15.3
5-L-glutamyl-4-nitroanilide
0.03 - 0.49
5-L-glutamyl-7-amido-4-methylcoumarin
0.0334
5-L-glutamyl-L-leucine
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0126
7-(N-gamma-glutamylamino)-4-methylcoumarin
-
25°C, pH 5.5
0.22
9-methylanthracenylglutathione
-
at pH 8.0 and 37°C
3.61
D-Glu-3-carboxy-4-nitroanilide
-
-
0.038 - 2.4
gamma-Glu-Cys
11.3
gamma-glutamyl-D,L-phenylthioglycylglycine
-
pH 7.5, 22°C
0.0143 - 0.1
gamma-L-glutamyl-4-nitroanilide
16.7 - 26.9
glutamyl-(3-carboxyl)-4-nitroanilide
0.0346
glutathione sulfonic acid
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0751
glutathionesulfonic acid
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
2.5
Gly-Gly
-
37°C, pH 8.0
0.687
glycyl-glycine
-
pH 8.0, 37°C
0.007 - 590
glycylglycine
2.9
L-alpha-methyl-5-glutamyl-L-alpha-aminobutyrate
-
hydrolase reaction
0.021 - 10.6
L-gamma-glutamyl-4-nitroanilide
0.005 - 4
L-Glu-4-nitroanilide
0.301
L-glutamic acid 5-(3-carboxy-4-nitroanilide)
-
pH 8.0, 37°C
10
L-glutamine
-
hydrolase reaction
0.0102 - 0.0108
leukotriene C4
0.0131 - 0.0148
S-(4-nitro-benzyl)glutathione
0.0099 - 0.0182
S-Methylglutathione
0.398
S-nitroso-glutathione
-
pH 8.0, 37°C
additional information
additional information
-
0.65
5-L-glutamyl 3-carboxy-4-nitroanilide
-
-
1.09
5-L-glutamyl 3-carboxy-4-nitroanilide
-
-
0.0109
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, transpeptidase reaction with Gly-Gly
0.0125
5-L-glutamyl-4-nitroanilide
-
-
0.0125
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, hydrolysis
0.021
5-L-glutamyl-4-nitroanilide
-
0.024
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.045
5-L-glutamyl-4-nitroanilide
wild-type, pH 9.0, 37°C
0.046
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
0.058
5-L-glutamyl-4-nitroanilide
mutant S463T, pH 9.0, 37°C
0.07
5-L-glutamyl-4-nitroanilide
-
wild-type, pH 8.0, 40°C
0.073
5-L-glutamyl-4-nitroanilide
-
hydrolysis
0.08
5-L-glutamyl-4-nitroanilide
in 1 mM MgCl2, 50 mM Tris-HCl buffer (pH 8.0), at 40°C
0.09
5-L-glutamyl-4-nitroanilide
-
mutant T417S, pH 8.0, 40°C
0.11
5-L-glutamyl-4-nitroanilide
-
mutant T399S, pH 8.0, 40°C
0.22
5-L-glutamyl-4-nitroanilide
-
monomeric 30-kDa enzyme, at pH 11.0, in the presence of subtilisin, at 80°C
0.25
5-L-glutamyl-4-nitroanilide
-
heterodimeric 67-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C
0.74
5-L-glutamyl-4-nitroanilide
-
at pH 8.0 and 37°C
0.75
5-L-glutamyl-4-nitroanilide
-
hydrolysis
0.84
5-L-glutamyl-4-nitroanilide
-
reaction in the presence of 20 mM glycylglycine
1.1
5-L-glutamyl-4-nitroanilide
mutant enzyme N266Q, at 37°C, pH 7.4
1.2
5-L-glutamyl-4-nitroanilide
mutant enzyme N95Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
mutant enzyme N120Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
mutant enzyme N230Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
mutant enzyme N297Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
mutant enzyme N344Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
mutant enzyme N511Q, at 37°C, pH 7.4
1.3
5-L-glutamyl-4-nitroanilide
wild type enzyme, at 37°C, pH 7.4
1.8
5-L-glutamyl-4-nitroanilide
-
-
4.3
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
4.4
5-L-glutamyl-4-nitroanilide
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
5.2
5-L-glutamyl-4-nitroanilide
-
monomeric 30-kDa enzyme, at pH 8.0, in the absence of subtilisin, at 60°C
10.4
5-L-glutamyl-4-nitroanilide
-
wild-type enzyme
12
5-L-glutamyl-4-nitroanilide
-
-
15.3
5-L-glutamyl-4-nitroanilide
-
mutant enzyme D445A
0.03
5-L-glutamyl-7-amido-4-methylcoumarin
-
-
0.39
5-L-glutamyl-7-amido-4-methylcoumarin
-
liver enzyme
0.41
5-L-glutamyl-7-amido-4-methylcoumarin
-
-
0.49
5-L-glutamyl-7-amido-4-methylcoumarin
-
biliary tract enzyme
0.038
gamma-Glu-Cys
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.046
gamma-Glu-Cys
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
2.3
gamma-Glu-Cys
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
2.4
gamma-Glu-Cys
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
0.0143
