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Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Homo sapiens and UniProt Accession P36269

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.2 gamma-glutamyltransferase
IUBMB Comments
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
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Homo sapiens
UNIPROT: P36269
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GGTLA1
formerly
(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase
-
alpha-glutamyl transpeptidase
-
-
-
-
gamma-glutamyl peptidyltransferase
-
-
-
-
gamma-glutamyl transferase 1
-
gamma-glutamyl transferase 5
-
-
gamma-glutamyl transferases
-
gamma-glutamyl transpeptidase
gamma-glutamyl transpeptidase 1
-
gamma-glutamyl transpeptidase-1
-
-
gamma-GPT
-
-
-
-
gamma-GT
gamma-GTP
-
-
-
-
gammaGT
-
-
GGT-1
-
-
glutamyl transpeptidase
-
-
-
-
glutamyltransferase, gamma-
-
-
-
-
L-gamma-glutamyl transpeptidase
-
-
-
-
L-gamma-glutamyltransferase
-
-
-
-
L-glutamyltransferase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(5-L-glutamyl)-peptide:amino-acid 5-glutamyltransferase
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity [3-4]. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions [3-4].
CAS REGISTRY NUMBER
COMMENTARY hide
9046-27-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
show the reaction diagram
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
show the reaction diagram
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-(Cys-Gly) + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
4,4'-diphenylmethane diisocyanate linked GSH-GSH + glycylglycine
4,4'-diphenylmethane diisocyanate linked (Cys-Gly)-GSH + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
5-D-glutamyl 3-carboxy-4-nitroanilide + glycylglycine
5-D-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
show the reaction diagram
-
-
-
-
?
5-L-glutamyl 3-carboxy-4-nitroanilide + glucana
5-amino-2-nitrobenzoic acid + N-(3-carboxy-4-nitrophenyl)-L-glutaminyl-L-glutamic acid
show the reaction diagram
-
-
-
ir
5-L-glutamyl 3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
show the reaction diagram
-
-
-
-
?
5-L-glutamyl 3-carboxy-4-nitronailide + glycylglycine
5-amino-2-nitrobenzoic acid + 5-L-glutamylglycylglycine
show the reaction diagram
5-L-glutamyl-(3-carboxyl)-4-nitroanilide + glycylglycine
3-carboxyl-4-nitroaniline + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
5-L-glutamyl-3-carboxy-4-nitroanilide + 5-L-glutamyl-3-carboxy-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-3-carboxy-4-nitroanilide + 3-carboxy-4-nitroaniline
show the reaction diagram
5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
show the reaction diagram
5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
show the reaction diagram
-
autotranspeptidase
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycyl-glycine
4-nitroaniline + 5-L-glutamyl-glycyl-glycine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycyl-L-proline
4-nitroaniline + 5-L-glutamyl-glycyl-L-proline
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 4-nitroaniline
show the reaction diagram
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + L-glutamate
show the reaction diagram
-
hydrolase reaction
-
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-asparagine
4-nitroaniline + 5-L-glutamyl-L-asparagine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
show the reaction diagram
5-L-glutamyl-4-nitroanilide + L-leucyl-L-alanine
4-nitroaniline + 5-L-glutamyl-L-leucyl-L-alanine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
show the reaction diagram
-
-
-
-
?
5-L-glutamyl-L-leucine + glycylglycine
L-Leu + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
7-(N-gamma-glutamylamino)-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + ?
show the reaction diagram
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
D-gamma-glutamyl-S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + glycylglycine
S-([4-[(4-aminophenyl)methyl]phenyl]carbamoyl)-L-cysteinylglycine + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + glycylglycine
(5R,20S)-5,20-diamino-4,8,17,21-tetraoxo-7,18-dithia-3,9,16,22-tetraazatetracosane-1,24-dioic acid + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
show the reaction diagram
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
show the reaction diagram
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
glutathione + Gly-Gly
L-cysteinylglycine + 5-L-glutamyl-Gly-Gly
show the reaction diagram
-
-
-
-
?
glutathione + H2O
L-cysteinylglycine + L-glutamate
show the reaction diagram
-
hydrolase reaction, concurrent to (auto-)transpeptidation
-
-
?
glutathione sulfonic acid + glycylglycine
?
show the reaction diagram
-
-
-
?
glutathionesulfonic acid + glycylglycine
?
show the reaction diagram
-
-
-
?
GSH + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
GSSG + glycylglycine
L-Cys-Gly + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
hexane-1,6-diyldicarbamic acid linked GSH-GSH + glycylglycine
gamma-glutamyl-S-[(6-[[([(2R)-2-amino-3-[(carboxymethyl)amino]-3-oxopropyl]sulfanyl)carbonyl]amino]hexyl)carbamoyl]cysteinylglycine + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
L-gamma-glutamyl-4-nitroanilide + glycine methylester
4-nitroaniline + 5-L-glutamyl-glycyl methylester
show the reaction diagram
very low activity
-
-
?
L-gamma-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamyl-glycylglycine
show the reaction diagram
L-gamma-glutamyl-4-nitroanilide + glycylglycine methylester
4-nitroaniline + 5-L-glutamyl-glycylglycine methylester
show the reaction diagram
low activity
-
-
?
L-gamma-glutamyl-S-[(6-aminohexyl)carbamoyl]-D-cysteinylglycine + glycylglycine
[[(2R)-2-amino-3-[[(6-aminohexyl)carbamoyl]sulfanyl]propanoyl]amino]acetic acid + L-Glu-Gly-Gly
show the reaction diagram
-
-
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
show the reaction diagram
-
-
-
-
?
leukotriene C4 + glycylglycine
leukotriene D4 + 5-L-glutamyl-glycylglycine
show the reaction diagram
-
-
-
?
S-(4-nitro-benzyl)glutathione + glycylglycine
?
show the reaction diagram
-
-
-
?
