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Information on EC 2.3.2.2 - gamma-glutamyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P07314
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2.3.2.2 gamma-glutamyltransferaseIUBMB 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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Word Map
- 2.3.2.2
- aminotransferase
-
alt
- bilirubin
- cholesterol
- albumin
- triglyceride
- bile
- biliary
- women
- creatinine
- gsh
- transaminase
- hepatocytes
- cirrhosis
- fibrosis
- urinary
- cholestasis
- duct
-
uric
-
c-reactive
- steatosis
- aminopeptidase
- jaundice
-
drinkers
-
hepatotoxicity
-
non-alcoholic
-
intrahepatic
- nafld
-
nephrotoxicity
-
ursodeoxycholic
-
waist
-
ultrasonography
- diethylnitrosamine
-
circumference
-
corpuscular
-
hepatocarcinogenesis
-
abuse
-
hepatectomy
- hepatobiliary
- phenobarbital
-
preneoplastic
- alpha-fetoprotein
-
homa-ir
-
abstinence
- pruritus
- 2-acetylaminofluorene
-
n-acetyl-beta-d-glucosaminidase
- cholangitis
-
cholangiopancreatography
- pharmacology
-
elastography
- diagnostics
- nutrition
- food industry
- drug development
- analysis
- medicine
- synthesis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
a (5-L-glutamyl)-peptide
+
=
+
Synonyms
ggt, gamma-glutamyl transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-gtp, gamma glutamyl transferase, glutamyl transpeptidase, gamma-glutamyl-transpeptidase, gammagt, blggt, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glutamyl transpeptidase
-
-
-
-
gamma-glutamyl peptidyltransferase
-
-
-
-
gamma-glutamyl transpeptidase
gamma-GPT
-
-
-
-
gamma-GT
-
-
-
-
gamma-GTP
-
-
-
-
glutamyl transpeptidase
-
-
-
-
glutamyltransferase, gamma-
-
-
-
-
L-gamma-glutamyl transpeptidase
-
-
-
-
L-gamma-glutamyltransferase
-
-
-
-
L-glutamyltransferase
-
-
-
-
gamma-glutamyl transpeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
mechanism
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
structure
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
almost the entire glutamyl moiety is necessary for recognition in the binding site of the donor substrate
-
a (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
active site on small subunit
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
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
9046-27-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-gamma-glutamyl-3-carboxy-4-nitroanilide + H2O
3-carboxy-4-nitroaniline + L-glutamate
assay at pH 8
-
-
?
5-D-glutamyl-4-nitroanilide + acceptor
4-nitroaniline + 5-D-glutamyl-acceptor
-
-
-
-
?
5-D/L-glutamyl-phenylhydrazine + acceptor
phenylhydrazine + 5-L-glutamyl-acceptor
-
-
product is cytotoxic
ir
5-L-glutamyl-3-carboxy-4-nitroanilide + glycylglycine
5-L-glutamyl-glycylglycine + 3-carboxy-4-nitroaniline
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + 5-L-glutamyl-4-nitroanilide
5-L-glutamyl-5-L-glutamyl-4-nitroanilide + 4-nitroaniline
-
-
-
?
5-L-glutamyl-4-nitroanilide + citrulline
4-nitroaniline + 5-L-glutamyl-citrulline
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + Gly-Gly
4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycine
4-nitroaniline + 5-L-glutamyl-glycine
-
glutamyl transfer at 17.2%
-
-
?
5-L-glutamyl-4-nitroanilide + H2O
4-nitroaniline + Glu
-
ping-pong mechanism
-
-
?