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme H368S
0.025
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme H368S
0.025
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, transpeptidase activity with Gly-Gly as acceptor, mutant enzyme Y327N
0.067
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, mutant enzyme Y327N
0.1
gamma-L-glutamyl-4-nitroanilide
pH 7.0, temperature not specified in the publication, hydrolytic activity, wild-type enzyme
16.7
glutamyl-(3-carboxyl)-4-nitroanilide
-
at pH 9.0 and 30°C
25.9
glutamyl-(3-carboxyl)-4-nitroanilide
-
at pH 7.5 and 30°C
26.9
glutamyl-(3-carboxyl)-4-nitroanilide
-
at pH 11.0 and 30°C
0.0057
glutathione
-
-
0.033
glutathione
-
hydrolase reaction
0.09
glutathione
-
isoform II
0.11
glutathione
-
isoform I
0.18
glutathione
-
transpeptidation
0.007
glycylglycine
pH 7.4, 37°C
0.7
glycylglycine
recombinant mutant R109E, pH 9.0, 60°C
0.8
glycylglycine
recombinant mutant R109F, pH 9.0, 60°C
0.94
glycylglycine
recombinant wild-type enzyme, pH 9.0, 60°C
1.5
glycylglycine
recombinant mutant R109K, pH 9.0, 60°C
1.6
glycylglycine
recombinant mutant R109S, pH 9.0, 60°C
2.9 - 2.96
glycylglycine
-
-
2.9 - 2.96
glycylglycine
-
recombinant wild-type enzyme
2.9 - 2.96
glycylglycine
-
rat kidney enzyme
3.4
glycylglycine
-
recombinant mutant enzyme
4
glycylglycine
-
with 0.8 mM L-Glu-4-nitroanilide, kidney enzyme
4 - 4.7
glycylglycine
-
L-Met, rat kidney enzyme
4.35
glycylglycine
-
with 1.6 mM L-Glu-4-nitroanilide, kidney enzyme
0.21
GS-bimane
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
0.22
GS-bimane
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.41
GS-bimane
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
0.47
GS-bimane
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
0.0105
GSH
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0106
GSH
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.032
GSH
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.042
GSH
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
0.6
GSH
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
0.66
GSH
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
0.008
GSSG
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.038
GSSG
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT I
0.042
GSSG
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II
0.0426
GSSG
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.39
GSSG
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT B
0.44
GSSG
-
37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A
1.09
L-cysteinylglycine
-
-
1.09
L-cysteinylglycine
-
L-Cys-Gly, rat kidney enzyme
0.029 - 0.035
L-cystine
-
kidney enzyme
0.029 - 0.035
L-cystine
-
hydrolase reaction
0.029 - 0.035
L-cystine
-
hydrolase reaction
0.029 - 0.035
L-cystine
-
D-Glu-4-nitroanilide
0.029 - 0.035
L-cystine
-
glutathione
0.021
L-gamma-glutamyl-4-nitroanilide
pH 7.4, 37°C
0.123
L-gamma-glutamyl-4-nitroanilide
pH 9.6, 37°C, recombinant enzyme
0.2
L-gamma-glutamyl-4-nitroanilide
-
pH 8.0, 37°C, native extracellular enzyme
0.214
L-gamma-glutamyl-4-nitroanilide
-
recombinant extracellular enzyme, pH 9.0, 40°C
0.3
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109F, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109E, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109S, pH 9.0, 60°C
0.4
L-gamma-glutamyl-4-nitroanilide
recombinant wild-type enzyme, pH 9.0, 60°C
0.42
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant wild-type enzyme, pH 9.0, 40°C
0.579
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized modified wild-type enzyme MTWs-GGT-Phar, pH 8.0, 37°C
0.58
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450D, pH 9.0, 40°C
0.58
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450Q, pH 9.0, 40°C
0.597
L-gamma-glutamyl-4-nitroanilide
-
recombinant free wild-type enzyme GGT, pH 8.0, 37°C
0.69
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450A, pH 9.0, 40°C
0.7
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109K, pH 9.0, 60°C
0.76