S-methylglutathione + glycylglycine
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(5-L-glutamyl)-peptide + an amino acid
peptide + a 5-L-glutamyl amino acid
show the reaction diagram
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
show the reaction diagram
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
show the reaction diagram
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
no effect
K+
-
no effect
Li+
-
no effect
Mg2+
-
no effect
Na+
-
no effect
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2RS,RPSP)-2-amino-4-(diphenoxyphosphoryl)butanoic acid
-
(2RS,RPSP)-2-amino-4-[(3-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[(4-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[bis[(3-carboxymethy)lphenoxy]phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(2-carboxyethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(carbamoylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-(ethoxycarbonylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
-
(2RS,RPSP)-2-amino-4-[[3-nitrophenoxy](methoxy)phosphoryl]butanoic acid
-
(2S)-2-amino-2-[(5S)-3-chloro-4,5-dihydro-1,2-oxazol-5-yl]acetic acid
i.e. acivicin
1,2,3,4-tetrahydroisoquinoline
-
the inhibitors can enhance cytostatic action of doxorubicin and cisplatin, which may permit clinicians to decrease their doses thereby alleviating side effects
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 5.0/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.4/per mol * s
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
-
second-order rate constant for enzyme inactivation is 0.16/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 75/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 46/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.24/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 2400/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 130/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 12/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 51/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
-
second-order rate constant for enzyme inactivation is 0.33/per mol * s
4-chloro-N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
5-(L-alpha-glutamylamino)-2-nitrobenzoic acid
-
weak
5-(L-gamma-glutamylamino)-2-nitrobenzoic acid
-
enzyme from human tissues, not serum
5-Iodoacetamidofluorescein
-
inactivation, active site modification
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
5-thiohistidine
mechanism of 5-thio driven inhibition of GGT, overview
6-diazo-5-oxo-L-norleucine
Acetazolamide Maleate
-
-
acivicin
brefeldin A
-
inhibition of recombinant mutant enzyme secretion into cell culture medium from Sf21 cells, accumulation in the cells
Bromocresol green
-
0.01 mM, 31% inhibition, noncompetitive
Co2+
-
weak
Cu2+
-
-
ergothioneine
a natural trimethyl-2-thiohistidine, reversible inhibition mechanism
GGsTop
a glutamate analog that inactivates hGGT1 by forming one covalent and 11 hydrogen bonds with the enzyme, increasing the melting temperature by 20°C
glutathione
-
-
glycine
-
-
glycylglycine
-
-
iodoacetamide
-
inhibition of transpeptidase reaction is more efficient than that of autotranspeptidase reaction
iodoacetate
-
weak
L-azaserine
L-methionine sulphoxide
-
L-Ser
-
in presence of borate, competitive
Maleate
-
-
N-(5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl)benzenesulfonamide
-
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-chlorobenzenesulfonamide
-
-
N-ethylmaleimide
-
-
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]-4-nitrobenzenesulfonamide
-
-
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
i.e. OU749. Competitive towards glycyclglycine, 150fold less toxic towards dividing cells than inhibitor acivicin. Inhibitory both to enzyme from 786-O cells and to human enzyme expressed in mouse fibroblast
NH4+
-
weak
O-diazoacetyl-L-serine
i.e. azaserine
ovothiol A
noncompetitive inhibition, reversible inhibition mechanism
p-hydroxymercuribenzoate
-
weak
serine-borate
competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5
Tris(hydroxymethyl)aminomethane
-
-
Urea
-
complete inactivation of wild-type and mutant at 6 M, low activity at 4 M
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Maleate
-
stimulates hydrolase reaction 3fold, inhibits transpeptidase reaction, with L-Glu as substrate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 1.09
5-L-glutamyl 3-carboxy-4-nitroanilide
1.1 - 1.8
5-L-glutamyl-4-nitroanilide
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
3.61
D-Glu-3-carboxy-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
2.9 - 16.9
glycylglycine
0.0105 - 0.0106
GSH
0.008 - 0.0426
GSSG
1.2
L-gamma-glutamyl-4-nitroanilide
pH 7.4, 37°C, recombinant enzyme
0.008 - 2.1
L-Glu-4-nitroanilide
0.0102 - 0.0108
leukotriene C4
0.0131 - 0.0148
S-(4-nitro-benzyl)glutathione
0.0099 - 0.0182
S-Methylglutathione
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1150
4-nitroanilide
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0287
4-chloro-N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
0.0102 - 0.0183
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
2.7
6-diazo-5-oxo-L-norleucine
pH 7.4, 37°C, recombinant enzyme
2.3
glycine
-
-
0.0759
N-(5-benzyl-1,3,4-thiadiazol-2-yl)-4-chlorobenzenesulfonamide
-
-
0.0743
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]-4-nitrobenzenesulfonamide
-
-
0.0433
N-[5-(4-chlorobenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
0.0738
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
-
-
4.2 - 41.6
serine-borate
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102.8
-
purified enzyme of cellular hepatic carcinoma
12
-
purified recombinant mutant H383A/H505A
120
-
hepatoma
150
-
purified recombinant mutant H383A
16
-
purified enzyme
200.4
-
purified enzyme
25.6
-
purified enzyme, normal and cirrhotic liver
250
-
purified enzyme from liver
423
-
purified enzyme
440
-
purified recombinant wild-type enzyme
450
-
purified recombinant mutant enzyme
47
-
purified recombinant mutant H505A
75.7
-
purified enzyme
800
-
purified enzyme
81
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
assay at
8.2 - 8.5
8.6
-
L-Glu-4-nitroanilide + glycylglycine
9.4
-
L-Glu-4-nitroanilide + L-Glu-4-nitroanilide
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
pH 6.5: about 50% of maximal activity, pH 9.0: about 90% of maximal activity
7 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
precursor
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
bronchial epithelial cell
Manually annotated by BRENDA team
-
cortex microvessels
Manually annotated by BRENDA team
-
WI-38 fetal
Manually annotated by BRENDA team
-
metastatic melanoma
Manually annotated by BRENDA team
-
GGT-overexpression in melanoma cells is associated with resistance to oxidative stress produced by prooxidant agents such as hydrogen peroxide and ascorbic acid
Manually annotated by BRENDA team
-
the enzyme is present in granules and released upon cell activation