5-L-glutamyl-4-nitroanilide + L-alanylglycine
4-nitroaniline + 5-L-glutamyl-L-alanylglycine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cysteine
4-nitroaniline + 5-L-glutamyl-L-cysteine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cysteinylglycine
4-nitroaniline + glutathione
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamate
4-nitroaniline + 5-L-glutamyl-L-glutamate
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-histidine
4-nitroaniline + 5-L-glutamyl-L-histidine
-
glutamyl transfer at 8.6% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-hydroxyproline
4-nitroaniline + 5-L-glutamyl-L-hydroxyproline
-
glutamyl transfer at 17% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-isoleucine
4-nitroaniline + 5-L-glutamyl-L-isoleucine
-
glutamyl transfer at 17% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-leucine
4-nitroaniline + 5-L-glutamyl-L-leucine
-
glutamyl transfer at 20% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-methioninamide
4-nitroaniline + 5-L-glutamyl-L-methioninamide
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionyl(2,2,2-trifluoroethylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(2,2,2-trifluoroethylamide)
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionyl(2-fluoroethylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(2-fluoroethylamide)
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionyl(3,3,3-trifluoropropylamide)
4-nitroaniline + 5-L-glutamyl-L-methionyl(3,3,3-trifluoropropylamide)
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionylethylamide
4-nitroaniline + 5-L-glutamyl-L-methionylethylamide
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionylpropylamide
4-nitroaniline + 5-L-glutamyl-L-methionylpropylamide
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
5-L-glutamyl-4-nitroanilide + L-threonine
4-nitroaniline + 5-L-glutamyl-L-threonine
-
glutamyl transfer at 20% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-valine
4-nitroaniline + 5-L-glutamyl-L-valine
-
glutamyl transfer at 20% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-7-amido-4-methylcoumarin + acceptor
7-amino-4-methylcoumarin + 5-L-glutamyl-acceptor
-
acceptors are amino acids and peptides, overview
-
-
?
5-L-glutamyl-7-amido-4-methylcoumarin + glycylglycine
7-amino-4-methylcoumarin + 5-L-glutamyl-glycylglycine
-
-
-
-
?
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
diclofenac-S-acyl-glutathione + Gly
diclofenac-S-acyl-cysteinylglycine + ?
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
ectoenzyme protects the epithelial cells against oxidants by replenishing intracellular glutathione
-
-
?
glutathione + daunomycin
L-cysteinylglycine + 5-L-glutamyl-daunomycin
-
detoxification of daunomycin by transpeptidation
-
ir
glutathione + H2O
L-cysteinylglycine + L-glutamate
-
hydrolase reaction, concurrent to (auto-)transpeptidation
-
ir
glutathione + L-cysteinylglycine
L-cysteinylglycine + glutathione
-
-
-
-
?
L-Glu-4-nitroanilide + glutathione
4-nitroaniline + 5-L-glutamyl-glutathione
-
-
-
-
?
leukotriene C4 + acceptor
leukotriene D4 + glutamyl-acceptor
-
i.e. glutathione containing derivative of arachidonic acid, acceptors are H2O, amino acids or dipeptides
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
487899, 487905, 487912, 487914, 487915, 487917, 487918, 487919, 487920, 487957, 487958, 487960, 487964, 487969
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
stereospecificity
-
?
(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
-
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
poor substrates are beta-substituted amino acids
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor binding site reacts with L- and to a lesser extent D-enantiomer
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: 5-L-Glu-3-sulfonic-4-nitroanilide
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: GSH S-substituted derivatives
-
-
?
(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
-
Glu-donor is 5-L-Glu-4-nitroanilide
-
-
ir
(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
-
acceptors are amino acids or dipeptides
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donors: ophthalmic acid, poly-5-Glu-derivatives, L-5-Glu-7-amino-4-methylcoumarin
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: 5-L-Glu-naphthylamide
-
-
?
(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
-
imino acids are no substrates
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
acceptor specificity, overview
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
acceptor specificity, overview
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
acceptor specificity, overview
-
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
strict L-stereospecificity of 5-Glu-acceptor site
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: leukotriene C
-
-
?
(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
-
Glu-donor is GSH
-
?
(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: glutathione disulfide
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: glutathione disulfide
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: glutathione disulfide
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor: S-acetophenoneglutathione
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
donor specificity, overview
-
ir
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
-
4-nitroaniline is cytotoxic
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
best acceptor
-
-
?