L-gamma-glutamyl-4-nitroanilide
Q62WE3
recombinant mutant N450K, pH 9.0, 40°C
0.879
L-gamma-glutamyl-4-nitroanilide
-
recombinant immobilized wild-type enzyme, MTWs-GGT, pH 8.0, 37°C
1.2
L-gamma-glutamyl-4-nitroanilide
pH 7.4, 37°C, recombinant enzyme
3.6
L-gamma-glutamyl-4-nitroanilide
-
pH 8.0, 37°C
8.2
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109L, pH 9.0, 60°C
10.6
L-gamma-glutamyl-4-nitroanilide
recombinant mutant R109M, pH 9.0, 60°C
0.0083
L-Gln
-
-
0.76
L-Gln
-
rat kidney enzyme
0.005 - 0.0068
L-Glu-4-nitroanilide
-
-
0.005 - 0.0068
L-Glu-4-nitroanilide
-
hydrolase reaction
0.005 - 0.0068
L-Glu-4-nitroanilide
-
hydrolase reaction
0.0068
L-Glu-4-nitroanilide
-
hydrolase reaction
0.008
L-Glu-4-nitroanilide
-
hydrolase reaction
0.035
L-Glu-4-nitroanilide
-
-
0.068
L-Glu-4-nitroanilide
-
hydrolase reaction
0.13 - 0.18
L-Glu-4-nitroanilide
-
-
0.13 - 0.18
L-Glu-4-nitroanilide
-
with GSH
0.13 - 0.18
L-Glu-4-nitroanilide
-
with L-Cys-bis-glycine, rat kidney enzyme
0.21
L-Glu-4-nitroanilide
-
with 8 mM L-Gly-Gly, kidney enzyme
0.21 - 0.32
L-Glu-4-nitroanilide
-
with L-Met-Gly, kidney enzyme
0.31
L-Glu-4-nitroanilide
-
hydrolase reaction
0.32
L-Glu-4-nitroanilide
-
with 16 mM L-Gly-Gly , kidney enzyme
0.4
L-Glu-4-nitroanilide
-
transpeptidation
0.67
L-Glu-4-nitroanilide
-
-
0.8
L-Glu-4-nitroanilide
-
-
0.8
L-Glu-4-nitroanilide
recombinant enzyme
0.8
L-Glu-4-nitroanilide
-
in presence of glycylglycine
0.81
L-Glu-4-nitroanilide
-
-
0.9
L-Glu-4-nitroanilide
-
-
0.9
L-Glu-4-nitroanilide
-
carcinoma enzyme
1
L-Glu-4-nitroanilide
-
-
1
L-Glu-4-nitroanilide
-
-
1.1
L-Glu-4-nitroanilide
-
-
1.25
L-Glu-4-nitroanilide
-
in absence of glycylglycine
1.3
L-Glu-4-nitroanilide
-
-
1.3
L-Glu-4-nitroanilide
-
enzyme from ciliary body
1.4
L-Glu-4-nitroanilide
-
recombinant wild-type, transpeptidation
1.5
L-Glu-4-nitroanilide
-
recombinant wild-type
1.5
L-Glu-4-nitroanilide
-
bile enzyme
1.7
L-Glu-4-nitroanilide
-
isoform I, hydrolase reaction
2.1
L-Glu-4-nitroanilide
-
isoform II, hydrolase reaction
2.1
L-Glu-4-nitroanilide
-
recombinant mutant enzyme
4
L-Glu-4-nitroanilide
-
-
0.0102
leukotriene C4
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0108
leukotriene C4
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0131
S-(4-nitro-benzyl)glutathione
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0148
S-(4-nitro-benzyl)glutathione
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0099
S-Methylglutathione
isoform GGT1, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
0.0182
S-Methylglutathione
isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
Km-values for several acceptors in diabetic and control rats, female and male, with donors L-Glu-4-nitroanilide and L-5-glutamyl-(7-amido-4-methylcoumarin)
-
additional information
additional information
-
hydrolysis data
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
kinetic study of renatured large subunit
-
additional information
additional information
-
enzyme from seminal plasma, kidney, prostate, and testis
-
additional information
additional information
-
biphasic kinetics in transpeptidase reaction with 1-aminocyclopropane-1-carboxylic acid as acceptor, Km-values
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
enzyme kinetics analysis is done according to the ping-pong mechanism when both the substrates L-gamma-glutamyl-4-nitroanilide and glycyl-glycine are used
-
additional information
additional information
-
enzyme kinetics analysis is done according to the ping-pong mechanism when both the substrates L-gamma-glutamyl-4-nitroanilide and glycyl-glycine are used
-
additional information
additional information
-
Michaelis-Menten kinetics with L-gamma-glutamyl-4-nitroanilide as substrate, native extracellular enzyme
-
additional information
additional information
steady-state kinetics of purified free enzyme BLGGT and purified immobilized enzyme CMS-GGT
-
additional information
additional information
-
thermodynamics and kinetic analysis of free and immobilized recombinant enzymes, overview
-