Manually annotated by BRENDA team
-
ATCC CRL-1932, a GGT-positive renal cell adenocarcinoma line
Manually annotated by BRENDA team
-
whole body, fetal
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
-
recombinant wild-type in Sf21 cells
-
Manually annotated by BRENDA team
GGT1 is an extracellular enzyme that is anchored to the plasma membrane of cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
human GGT protein without the N-terminal anchor domain is expressed as a soluble enzyme and it exhibits virtually identical enzymatic character to that of wild-type human GGT with the anchor domain
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGT5_HUMAN
586
1
62261
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
110000
14000
-
1 * 38000 + 1 * 14000, SDS-PAGE
150000
-
1 * 150000 + 1 * 95000, SDS-PAGE
160000
20000
200000
-
Triton X-100 solubilized
2000000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
21000
-
1 * 57000 + 1 * 21000, SDS-PAGE, presence of urea, 2-mercaptoethanol
210000
-
Triton X-100 solubilized
22000
24000
-
x * 43000-44000 + x * 24000, wild-type and mutant enzyme, SDS-PAGE
25000
1 * 64000 + 1 * 25000, isoform GGT5, SDS-PAGE
250000
27000
-
1 * 61000 + 1 * 27000, SDS-PAGE
29000
-
1 * 64000 + 1 * 29000, SDS-PAGE
300000
-
serum enzyme, gel filtration
38000
-
1 * 38000 + 1 * 14000, SDS-PAGE
41500
-
x * 41500, heavy subunit of isoform GGT5, SDS-PAGE
47000
-
1 * 47000 + 1 * 22000, SDS-PAGE
500000
-
gel filtration without Triton X-100
53000
-
1 * 53000 + 1 * 20000, papain-solubilized, SDS-PAGE
54000
-
gel filtration
57000
-
1 * 57000 + 1 * 21000, SDS-PAGE, presence of urea, 2-mercaptoethanol
61000
-
1 * 61000 + 1 * 27000, SDS-PAGE
62000
64000
70000
-
there are four enzyme fractions in plasma of healthy subjects, named big-GGT, medium-GGT, small-GGT and free-GGT, with molecular weight corresponding to 2000, 1000, 250, and 70 kDa, respectively
71000
-
papain-solubilized, gel filtration
78000
-
seminal plasma, prostate, testis
80000
-
bile enzyme, gel filtration
82000
-
papain-solubilized enzyme, gel filtration
86000
90000
95000
-
1 * 150000 + 1 * 95000, SDS-PAGE
98000
-
Triton X-100-solubilized, PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant deglycosylated hGGT1 mutant V272A with bound inhibitor DON, mixing of 0.002 ml of 4.3 mg/ml protein in 50 mM HEPES, pH 8.0, 0.5 mM EDTA, 0.02% sodium azide, and 2 mM DON, with 0.0017 ml of H2O, and 0.002 ml of reservoir solution containing 20-25% PEG 3350, 0.1 M Na-cacodylate, pH 6.0, and 0.1 M ammonium chloride, microseeding with apo-hGGT1 crystals, room temperature, 1-2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, modeling using the apo-form crystals of hGGT1 (PDB ID 4Z9O) as template
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H383A
-
site-directed mutagenesis of conserved His383 residue, 3fold reduced activity and 62% reduced Vmax, altered binding of acceptor
H383A/H505A
-
site-directed mutagenesis, 37fold reduced activity
H505A
-
site-directed mutagenesis, 10fold reduced activity
K562S
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type: the mutant's affinity towards Gly-Gly dramatically decreases to 2.0% of wild-type level, whereas it retains 45% of wild-type hydrolytic activity
K568S
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N120Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N230Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N266Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N297Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a slightly decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N344Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N511Q
the mutant exhibits a Km value for the transpeptidation reaction that is not significantly different from that of wild type enzyme. The mutation results in a decreased maximal rate of 5-L-glutamyl-4-nitroanilide turnover
N95Q
the mutation results in an 8fold decrease in the cleavage efficiency of the propeptide
N95Q/N120Q/N230Q/N266Q/N297Q/N344Q/N511Q
total N-glycosylation knock-out mutant
V272A
structure analysis
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 77
in both the transpeptidation and hydrolysis reactions, wild type enzyme exhibits full activity up to 47°C. At temperatures greater than 62°C, the wild type enzyme is rendered completely inactive
56
-
30 min, 42% loss of activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PMSF stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, freeze-dried, at least 3 months
-
-80°C, 9 months
-
2-8°C, 7 days
-
4°C, at least 5 days
-
4°C, t1/2: 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from normal and cirrhotic liver and 6 isoforms from serum of patients with cellular hepatic carcinoma
-
from seminal plasma, kidney, prostate, and testis
-
partial from bile
-
partial from liver
-
partial from pancreas and pancreatic carcinoma and pancreatic carcinoma cell line HPC-Y1
-
recombinant GGT1 mutant V272A from Pichia pastoris strain X-33
recombinant wild-type and mutants from Sf21 insect cells
-
Triton X-100 solubilized liver enzyme is hydrophobic, papain-solubilized liver enzyme is hydrophilic
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris
expressed in Pichia pastoris and in HEK-293 cells
expression in mouse fibroblast
-
expression of recombinant wild-type and mutants in Spodoptera frugiperda Sf21 cells via baculovirus infection
-
expression of wild-type and mutant lacking the putative signal sequence/anchor domain, amino acid 1-27, in Spodoptera frugiperda Sf21 cells via baculovirus infection
-
gene ggt, recombinant expression of wild-type and K562S mutant enzymes in Spodoptera frugiperda Sf9 cells via baculovirus transfection method
gene GGT1, recombinant expression of enzyme mutant V272A in Pichia pastoris strain X-33
transfection of human melanoma cell
-
transfection of Me665/2 cell
-
transfection of Me665/2/21 human melanoma cell, DU145 human prostatic carcinoma cell, and BEAS-2B human bronchial epithelial cell
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
tumor necrosis factor TNFalpha induces GGT promoter transactivation, mRNA and protein synthesis, as well as enzymatic activity. Remicade, a clinically used anti-TNFalpha antibody, small interfering RNA against p50 and p65 nuclear factor NF-kB isoforms, curcumin, a well characterized natural NF-kB inhibitor, as well as a dominant negative inhibitor IkBa, prevent GGT activation at various levels. Over-expression of receptor of TNFalpha-1, TNFR-associated factor-2 TRAF2, TNFR-1 associated death domain TRADD, dominant negative IkBa or NF-kB p65 further confirm GGT promoter activation via NF-kB.Mutation of the NF-kB site located at 110 additionally inhibits TNFalpha-induced promoter induction
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
drug development
development of 5-thiohistidine derivatives as therapeutics for GGT-positive tumors
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, K.I.; Arai, K.; Kobayashi, N.; Saitoh, H.