5-L-glutamyl-4-nitroanilide + glycylglycine
4-nitroaniline + 5-L-glutamylglycylglycine
-
best acceptor
-
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-alanine
4-nitroaniline + 5-L-glutamyl-L-alanine
-
glutamyl transfer at 32% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-arginine
4-nitroaniline + 5-L-glutamyl-L-arginine
-
glutamyl transfer at 30% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-aspartate
4-nitroaniline + 5-L-glutamyl-L-aspartate
-
glutamyl transfer at 8.6% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-cystine
4-nitroaniline + 5-L-glutamyl-L-cystine
-
best acceptor
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
glutamyl transfer at 43% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-glutamine
4-nitroaniline + 5-L-glutamyl-L-glutamine
-
L-methionine and L-glutamine are best acceptors
-
-
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-lysine
4-nitroaniline + 5-L-glutamyl-L-lysine
-
glutamyl transfer at 26% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
glutamyl transfer at 39% the rate with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-methionine
4-nitroaniline + 5-L-glutamyl-L-methionine
-
L-methionine and glutamine are best acceptors
-
-
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-phenylalanine
4-nitroaniline + 5-L-glutamyl-L-phenylalanine
-
glutamyl transfer at 26% the rate of the reaction with glycylglycine
-
-
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
-
-
-
?
5-L-glutamyl-4-nitroanilide + L-serine
4-nitroaniline + 5-L-glutamyl-L-serine
-
glutamyl transfer at 28% the rate of the reaction with glycylglycine
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
-
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
best donor
-
-
?
glutathione + acceptor
cysteinylglycine + 5-L-glutamyl-acceptor
-
acceptor: amino acids
-
r
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
ir
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
autotranspeptidation
-
-
?
glutathione + glutathione
L-cysteinylglycine + 5-glutamyl-glutathione
-
autotranspeptidation
-
r
additional information
?
-
-
ester and amide derivatives of L-Glu-4-nitroanilide are no substrates, overview
-
-
?
additional information
?
-
-
activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
-
-
?
additional information
?
-
-
the enzyme is implicated in cellular detoxification, the biosynthesis of leukotrienes and control of the physiological concentration of glutathione. It also plays important roles in Parkinsons disease, diabetes, apoptosis inhibition and cancer drug resistance
-
-
?
additional information
?
-
-
the mechanism of the deacylation step of GGT-mediated transpeptidation using L-methionine derivatives as acceptor substrates is consistent with the observed Bronsted linear free energy relationship, pH-rate profile, and solvent kinetic isotope effects. It is proposed that in the rate-limiting step these acceptor substrates carry out a nucleophilic attack on the acyl-enzyme intermediate, with simultaneous deprotonation of the nucleophilic amino group, to form a tetrahedral intermediate. At the transition state, nucleophilic attack is more advanced than deprotonation of the amine, leading to significant development of positive charge on the nucleophilic nitrogen
-
-
?
additional information
?
-
-
in vivo expreriments in rat kidney, liver, heart, or brain. gamma-Glu-[1-13C]Gly is hyperpolarized using the TEMPOL nitroxyl radical (4-hydroxy-2,2,6,6-tetramethylpiperidine-N-oxyl), and the resulting 13C polarization at the time of injection is 9%, overview. A spectral peak corresponding to [1-13C]Gly is readily detected in the kidney
-
-
-
additional information
?
