2.3.2.2: gamma-glutamyltransferase
This is an abbreviated version!
For detailed information about gamma-glutamyltransferase, go to the full flat file.
Word Map on EC 2.3.2.2
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2.3.2.2
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aminotransferase
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alt
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bilirubin
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cholesterol
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albumin
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triglyceride
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bile
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biliary
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women
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creatinine
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gsh
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transaminase
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hepatocytes
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cirrhosis
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fibrosis
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urinary
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cholestasis
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duct
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uric
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c-reactive
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steatosis
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aminopeptidase
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jaundice
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drinkers
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hepatotoxicity
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non-alcoholic
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intrahepatic
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nafld
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nephrotoxicity
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ursodeoxycholic
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waist
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ultrasonography
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diethylnitrosamine
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circumference
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corpuscular
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hepatocarcinogenesis
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abuse
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hepatectomy
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hepatobiliary
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phenobarbital
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preneoplastic
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alpha-fetoprotein
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homa-ir
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abstinence
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pruritus
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2-acetylaminofluorene
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n-acetyl-beta-d-glucosaminidase
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cholangitis
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cholangiopancreatography
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pharmacology
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elastography
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diagnostics
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nutrition
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food industry
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drug development
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analysis
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medicine
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synthesis
- 2.3.2.2
- aminotransferase
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alt
- bilirubin
- cholesterol
- albumin
- triglyceride
- bile
- biliary
- women
- creatinine
- gsh
- transaminase
- hepatocytes
- cirrhosis
- fibrosis
- urinary
- cholestasis
- duct
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uric
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c-reactive
- steatosis
- aminopeptidase
- jaundice
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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
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n-acetyl-beta-d-glucosaminidase
- cholangitis
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cholangiopancreatography
- pharmacology
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elastography
- diagnostics
- nutrition
- food industry
- drug development
- analysis
- medicine
- synthesis
Reaction
Synonyms
(5-L-glutamyl) peptide: amino-acid 5-glutamyl transferase, alpha-glutamyl transpeptidase, AngammaGT, AsGGT1, At1g69820, At4g29210, At4g39640, At4g39650, BaGGT, BaGGT42, BaGGT469, BlGGT, BlGGT13, BsGGT168, Cgl0954, eqGGT, gamma glutamyl transferase, gamma-glutamyl peptidyltransferase, gamma-glutamyl transferase, gamma-glutamyl transferase 1, gamma-glutamyl transferase 5, gamma-glutamyl transferase/transpeptidase, gamma-glutamyl transferases, gamma-glutamyl transpeptidase, gamma-glutamyl transpeptidase 1, gamma-glutamyl transpeptidase 4, gamma-glutamyl transpeptidase-1, gamma-glutamyl-transpeptidase, gamma-glutamyltransferase, gamma-glutamyltranspeptidase, gamma-GPT, gamma-GT, gamma-GTase, gamma-GTP, gammaGT, GGT, GGT A, GGT I, GGT-1, GGT1, GGT2, GGT3, GGT4, GGT5, ggtB, GGTII protein, GGTLA1, glutamyl transpeptidase, glutamyltransferase, gamma-, HGGT, L-gamma-glutamyl transpeptidase, L-gamma-glutamyltransferase, L-glutamyltransferase, More, PnGGT, SBLGGT, VvGGT3