Purification and properties of gamma-glutamyl transpeptidase from human testis
Andrologia
22
239-246
1990
Homo sapiens
Manually annotated by BRENDA team
Arai, K.; Yoshida, K.; Komoda, T.; Sakagishi, Y.
Comparative studies on the properties of purified gamma-glutamyl transferase from human reproductive system and the kidney
Clin. Biochem.
23
105-112
1990
Homo sapiens
Manually annotated by BRENDA team
Sugimoto, M.; Yamaguchi, N.; Keiichi, K.
Characterization of gamma-GTP in a human pancreatic cancer cell line
Gastroenterol. Jpn.
19
227-231
1984
Homo sapiens
Manually annotated by BRENDA team
Vesely, J.; Cernoch, M.
Solubilization and some properties of gamma-glutamyltransferase from human brain microvessels
Neurochem. Res.
9
927-934
1984
Homo sapiens
Manually annotated by BRENDA team
Rambabu, K.; Pattabiraman, T.N.
Studies on the properties of the variants of gamma-glutamyl transpeptidase in human urine
J. Biosci.
4
287-294
1982
Homo sapiens
-
Manually annotated by BRENDA team
Masuike, M.; Ogawa, M.; Kosaki, G.; Minamiura, N.; Yamamoto, T.
Purification and characterization of gamma-glutamyl transpeptidase from human pancreas
Enzyme
27
163-170
1982
Homo sapiens
Manually annotated by BRENDA team
Echetebu, Z.O.; Moss, D.W.
Multiple forms of human gamma-glutamyltransferase: preparation and characterization of different molecular weight fractions
Enzyme
27
1-8
1982
Homo sapiens
Manually annotated by BRENDA team
Tsuji, A.; Matsuda, Y.; Katunuma, N.
Characterization of human serum gamma-glutamyltranspeptidase
Clin. Chim. Acta
104
361-364
1980
Homo sapiens
Manually annotated by BRENDA team
Shaw, L.M.
gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 1. General
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
3
349-352
1983
Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Wahlefeld, A.W.; Bergmeyer, H.U.
gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 2. Routine method
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
3
352-356
1983
Homo sapiens
-
Manually annotated by BRENDA team
Shaw, L.M.; Stromme, J.H.
gamma-Glutamyltransferase. (gamma-Glutamyl)-peptide:amino acid gamma-glutamyltransferase, EC 2.3.2.2. 3. IFCC reference method (provisional)
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
3
357-364
1983
Homo sapiens
-
Manually annotated by BRENDA team
Takahashi, S.; Zukin, R.S.; Steinman, H.M.
gamma-Glutamyl transpeptidase from WI-38 fibroblasts: purification and active site modification studies
Arch. Biochem. Biophys.
207
87-95
1981
Homo sapiens
Manually annotated by BRENDA team
Miller, S.P.; Awasthi, Y.C.; Srivastava, S.K.
Studies of human kidney gamma-glutamyl transpeptidase. Purification and structural, kinetic and immunological properties
J. Biol. Chem.
251
2271-2278
1976
Homo sapiens
Manually annotated by BRENDA team
Tate, S.S.; Ross, M.E.
Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit
J. Biol. Chem.
252
6042-6045
1977
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Yamashita, K.; Totani, K.; Iwaki, Y.; Takamisawa, I.; Tateishi, N.; Higashi, T.; Sakamoto, Y.; Kobata, A.
Comparative study of the sugar chains of gamma-glutamyltranspeptidases purified from human hepatocellular carcinoma and from human liver
J. Biochem.
105
728-735
1989
Homo sapiens
Manually annotated by BRENDA team
Abe, S.; Kochi, H.; Hiraiwa, K.
Purification and immunological characterization of a new form of gamma-glutamyltransferase of human semen
Biochim. Biophys. Acta
1077
259-264
1991
Homo sapiens
Manually annotated by BRENDA team
Huseby, N.
Purification and some properties of gamma-glutamyltransferase from human liver
Biochim. Biophys. Acta
483
46-56
1977
Homo sapiens
Manually annotated by BRENDA team
Indirani, N.; Hill, P.G.
Partial purification and some properties of gamma-glutamyl transpeptidase from human bile
Biochim. Biophys. Acta
483
57-62
1977
Homo sapiens
Manually annotated by BRENDA team
Minato, S.
Isolation of anthglutin, an inhibitor of gamma-glutamyl transpeptidase from Penicillum oxalicum
Arch. Biochem. Biophys.
192
235-240
1979
Canis lupus familiaris, Homo sapiens
Manually annotated by BRENDA team
Ohta, H.; Sawabu, N.; Kawakami, H.; Watanabe, H.; Ozaki, K.; Toya, D.; Hattori, N.
Characterization of g-glutamyltranspeptidase from human hepatocellular carcinoma, compared with enzymes from normal liver and cirrhotic liver
Clin. Chim. Acta
214
83-92
1993
Homo sapiens
Manually annotated by BRENDA team
Ikeda, Y.; Fujii, J.; Taniguchi, N.; Meister, A.
Expression of an active glycosylated human gamma-glutamyl transpeptidase mutant that lacks a membrane anchor domain
Proc. Natl. Acad. Sci. USA
92
126-130
1995
Homo sapiens
Manually annotated by BRENDA team
Ikeda, Y.; Fujii, J.; Taniguchi, N.
Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase
J. Biochem.
119
1166-1170
1996
Homo sapiens
Manually annotated by BRENDA team
Storozhenko, S.; Belles-Boix, E.; Babiychuk, E.; Herouart, D.; Davey, M.W.; Slooten, L.; Van Montagu, M.; Inze, D.; Kushnir, S.
gamma-Glutamyl transpeptidase in transgenic tobacco plants. Cellular localization, processing, and biochemical properties
Plant Physiol.
128
1109-1119
2002
Arabidopsis thaliana, Arabidopsis thaliana (O65652), Arabidopsis thaliana (Q39078), Arabidopsis thaliana (Q9M0G0), Homo sapiens (P19440), Mus musculus (Q60928)
Manually annotated by BRENDA team
Sener, A.; Yardimci, T.