-
-
enzyme GGT catalyzes the cleavage of the gamma-peptide bond between the glutamyl and cysteinyl residues of GSH and related molecules, either hydrolyzing the bond or ligating the free alpha-amine of an amino acid or peptide, cf. glutathione hydrolase, EC 3.4.19.13. Development of a HP-GGT probe for hyperpolarized (HP) MR measurements for dissolution dynamic nuclear polarization (DNP), a versatile method to hyperpolarize nuclear spins. It can temporarily increase the signal from NMR-active nuclei by as much as 4 or 5 orders of magnitude, which has enabled the detection of metabolic transformations in real-time with high sensitivity using NMR spectroscopy and imaging. Design and preparation of an HP molecular probe targeting GGT activity, gamma-Glu-[1-13C]Gly. gamma-Glu-[1-13C]Gly fulfills the requirements of an HP molecular probe, and the probe can monitor real-time GGT activity in vivo. Detection of enzyme bound-gamma-Glu and radiolabeled Gly from hydrolysis. Method, overview
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-D/L-glutamyl-phenylhydrazine + acceptor
phenylhydrazine + 5-L-glutamyl-acceptor
-
-
product is cytotoxic
ir
a (5-L-glutamyl)-peptide + an amino acid
a peptide + a 5-L-glutamyl amino acid
-
-
-
-
?
glutathione + an amino acid
L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
ectoenzyme protects the epithelial cells against oxidants by replenishing intracellular glutathione
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
-
-
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
?
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
involved in amino acid transport systems, processing of mercapturic acids, and in pathways of metabolism of prostaglandins, estrogens and leukotrienes
-
-
r
(5-L-glutamyl)-peptide + acceptor + H+
peptide + 5-L-glutamyl amino acid
-
concurrent reactions: autotranspeptidation with another donor molecule as acceptor, and hydrolase reaction with H2O as acceptor
-
?
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
involved in 5-L-glutamyl cycle of glutathione metabolism
-
ir
glutathione + an amino acid
L-cysteinylglycine + 5-L-glutamyl-amino acid
-
initial step of glutathione degradation
-
ir
additional information
?
-
-
activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
-
-
?
additional information
?
-
-
the enzyme is implicated in cellular detoxification, the biosynthesis of leukotrienes and control of the physiological concentration of glutathione. It also plays important roles in Parkinsons disease, diabetes, apoptosis inhibition and cancer drug resistance
-
-
?
additional information
?
-
-
in vivo expreriments in rat kidney, liver, heart, or brain. gamma-Glu-[1-13C]Gly is hyperpolarized using the TEMPOL nitroxyl radical (4-hydroxy-2,2,6,6-tetramethylpiperidine-N-oxyl), and the resulting 13C polarization at the time of injection is 9%, overview. A spectral peak corresponding to [1-13C]Gly is readily detected in the kidney
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl)butanoic acid
-
competitive
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfonyl)butanoic acid
-
-
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)thio)butanoic acid
-
competitive
(2S)-2-amino-4-((4-(((carboxymethyl)amino)carbonyl)benzyl)sulfinyl)butanoic acid
-
competitive
2-amino-4-[(3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl]butanoic acid
-
-
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
-
i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
6-diazo-5-oxo-L-norleucine
-
irreversible inactivation of pancreatic enzyme, S-methylglutathione prevents at 10 mM, maleate increases inhibition at 0.25-1 M
L- or D-Serine/borate
-
formation of a tetrahedral complex at the active site
-
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
Phenobarbital
-
active site-directed, irreversible inactivation, optimal at pH 9.0, serine/borate or GSH protects, maleate protects slightly, kinetics
Thiobarbituric acid
-
active site-directed, irreversible inactivation, optimal at pH 9.5, serine/borate or GSH protects, maleate protects slightly, kinetics
additional information
-
no inhibition by phorbol ester, polyamines, cAMP
-
additional information
-
no inhibition: 2-amino-3-(S-methylsulfonimidoyl)propanoic acid, 2-amino-4-(methylsulfonyl)butanoic acid, 5-hydroxy-DL-lysine
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hippurate
-
stimulates hydrolase reaction, inhibits transpeptidation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13 - 0.18