ECTree
2.3.2.2 gamma-glutamyltransferaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.3.2.2 - gamma-glutamyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2RS,RPSP)-2-amino-4-[(3-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[(4-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[bis[(3-carboxymethy)lphenoxy]phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[[3-(2-carboxyethyl)phenoxy](methoxy)phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[[3-(carbamoylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[[3-(ethoxycarbonylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid
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(2RS,RPSP)-2-amino-4-[[3-nitrophenoxy](methoxy)phosphoryl]butanoic acid
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(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl)butanoic acid
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competitive
(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)sulfonyl)butanoic acid
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(2S)-2-amino-4-((3-((carboxymethyl)amino)-3-oxopropyl)thio)butanoic acid
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competitive
(2S)-2-amino-4-((4-(((carboxymethyl)amino)carbonyl)benzyl)sulfinyl)butanoic acid
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competitive
1,10-phenanthroline
slight inhibition of free and immobilized enzyme
1,2,3,4-tetrahydroisoquinoline
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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-[(3-((carboxymethyl)amino)-3-oxopropyl)sulfinyl]butanoic acid
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2-mercaptoethanol
slight inhibition of free and immobilized enzyme
5-(L-gamma-glutamylamino)-2-nitrobenzoic acid
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enzyme from human tissues, not serum
6-diazo-4 oxonorleucine
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
brefeldin A
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inhibition of recombinant mutant enzyme secretion into cell culture medium from Sf21 cells, accumulation in the cells
Cd2+
inhibits the free enzyme by about 75% and the immobilized enzyme by about 20% at 5 mM
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
iodoacetic acid
slight inhibition of free and immobilized enzyme
N-[5-(4-methoxybenzyl)-1,3,4-thiadiazol-2-yl]benzenesulfonamide
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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
phenylmethylsulfonyl fluoride
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
tosyl fluoride
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inhibition by tosyl fluoride only in presence of maleate
Urea
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complete inactivation of wild-type and mutant at 6 M, low activity at 4 M
(2S)-2-amino-2-[(5S)-3-chloro-4,5-dihydro-1,2-oxazol-5-yl]acetic acid
i.e. acivicin
(2S)-2-amino-2-[(5S)-3-chloro-4,5-dihydro-1,2-oxazol-5-yl]acetic acid
i.e. acivicin
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 610/per mol * s
2-amino 4-[4-chlorophenyl(methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 5.0/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 120/per mol * s
2-amino 4-[methyl(phenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 0.4/per mol * s
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop, weak inhibition, structure-activity relationship, Escherichia coli enzyme GGT in complex with the inhibitor, Lys562 is the probable residue for the recognition of negative charge at C-terminal of GGsTop
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop. GGsTop shows no cytotoxicity toward human fibroblasts and hepatic stellate cells up to 1 mM. GGsTop serves as a non-toxic, selective and highly potent irreversible GGT inhibitor that can be used for various in vivo as well as in vitro biochemical studies. Lys562 of human GGT is the key residue for the recognition of the negatively charged GGsTop. The active site Lys562 of human GGT enhances the inhibitory activity of GGsTop by 128fold. GGsTop does not induce cytotoxicity for mammalian cells at up to 1 mM
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
i.e. GGsTop, a potent and selective, nontoxic, and irreversible inhibitor of human gamma-glutamyl transpeptidase. GGsTop consists of four stereoisomers due to the presence of two stereogenic centers, i.e. the alpha-carbon atom of the glutamate mimic (L/D) and the phosphorus atom (RP/SP), stereoselective synthesis of the 4 isomers. With respect to the configuration of the alpha-carbon atom of the glutamate mimic, the L-isomer is about 8fold more potent than the D-isomer. In contrast, the configuration of the phosphorus atom is critical for GGT inhibitory activity. Based on a molecular modeling approach, the absolute configuration of the phosphorus atom of the active GGsTop isomers is postulated to be SP. The SP-isomers inhibits human GGT, while the RP-isomers are inactive even at concentrations of 0.1 mM
2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid
peptidyl phosphonate inhibitor GGsTop, the hydroxy-2-oxoethylamino-oxidanylidene-butane moiety of the inhibitor mimicks an acceptor substrate
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
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second-order rate constant for enzyme inactivation is 19/per mol * s
2-amino-4-[(4-methoxyphenyl)(methyl)phosphono]-butanoic acid
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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
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second-order rate constant for enzyme inactivation is 80/per mol * s
2-amino-4-[1-[N-(carboxymethyl)carbamoyl]propyl(phenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 75/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 12000/per mol * s