Activity determination, kinetic analyses and isoenzyme identification of gamma glutamyltransferase in human neutrophils
J. Biochem. Mol. Biol.
38
343-349
2005
Homo sapiens
Manually annotated by BRENDA team
Corti, A.; Paolicchi, A.; Franzini, M.; Dominici, S.; Casini, A.F.; Pompella, A.
The S-thiolating activity of membrane gamma-glutamyltransferase: formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment
Antioxid. Redox Signal.
7
911-918
2005
Homo sapiens
Manually annotated by BRENDA team
Iciek, M.; Chwatko, G.; Rokita, H.; Bald, E.; Wlodek, L.
The effects of modulation of gamma-glutamyl transpeptidase activity in HepG2 cells on thiol homeostasis and caspase-3-activity
Biochim. Biophys. Acta
1773
201-208
2007
Homo sapiens
Manually annotated by BRENDA team
Keillor, J.W.; Castonguay, R.; Lherbet, C.
gamma-Glutamyl transpeptidase substrate specificity and catalytic mechanism
Methods Enzymol.
401
449-467
2005
Homo sapiens
Manually annotated by BRENDA team
Khedmat, H.; Fallahian, F.; Abolghasemi, H.; Hajibeigi, B.; Attarchi, Z.; Alaeddini, F.; Holisaz, M.T.; Pourali, M.; Sharifi, S.; Zarei, N.
Serum gamma-glutamyltransferase, alanine aminotransferase, and aspartate aminotransferase activity in Iranian healthy blood donor men
World J. Gastroenterol.
13
889-894
2007
Homo sapiens
Manually annotated by BRENDA team
do Amaral, R.A.; Malbergier, A.
Effectiveness of the CAGE questionnaire, gamma-glutamyltransferase and mean corpuscular volume of red blood cells as markers for alcohol-related problems in the workplace
Addict. Behav.
33
772-781
2008
Homo sapiens
Manually annotated by BRENDA team
Franzini, M.; Bramanti, E.; Ottaviano, V.; Ghiri, E.; Scatena, F.; Barsacchi, R.; Pompella, A.; Donato, L.; Emdin, M.; Paolicchi, A.
A high performance gel filtration chromatography method for gamma-glutamyltransferase fraction analysis
Anal. Biochem.
374
1-6
2008
Homo sapiens
Manually annotated by BRENDA team
Laskaj, R.; Dodig, S.; Slavica, D.; Cepelak, I.; Kuzman, I.
gamma-Glutamyltransferase activity and total antioxidant status in serum and platelets of patients with community-acquired pneumonia
Arch. Med. Res.
38
424-431
2007
Homo sapiens
Manually annotated by BRENDA team
Fraser, A.; Harris, R.; Sattar, N.; Ebrahim, S.; Smith, G.D.; Lawlor, D.A.
gamma-Glutamyltransferase is associated with incident vascular events independently of alcohol intake: analysis of the British womens heart and health study and meta-analysis
Arterioscler. Thromb. Vasc. Biol.
27
2729-2735
2007
Homo sapiens
Manually annotated by BRENDA team
Strasak, A.M.; Kelleher, C.C.; Klenk, J.; Brant, L.J.; Ruttmann, E.; Rapp, K.; Concin, H.; Diem, G.; Pfeiffer, K.P.; Ulmer, H.; Ulmer, H.
Longitudinal change in serum gamma-glutamyltransferase and cardiovascular disease mortality: a prospective population-based study in 76,113 Austrian adults
Arterioscler. Thromb. Vasc. Biol.
28
1857-1865
2008
Homo sapiens
Manually annotated by BRENDA team
Giral, P.; Jacob, N.; Dourmap, C.; Hansel, B.; Carrie, A.; Bruckert, E.; Girerd, X.; Chapman, M.J.
Elevated gamma-glutamyltransferase activity and perturbed thiol profile are associated with features of metabolic syndrome
Arterioscler. Thromb. Vasc. Biol.
28
587-593
2008
Homo sapiens
Manually annotated by BRENDA team
Shankar, A.; Li, J.; Klein, B.E.; Javier Nieto, F.; Klein, R.
Serum gamma-glutamyltransferase level and peripheral arterial disease
Atherosclerosis
199
102-109
2008
Homo sapiens
Manually annotated by BRENDA team
Caliskan, M.; Erdogan, D.; Gullu, H.; Muderrisoglu, H.
Higher serum gamma-glutamyltransferase levels are independently associated with impaired coronary microvascular function in patients with dilated cardiomyopathy
Atherosclerosis
201
163-167
2008
Homo sapiens
Manually annotated by BRENDA team
Franzini, M.; Corti, A.; Martinelli, B.; Del Corso, A.; Emdin, M.; Parenti, G.F.; Glauber, M.; Pompella, A.; Paolicchi, A.
gamma-Glutamyltransferase activity in human atherosclerotic plaques - biochemical similarities with the circulating enzyme
Atherosclerosis
202
119-127
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Strasak, A.M.; Rapp, K.; Brant, L.J.; Hilbe, W.; Gregory, M.; Oberaigner, W.; Ruttmann, E.; Concin, H.; Diem, G.; Pfeiffer, K.P.; Ulmer, H.; Ulmer, H.
Association of gamma-glutamyltransferase and risk of cancer incidence in men: a prospective study
Cancer Res.
68
3970-3977
2008
Homo sapiens
Manually annotated by BRENDA team
Shankar, A.; Li, J.
Association between serum gamma-glutamyltransferase level and prehypertension among US adults
Circ. J.
71
1567-1572
2007
Homo sapiens
Manually annotated by BRENDA team
Song, S.H.; Kwak, I.S.; Kim, Y.J.; Kim, S.J.; Lee, S.B.; Lee, D.W.; Lee, B.E.
Can gamma-glutamyltransferase be an additional marker of arterial stiffness?
Circ. J.
71
1715-1720
2007
Homo sapiens
Manually annotated by BRENDA team
Lim, J.S.; Lee, D.H.; Park, J.Y.; Jin, S.H.; Jacobs, D.R.
A strong interaction between serum gamma-glutamyltransferase and obesity on the risk of prevalent type 2 diabetes: results from the third national health and nutrition examination survey
Clin. Chem.