L-Glu-4-nitroanilide
-
with L-Cys-bis-glycine, rat kidney enzyme
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
-
Km values for several amino acids and dipeptides, overview
-
additional information
additional information
-
kinetic study of renatured large subunit
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl)butanoic acid
-
-
3.5
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfonyl)butanoic acid
-
-
0.52
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)thio)butanoic acid
-
-
0.23
(2S)-2-amino-4-((4-(((carboxymethyl)amino)carbonyl)benzyl)sulfinyl)butanoic acid
-
-
0.053
2-amino-4-[(3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl]butanoic acid
-
-
additional information
additional information
-
Ki-values for derivatives of 4-acrboxybutyramide, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
additional information
additional information
-
Ki values for diverse amino acids, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats with tumor
20
measured in jejunal mucosa after treatment with dietary glutamine in normal rats
25
measured in jejunal mucosa after treatment with dietary glutamine in DMBA-treated rats without tumor
additional information
additional information
-
activity in induced diabetic rats is higher than in control rats and higher in male than in female rats
additional information
-
activity during developmental stages in lung epithelial cells type I and II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.1 - 9.6
-
about 70% of maximal activity at pH 8.1, about 75% of maximal activity at pH 9.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
upreglation of gamma-glutamyl transpeptidase is induced by suboptimal concentrations of the serum and modification of intracellular cAMP level by dibutyryl cAMP. Up-regulation of gamma-glutamyl transpeptidase can contribute to adaption of astrocytic cells to metabolic and/or oxidative perturbances occuring under various pathological conditions, including radiation- and drug-induced toxicity
-
gamma-glutamyltransferase is upregulated after oxidative stress through the Ras signal transduction pathway in rat colon carcinoma cells
-
decrease in the hippocampal GGT decreases 2 h after the intravenous injection of 0.005 mg IL-1beta, increaes after 24 h and returns to control levels after 96 h. No significant changes in the hippocampal GGT activity are observed at 2 h and 24 h following the intracerebroventricular infusion of 50 ng IL-1beta
additional information
-
treatment with 1,2,3,4-tetrahydroisoquinolone affects the enzymatic activity of gamma-glutamyl transpeptidase in the dopaminergic structures of brain
-
-
487899, 487905, 487912, 487916, 487918, 487929, 487930, 487931, 487936, 487938, 487964, 487971, 657955, 658282, 659787, 660051, 755785
-
normal and induced enzyme activity, not expression level, by streptozotocin diabetes induced in rats
-
hyperplastic hepatic nodules, primary and Yoshida ascites (AH 13) hepatomas
additional information
-
blood-brain-barrier-associated isozyme activity induces the cell to form three-dimensional structures in cell culture, inducible by angiogenic and astroglial factors, e.g. bFGF, formation is reduced by cAMP
additional information
-
the enzyme is widely expressed on the apical surface of epithelial-cell lining ducts, most prominently in the proximal tubules of the kidney and liver biliary ducts, and is also expressed on leukocytes and astrocytes. Non-invasive, real-time detection of GGT activity in vivo, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
gamma glutamyltranspeptidase is a key enzyme involved in mediating cisplatin nephrotoxicity, which potentially acts to cleave cisplatin-GSH conjugates to a toxic metabolite
physiological function
-
the gamma-glutamyl transpeptidase (GGT) is a cell surface enzyme that plays an essential central role in glutathione (GSH) homeostasis. Elevated serum GGT levels are a general marker of diseases affecting the liver
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GGT1_RAT
568
1
61610
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
22000
48000
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
additional information
additional information
-
in the presence of Triton X-100: molecular aggregation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
1 * 48000 + 1 * 20000, about, gel filtration of denatured and native enzyme
additional information