53
1092-1098
2007
Homo sapiens
Manually annotated by BRENDA team
Steinmetz, J.; Schiele, F.; Gueguen, R.; Ferard, G.; Henny, J.; Henny, J.
Standardization of gamma-glutamyltransferase assays by intermethod calibration. Effect on determining common reference limits
Clin. Chem. Lab. Med.
45
1373-1380
2007
Homo sapiens
Manually annotated by BRENDA team
Salvagno, G.L.; Lippi, G.; Montagnana, M.; Brocco, G.; Guidi, G.C.
Non-homogeneous separation of triglycerides, gamma-glutamyltransferase, C-reactive protein and lactate dehydrogenase after centrifugation of lithium-heparin tubes
Clin. Chem. Lab. Med.
46
1180-1182
2008
Homo sapiens
Manually annotated by BRENDA team
Lippi, G.; Targher, G.; Montagnana, M.; Salvagno, G.L.; Guidi, G.C.
Relationship between gamma-glutamyltransferase, lipids and lipoprotein(a) in the general population
Clin. Chim. Acta
384
163-166
2007
Homo sapiens
Manually annotated by BRENDA team
Fukushima, Y.; Seo, T.; Hashimoto, N.; Higa, Y.; Ishitsu, T.; Nakagawa, K.
Glutathione-S-transferase (GST) M1 null genotype and combined GSTM1 and GSTT1 null genotypes are risk factors for increased serum gamma-glutamyltransferase in valproic acid-treated patients
Clin. Chim. Acta
389
98-102
2008
Homo sapiens
Manually annotated by BRENDA team
Pompella, A.; Corti, A.; Paolicchi, A.; Giommarelli, C.; Zunino, F.
gamma-Glutamyltransferase, redox regulation and cancer drug resistance
Curr. Opin. Pharmacol.
7
360-366
2007
Homo sapiens
Manually annotated by BRENDA team
Lee, M.Y.; Koh, S.B.; Koh, J.H.; Nam, S.M.; Shin, J.Y.; Shin, Y.G.; Kong, I.D.; Ryu, S.Y.; Lee, T.Y.; Park, J.K.; Chung, C.H.
Relationship between gamma-glutamyltransferase and metabolic syndrome in a Korean population
Diabet. Med.
25
469-475
2008
Homo sapiens
Manually annotated by BRENDA team
Andre, P.; Balkau, B.; Vol, S.; Charles, M.A.; Eschwege, E.; Eschwege, E.
gamma-Glutamyltransferase activity and development of the metabolic syndrome (International Diabetes Federation Definition) in middle-aged men and women: Data from the Epidemiological Study on the Insulin Resistance Syndrome (DESIR) cohort
Diabetes Care
30
2355-2361
2007
Homo sapiens
Manually annotated by BRENDA team
Botton, J.; Heude, B.; Andre, P.; Bresson, J.L.; Ducimetiere, P.; Charles, M.A.; Charles, M.A.
Relationship between gamma-glutamyltransferase and fat mass in a general population of 8-17 years old children. The FLVS II study
Diabetes Metab.
33
354-359
2007
Homo sapiens
Manually annotated by BRENDA team
Kang, Y.H.; Min, H.K.; Son, S.M.; Kim, I.J.; Kim, Y.K.
The association of serum gamma glutamyltransferase with components of the metabolic syndrome in the Korean adults
Diabetes Res. Clin. Pract.
77
306-313
2007
Homo sapiens
Manually annotated by BRENDA team
Iwasaki, T.; Yoneda, M.; Kawasaki, S.; Fujita, K.; Nakajima, A.; Terauchi, Y.
Hepatic fat content-independent association of the serum level of gamma-glutamyltransferase with visceral adiposity, but not subcutaneous adiposity
Diabetes Res. Clin. Pract.
79(1)
e13-e14
2008
Homo sapiens
Manually annotated by BRENDA team
Hashimoto, Y.; Futamura, A.
Relationship between response of gamma-glutamyltransferase to alcohol consumption and levels of fasting plasma glucose
Diabetes Res. Clin. Pract.
80
469-472
2008
Homo sapiens
Manually annotated by BRENDA team
Lee, D.H.; Steffes, M.W.; Jacobs, D.R.
Can persistent organic pollutants explain the association between serum gamma-glutamyltransferase and type 2 diabetes?
Diabetologia
51
402-407
2008
Homo sapiens
Manually annotated by BRENDA team
Sattar, N.; Wannamethee, S.G.; Forouhi, N.G.
Novel biochemical risk factors for type 2 diabetes: pathogenic insights or prediction possibilities?
Diabetologia
51
926-940
2008
Homo sapiens
Manually annotated by BRENDA team
Rinck, D.; Frieling, H.; Freitag, A.; Hillemacher, T.; Bayerlein, K.; Kornhuber, J.; Bleich, S.
Combinations of carbohydrate-deficient transferrin, mean corpuscular erythrocyte volume, gamma-glutamyltransferase, homocysteine and folate increase the significance of biological markers in alcohol dependent patients
Drug Alcohol Depend.
89
60-65
2007
Homo sapiens
Manually annotated by BRENDA team
Giommarelli, C.; Corti, A.; Supino, R.; Favini, E.; Paolicchi, A.; Pompella, A.; Zunino, F.
Cellular response to oxidative stress and ascorbic acid in melanoma cells overexpressing gamma-glutamyltransferase
Eur. J. Cancer
44
750-759
2008
Homo sapiens
Manually annotated by BRENDA team
Lee, D.H.; Buijsse, B.; Steffen, L.; Holtzman, J.; Luepker, R.; Jacobs, D.R.
Association between serum gamma-glutamyltransferase and cardiovascular mortality varies by age: the Minnesota Heart Survey
Eur. J. Cardiovasc. Prev. Rehabil.
16
16-20
2008
Homo sapiens
Manually annotated by BRENDA team
Bidel, S.; Silventoinen, K.; Hu, G.; Lee, D.H.; Kaprio, J.; Tuomilehto, J.
Coffee consumption, serum gamma-glutamyltransferase and risk of type II diabetes
Eur. J. Clin. Nutr.
62
178-185
2008
Homo sapiens
Manually annotated by BRENDA team
Langford, M.P.; Redens, T.B.; Harris, N.R.; Lee, S.; Jain, S.K.; Reddy, S.; McVie, R.
Plasma levels of cell-free apoptotic DNA ladders and gamma-glutamyltranspeptidase (GGT) in diabetic children
Exp. Biol. Med.
232
1160-1169
2007
Homo sapiens
Manually annotated by BRENDA team
Kwiecien, I.; Rokita, H.; Lorenc-Koci, E.; Sokolowska, M.; Wlodek, L.
The effect of modulation of gamma-glutamyl transpeptidase and nitric oxide synthase activity on GSH homeostasis in HepG2 cells
Fundam. Clin. Pharmacol.
21
95-103
2007
Homo sapiens
Manually annotated by BRENDA team
Takigawa, T.; Hibino, Y.; Kimura, S.; Yamauchi, H.; Wang, B.; Wang, D.; Ogino, K.
Association between serum gamma-glutamyltransferase and oxidative stress related factors
Hepatogastroenterology
55
50-53
2008
Homo sapiens
Manually annotated by BRENDA team
Fraser, A.; Ebrahim, S.; Smith, G.D.; Lawlor, D.A.
A comparison of associations of alanine aminotransferase and gamma-glutamyltransferase with fasting glucose, fasting insulin, and glycated hemoglobin in women with and without diabetes
Hepatology
46
158-165
2007
Homo sapiens
Manually annotated by BRENDA team
Hu, G.; Tuomilehto, J.; Pukkala, E.; Hakulinen, T.; Antikainen, R.; Vartiainen, E.; Jousilahti, P.
Joint effects of coffee consumption and serum gamma-glutamyltransferase on the risk of liver cancer
Hepatology
48
129-136
2008
Homo sapiens
Manually annotated by BRENDA team
Heisterkamp, N.; Groffen, J.; Warburton, D.; Sneddon, T.P.
The human gamma-glutamyltransferase gene family
Hum. Genet.
123
321-332
2008
Homo sapiens (P19440), Homo sapiens (P36269), Homo sapiens
Manually annotated by BRENDA team
Strasak, A.M.; Pfeiffer, R.M.; Klenk, J.; Hilbe, W.; Oberaigner, W.; Gregory, M.; Concin, H.; Diem, G.; Pfeiffer, K.P.; Ruttmann, E.; Ulmer, H.; Ulmer, H.
Prospective study of the association of gamma-glutamyltransferase with cancer incidence in women
Int. J. Cancer
123
1902-1906
2008
Homo sapiens
Manually annotated by BRENDA team
Emdin, M.; Passino, C.; Michelassi, C.; Donato, L.; Pompella, A.; Paolicchi, A.
Additive prognostic value of gamma-glutamyltransferase in coronary artery disease
Int. J. Cardiol.
136
80-85
2008
Homo sapiens
Manually annotated by BRENDA team
Yavuz, B.B.; Yavuz, B.; Halil, M.; Cankurtaran, M.; Ulger, Z.; Cankurtaran, E.S.; Aytemir, K.; Ariogul, S.
Serum elevated gamma glutamyltransferase levels may be a marker for oxidative stress in Alzheimers disease
Int. Psychogeriatr.
20
815-823
2008
Homo sapiens
Manually annotated by BRENDA team
Corti, A.; Franzini, M.; Casini, A.F.; Paolicchi, A.; Pompella, A.
Vitamin C supply to bronchial epithelial cells linked to glutathione availability in elf--a role for secreted gamma-glutamyltransferase?
J. Cyst. Fibros.
7
174-178
2008
Homo sapiens
Manually annotated by BRENDA team
Bozbas, H.; Yildirir, A.; Demir, O.; Cakmak, A.; Karacaglar, E.; Yilmaz, M.; Eroglu, S.; Pirat, B.; Ozin, B.; Muderrisoglu, H.
Serum gamma-glutamyltransferase activity is increased in patients with calcific aortic valve stenosis
J. Heart Valve Dis.
17
371-375
2008
Homo sapiens
Manually annotated by BRENDA team
Caliskan, M.; Erdogan, D.; Gullu, H.; Ciftci, O.; Yildirim, I.; Baycan, S.; Yildirir, A.; Muderrisoglu, H.
Association between serum gamma-glutamyltransferase levels and coronary microvascular function in hypertensive patients
J. Hypertens.
25
2497-2503
2007
Homo sapiens
Manually annotated by BRENDA team
Bergmann, J.F.; Vrolijk, J.M.; van der Schaar, P.; Vroom, B.; van Hoek, B.; van der Sluys Veer, A.; de Vries, R.A.; Verhey, E.; Hansen, B.E.; Brouwer, J.T.; Janssen, H.L.; Schalm, S.W.; de Knegt, R.J.
gamma-Glutamyltransferase and rapid virological response as predictors of successful treatment with experimental or standard peginterferon-alpha-2b in chronic hepatitis C non-responders
Liver Int.
27
1217-1225
2007
Homo sapiens
Manually annotated by BRENDA team
Harasymiw, J.; Bean, P.
The early detection of alcohol consumption (EDAC) test shows better performance than gamma-glutamyltransferase (GGT) to detect heavy drinking in a large population of males and females
Med. Sci. Monit.
13
PI19-PI24
2007
Homo sapiens
Manually annotated by BRENDA team
Kim, J.A.; Kim, S.M.; Yoon, D.
The relationship between gamma-glutamyltransferase and adiponectin in nonalcoholic women
Metab. Clin. Exp.
56
578-582
2007
Homo sapiens
Manually annotated by BRENDA team
Saijo, Y.; Utsugi, M.; Yoshioka, E.; Horikawa, N.; Sato, T.; Gong, Y.; Kishi, R.
The relationship of gamma-glutamyltransferase to C-reactive protein and arterial stiffness
Nutr. Metab. Cardiovasc. Dis.
18
211-219
2008
Homo sapiens
Manually annotated by BRENDA team
Simao, A.N.; Dichi, J.B.; Barbosa, D.S.; Cecchini, R.; Dichi, I.
Influence of uric acid and gamma-glutamyltransferase on total antioxidant capacity and oxidative stress in patients with metabolic syndrome
Nutrition
24
675-681
2008
Homo sapiens
Manually annotated by BRENDA team
Trachtenberg, F.; Barregard, L.; McKinlay, S.