-
the enzyme is composed of two non-identical catalytically active subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
rat gammaGT is synthesized as a propeptide of 568 amino acids and is cleaved to yield a stable heterodimer with a large amphipathic subunit (379 amino acids) and a smaller hydrophilic subunit (189 amino acids). gammaGT propeptide cleavage occurs within the endoplasmic reticulum
glycoprotein
-
post-translational multiple forms differing in sugar portion
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from hyperplastic hepatic nodules, Yoshida ascites hepatoma, primary hepatoma, kidney
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of liver specific isoform III from fetal mRNA, screening of rat genetic library, single copy gene, DNA, including enhancer and promotor, sequence determination, plasmid construction and expression in Escherichia coli, transient enzyme expression in hepatoma cell lines, dependent on differentiation state of the cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
renaturation as catalytically active enzyme after inactivation with 6-diazo-5-oxo-L-norleucine, requires glutathione or S-methyl derivative as a substrate ligand, circular dichroic spectra
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
direct detection of GGT activity can provide critical information for the diagnosis of several pathologies. Elevated serum GGT levels are a general marker of diseases affecting the liver
medicine
pharmacology
medicine
-
bioconversion of cytotoxic and mutagenic agents to inactive 5-L-glutamyl-derivatives
medicine
-
direct detection of GGT activity can provide critical information for the diagnosis of several pathologies. GGT may serve as a tumor biomarker and its presence on the cell surface is particularly attractive for imaging applications
pharmacology
-
bile extracts from diclofenac-dosed rats at 200 mg/kg, show the presence of the gamma-GT-mediated diclofenac-S-acyl-glutathione degradation product diclofenac-N-acyl-cysteinylglycine, where a total of 8 microg is excreted 6 h postadministration. When diclofenac-S-acyl-glutathione is incubated with gamma-GT, the GSH adduct is degraded in a linear time-dependent fashion
pharmacology
-
cisplatin administration significantly elevates blood urea nitrogen and serum creatinine in male rats day 5 post-treatment. Inhibition of gamma glutamyltranspeptidase prevents cisplatin nephrotoxicity, but not cellular toxicity in rat proximal tubular cultures
pharmacology
-
the administration of a single intraperitoneal dose of potassium dichromate decreases the activity of gamma-glutamyl transpeptidase and alanine aminopeptidase. Utility of gamma-GT and AAP activities as biomarkers in the evaluation of the Cr-induced nephrotoxicity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kimm, S.W.; Kim, E.G.; Park, S.C.
Partial purification and characterization of gamma-glutamyl transpeptidase from rat kidney
Korean J. Biochem.
18
135-143
1986
Rattus norvegicus
-
Frielle, T.; Curthoys, N.P.
Characterization of the amphipathic structure of gamma-glutamyltranspeptidase F13
Biophys. J.
37
193-195
1982
Rattus norvegicus
Tsuchida, S.; Hoshino, K.; Sato, T.; Ito, N.
Purification of gamma-glutamyltransferases from rat hepatomas and hyperplastic hepatic nodules, and comparison with the enzyme from rat kidney
Cancer Res.
39
4200-4205
1979
Rattus norvegicus
Taniguchi, N.
Purification and some properties of gamma-glutamyl transpeptidase from azo dye-induced hepatoma
J. Biochem.
75
473-480
1974
Rattus norvegicus
Jaken, S.; Mason, M.
Purification and comparison of several catalytic parameters of the gamma-glutamyltranspeptidase of rat mammary adenocarcinoma (13762) and of normal rat mammary gland
Biochim. Biophys. Acta
568
331-338
1979
Rattus norvegicus
Ding, J.L.; Smith, G.D.; Peters, T.J.
The purification of gamma-glutamyltransferase from normal rat liver
Biochem. Soc. Trans.
8
77
1980
Rattus norvegicus, Rattus norvegicus Wistar
Horiuchi, S.; Inoue, M.; Morino, Y.
Latent active site in rat-kidney gamma-glutamyl transpeptidase. The refolding process of the large subunit and characterization of the renatured enzyme
Eur. J. Biochem.
105
93-102
1980
Rattus norvegicus, Rattus norvegicus Wistar
Ding, J.L.; Smith, G.D.; Peters, T.J.
Purification and properties of gamma-glutamyl transferase from normal rat liver
Biochim. Biophys. Acta
657
334-343
1981
Rattus norvegicus
Sachdev, G.P.; Leahy, D.S.; Chace, K.V.
Phenobarbital and related compounds as novel inhibitors of gamma-glutamyltranspeptidase
Biochim. Biophys. Acta
749
125-129
1983
Rattus norvegicus
Takahashi, S.; Steinman, H.M.; Ball, D.
Purification and characterization of gamma-glutamyltransferase from rat pancreas
Biochim. Biophys. Acta
707
66-73
1982
Rattus norvegicus, Rattus norvegicus Wistar
Tarachand, U.
Purification and properties of gamma-glutamyl transpeptidase from rat deciduoma
J. Appl. Biochem.
6
278-288
1984
Rattus norvegicus
Bernstrm, K.; Orning, L.; Hammarstrm, S.
gamma-Glutamyl transpeptidase, a leukotriene metabolizing enzyme
Methods Enzymol.
86
38-45
1982
Rattus norvegicus, Sus scrofa
Allison, D.
gamma-Glutamyl transpeptidase: kinetics and mechanism
Methods Enzymol.
113
419-437
1985
Ovis aries, Mammalia, Mus musculus, Rattus norvegicus
Tate, S.S.; Meister, A.
gamma-Glutamyl transpeptidase from kidney
Methods Enzymol.
113
400-419
1985
Mammalia, Mus musculus, Rattus norvegicus
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
-
Cook, N.D.; Peters, T.J.
Purification of gamma-glutamyltransferase by phenyl boronate affinity chromatography. Studies on the acceptor specificity of transpeptidation by rat kidney gamma-glutamyltransferase
Biochim. Biophys. Acta
828
205-212
1985
Rattus norvegicus
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
Brouillet, A.; Darbouy, M.; Okamoto, T.; Chobert, M.N.; Lahuna, O.; Garlatti, M.; Goodspeed, D.; Laperche, Y.
Functional characterization of the rat g-glutamyl transpeptidase promoter that is expressed and regulated in the liver and hepatoma cells
J. Biol. Chem.
269
14878-14884
1994
Rattus norvegicus
Roux, F.; Durieu-Trautmann, O.; Chaverot, N.; Claire, M.; Mailly, P.; Bourre, J.M.; Strosberg, A.D.; Couraud, P.O.
Regulation of gamma-glutamyl transpeptidase and alkaline phosphatase activities in immortalized rat brain microvessel endothelial cells
J. Cell. Physiol.
159
101-113
1994
Rattus norvegicus
Ingbar, D.H.; Hepler, K.; Dowin, R.; Jacobsen, E.; Dunitz, J.M.; Nici, L.; Jamieson, J.D.
gamma-Glutamyl transpeptidase is a polarized alveolar epithelial membrane protein
Am. J. Physiol.
269
L261-L271
1995
Rattus norvegicus
Dvorakova, L.; Krusek, J.; Stastny, F.; Lisy, V.
Relationship between kinetic properties of gamma-glutamyl transpeptidase and the structure of its saccharide moiety
Biochim. Biophys. Acta
1292
163-167
1996
Rattus norvegicus
Keren, R.; Stark, A.A.
gamma-Glutamyl transpeptidase-dependent mutagenicity and cytotoxicity of gamma-glutamyl derivatives: a model for biochemical targeting of chemotherapeutic agents
Environ. Mol. Mutagen.
32
377-386
1998
Rattus norvegicus
Cornwell, P.D.; Watkins, J.B.
Changes in the kinetic parameters of hepatic gamma-glutamyltransferase from streptozotocin-induced diabetic rats
Biochim. Biophys. Acta
1545
184-191
2001
Rattus norvegicus
Castonguay, R.; Lherbet, C.; Keillor, J.W.
Mapping of the active site of rat kidney gamma-glutamyl transpeptidase using activated esters and their amide derivatives
Bioorg. Med. Chem.
10
4185-4191
2002
Rattus norvegicus
Castonguay, R.; Lherbet, C.; Keillor, J.W.