The influence of urinary flow rate in children on excretion of markers used for assessment of renal damage: albumin, gamma-glutamyl transpeptidase, N-acetyl-beta-D-glucosaminidase, and alpha1-microglobulin
Pediatr. Nephrol.
23
445-456
2008
Homo sapiens
Manually annotated by BRENDA team
Puukka, K.; Hietala, J.; Koivisto, H.; Anttila, P.; Bloigu, R.; Niemelae, O.
Obesity and the clinical use of serum GGT activity as a marker of heavy drinking
Scand. J. Clin. Lab. Invest.
67
480-488
2007
Homo sapiens
Manually annotated by BRENDA team
Souza, J.F.; Longui, C.A.; Miorin, L.A.; Sens, Y.A.
gamma-Glutamyltransferase activity in chronic dialysis patients and renal transplant recipients with hepatitis C virus infection
Transplant. Proc.
40
1319-1323
2008
Homo sapiens
Manually annotated by BRENDA team
Wannamethee, S.G.; Lennon, L.; Shaper, A.G.
The value of gamma-glutamyltransferase in cardiovascular risk prediction in men without diagnosed cardiovascular disease or diabetes
Atherosclerosis
201
168-175
2008
Homo sapiens
Manually annotated by BRENDA team
Reuter, S.; Schnekenburger, M.; Cristofanon, S.; Buck, I.; Teiten, M.H.; Daubeuf, S.; Eifes, S.; Dicato, M.; Aggarwal, B.B.; Visvikis, A.; Diederich, M.
Tumor necrosis factor alpha induces gamma-glutamyltransferase expression via nuclear factor-kappaB in cooperation with Sp1
Biochem. Pharmacol.
77
397-411
2009
Homo sapiens
Manually annotated by BRENDA team
Franzini, M.; Corti, A.; Fornaciari, I.; Balderi, M.; Torracca, F.; Lorenzini, E.; Baggiani, A.; Pompella, A.; Emdin, M.; Paolicchi, A.
Cultured human cells release soluble gamma-glutamyltransferase complexes corresponding to the plasma b-GGT
Biomarkers
14
486-492
2009
Homo sapiens
Manually annotated by BRENDA team
Demircan, S.; Yazici, M.; Durna, K.; Kilicaslan, F.; Demir, S.; Pinar, M.; Gulel, O.
The importance of gamma-glutamyltransferase activity in patients with coronary artery disease
Clin. Cardiol.
32
220-225
2009
Homo sapiens
Manually annotated by BRENDA team
Giommarelli, C.; Corti, A.; Supino, R.; Favini, E.; Paolicchi, A.; Pompella, A.; Zunino, F.
Gamma-glutamyltransferase-dependent resistance to arsenic trioxide in melanoma cells and cellular sensitization by ascorbic acid
Free Radic. Biol. Med.
46
1516-1526
2009
Homo sapiens
Manually annotated by BRENDA team
Claessen, H.; Brenner, H.; Drath, C.; Arndt, V.
Gamma-glutamyltransferase and disability pension: a cohort study of construction workers in Germany
Hepatology
51
482-490
2010
Homo sapiens
Manually annotated by BRENDA team
King, J.B.; West, M.B.; Cook, P.F.; Hanigan, M.H.
A novel, species-specific class of uncompetitive inhibitors of gamma-glutamyl transpeptidase
J. Biol. Chem.
284
9059-9065
2009
Homo sapiens
Manually annotated by BRENDA team
Corti, A.; Duarte, T.L.; Giommarelli, C.; De Tata, V.; Paolicchi, A.; Jones, G.D.; Pompella, A.
Membrane gamma-glutamyl transferase activity promotes iron-dependent oxidative DNA damage in melanoma cells
Mutat. Res.
669
112-121
2009
Homo sapiens
Manually annotated by BRENDA team
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, Homo sapiens (P19440)
Manually annotated by BRENDA team
West, M.B.; Wickham, S.; Quinalty, L.M.; Pavlovicz, R.E.; Li, C.; Hanigan, M.H.
Autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95
J. Biol. Chem.
286
28876-28888
2011
Homo sapiens (P19440), Homo sapiens
Manually annotated by BRENDA team
Balakrishna, S.; Prabhune, A.
Gamma-glutamyl transferases: A structural, mechanistic and physiological perspective
Front. Biol.
9
51-65
2014
Homo sapiens (P19440), Bacillus subtilis (P54422), Bacillus subtilis 168 (P54422)
-
Manually annotated by BRENDA team
Hanigan, M.H.; Gillies, E.M.; Wickham, S.; Wakeham, N.; Wirsig-Wiechmann, C.R.
Immunolabeling of gamma-glutamyl transferase 5 in normal human tissues reveals that expression and localization differ from gamma-glutamyl transferase 1
Histochem. Cell Biol.
143
505-515
2015
Homo sapiens
Manually annotated by BRENDA team
Fornaciari, I.; Fierabracci, V.; Corti, A.; Aziz Elawadi, H.; Lorenzini, E.; Emdin, M.; Paolicchi, A.; Franzini, M.
Gamma-glutamyltransferase fractions in human plasma and bile: characteristic and biogenesis
PLoS ONE
9
e88532
2014
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Watanabe, B.; Tabuchi, Y.; Wada, K.; Hiratake, J.
Synthesis and evaluation of the inhibitory activity of the four stereoisomers of the potent and selective human gamma-glutamyl transpeptidase inhibitor GGsTop
Bioorg. Med. Chem. Lett.
27
4920-4924
2017
Homo sapiens (P19440)
Manually annotated by BRENDA team
Milito, A.; Brancaccio, M.; Lisurek, M.; Masullo, M.; Palumbo, A.; Castellano, I.
Probing the interactions of sulfur-containing histidine compounds with human gamma-glutamyl transpeptidase
Mar. Drugs
17
650
2019
Equus caballus (E5G727), Homo sapiens (P19440), Homo sapiens
Manually annotated by BRENDA team
Terzyan, S.; Cook, P.; Heroux, A.; Hanigan, M.
Structure of 6-diazo-5-oxo-norleucine-bound human gamma-glutamyl transpeptidase 1, a novel mechanism of inactivation
Protein Sci.
26
1196-1205
2017
Homo sapiens (P19440), Homo sapiens
Manually annotated by BRENDA team