Kinetic studies of rat kidney gamma-glutamyltranspeptidase deacylation reveal a general base-catalyzed mechanism
Biochemistry
42
11504-11513
2003
Rattus norvegicus
Lherbet, C.; Gravel, C.; Keillor, J.W.
Synthesis of S-alkyl L-homocysteine analogues of glutathione and their kinetic studies with gamma-glutamyl transpeptidase
Bioorg. Med. Chem. Lett.
14
3451-3455
2004
Rattus norvegicus
Keillor, J.W.; Menard, A.; Castonguay, R.; Lherbet, C.; Rivard, C.
Pre-steady-state kinetic studies of rat kidney gamma-glutamyl transpeptidase confirm its ping-pong mechanism
J. Phys. Org. Chem.
17
529-536
2004
Rattus norvegicus
-
Lherbet, C.; Keillor, J.W.
Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulfur derivatives of L-glutamic acid
Org. Biomol. Chem.
2
238-245
2004
Rattus norvegicus
Lorenc-Koci, E.; Sokolowska, M.; Kwiecien, I.; Wlodek, L.
Treatment with 1,2,3,4-tetrahydroisoquinolone affects the levels of nitric oxide, S-nitrosothiols, glutathione and the enzymatic activity of gamma-glutamyl transpeptidase in the dopaminergic structures of rat brain
Brain Res.
1049
133-146
2005
Rattus norvegicus
Mares, V.; Malik, R.; Lisa, V.; Sedo, A.
Up-regulation of gamma-glutamyl transpeptidase (GGT) activity in growth perturbed C6 astrocytes
Brain Res. Mol. Brain Res.
136
75-80
2005
Rattus norvegicus
Kinlough, C.L.; Poland, P.A.; Bruns, J.B.; Hughey, R.P.
gamma-Glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum
Methods Enzymol.
401
426-449
2005
Rattus norvegicus
Kaiser, M.; Mares, V.; Stastny, F.; Bubenikova-Valesova, V.; Lisa, V.; Suchomel, P.; Balcar, V.J.
The influence of interleukin-1beta on gamma-glutamyl transpepidase activity in rat hippocampus
Physiol. Res.
55
461-465
2006
Rattus norvegicus
Pandur, S.; Pankiv, S.; Johannessen, M.; Moens, U.; Huseby, N.E.
Gamma-glutamyltransferase is upregulated after oxidative stress through the Ras signal transduction pathway in rat colon carcinoma cells
Free Radic. Res.
41
1376-1384
2007
Rattus norvegicus
Kaufmann, Y.; Todorova, V.K.; Luo, S.; Klimberg, V.S.
Glutamine affects glutathione recycling enzymes in a DMBA-induced breast cancer model
Nutr. Cancer
60
518-525
2008
Rattus norvegicus (P07314)
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
Rattus norvegicus
Becerra-Torres, S.L.; Rodriguez-Vazquez, M.L.; Medina-Ramirez, I.E.; Jaramillo-Juarez, F.
Potassium dichromate-induced changes on urinary-specific activities of gamma-glutamyl transpeptidase and alanine aminopeptidase enzymes
Drug Chem. Toxicol.
32
21-25
2009
Rattus norvegicus
Wainford, R.D.; Weaver, R.J.; Stewart, K.N.; Brown, P.; Hawksworth, G.M.
Cisplatin nephrotoxicity is mediated by gamma glutamyltranspeptidase, not via a C-S lyase governed biotransformation pathway
Toxicology
249
184-193
2008
Mus musculus, Rattus norvegicus
Nishihara, T.; Yoshihara, H.; Nonaka, H.; Takakusagi, Y.; Hyodo, F.; Ichikawa, K.; Can, E.; Bastiaansen, J.; Takado, Y.; Comment, A.; Sando, S.
Direct monitoring of gamma-glutamyl transpeptidase activity in vivo using a hyperpolarized 13C-labeled molecular probe
Angew. Chem. Int. Ed. Engl.
55
10626-10629
2016
Rattus norvegicus
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