2-amino-4-[4-cyanophenyl(methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 46/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 24/per mol * s
2-amino-4-[methyl(4-methylphenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 0.24/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 16000/per mol * s
2-amino-4-[methyl(4-methylumbelliferyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 2400/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 35000/per mol * s
2-amino-4-[methyl(4-nitrophenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 130/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 2900/per mol * s
2-amino-4-[methyl(4-trifluoromethylphenyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 12/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 150/per mol * s
2-amino-4-[[3-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 51/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 210/per mol * s
2-amino-4-[[4-(carboxymethyl)phenyl](methyl)phosphono]butanoic acid
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second-order rate constant for enzyme inactivation is 0.33/per mol * s
4-nitroaniline
strong, competitive against glutathione
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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methionine protects in vivo; transpeptidation, competitive to the glutamyl-donor, kinetics
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, isolated from Penicillium oxalicum
5-L-glutamyl-2-(2-carboxyphenyl)hydrazine
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i.e. anthglutin, strong, in vivo and in vitro, p-derivative less effective
5-thiohistidine
50% inhibition at 0.015 mM, mechanism of 5-thio driven inhibition of GGT, overview. Reversible inhibition mechanism
6-diazo-5-oxo-L-norleucine
i.e. DON, irreversible inhibition 50% inhibition at 0.282 mM
6-diazo-5-oxo-L-norleucine
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complete inactivation, accelerated by maleate, prevented by S-methylglutathione; i.e. DON, strong, irreversible modification of glutamyl-binding site of light subunit; maleate accelerates inactivation; S-methylglutathione
6-diazo-5-oxo-L-norleucine
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5-glutamyl-donor, protect transpeptidase and hydrolase activity, not 5-carbon derivative; i.e. DON, strong, irreversible modification of glutamyl-binding site of light subunit
6-diazo-5-oxo-L-norleucine
i.e. DON, a glutamate analogue, irreversible inhibitor of hGGT1, but also inhibits many essential glutamine metabolizing enzymes rendering it too toxic for use in the clinic as a GGT1 inhibitor. Binding structure analysis with human gamma-glutamyl transpeptidase 1, and molecular mechanism of hGGT1 inactivation by DON, overview. The crystal structure of DON-inactivated hGGT1 contains a molecule of DON without the diazo-nitrogen atoms in the active site. The overall structure of the hGGT1-DON complex resembles the structure of the apo-enzyme. The structure of hGGT1-DON complex reveals two covalent bonds between the enzyme and inhibitor which are part of a six membered ring. The ring includes the OG atom of Thr381, the reactive nucleophile of hGGT1 and the alpha-amine of Thr381. The mechanism of inactivation by DON differs from its inactivation of other glutamine metabolizing enzymes
6-diazo-5-oxo-L-norleucine
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irreversible inactivation of pancreatic enzyme, S-methylglutathione prevents at 10 mM, maleate increases inhibition at 0.25-1 M
acivicin
i.e. L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
acivicin
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the inhibitors can enhance cytostatic action of doxorubicin and cisplatin, which may permit clinicians to decrease their doses thereby alleviating side effects
acivicin
i.e. L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
azaserine
1 mM, complete inhibition of hydrolysis of gamma-L-glutamyl-4-nitroanilide
Co2+
inhibits the free enzyme by about 70% and the immobilized enzyme by about 15% at 5 mM
ergothioneine
a natural trimethyl-2-thiohistidine, 50% inhibition at 0.297 mM. Reversible inhibition mechanism
ergothioneine
a natural trimethyl-2-thiohistidine, reversible inhibition mechanism
glycylglycine
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high concentration, with L-Glu-4-nitroanilide, not glutathione as donor
iodoacetamide
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inhibition of transpeptidase reaction is more efficient than that of autotranspeptidase reaction
L- or D-Serine/borate
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formation of a tetrahedral complex at the active site
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L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazolacetic acid
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i.e. acivicin; in vivo inhibition and accumulation of glutathione; kinetics; strong, irreversible, reacts with glutamyl binding site
L-(alphaS,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazolacetic acid
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i.e. acivicin; strong, irreversible, reacts with glutamyl binding site
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
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i.e. AT-125; strong, irreversible, 1 mM
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
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i.e. AT-125; strong, irreversible
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
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i.e. AT-125; strong, irreversible
L-(alphaS,5S)-alpha-Amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid
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i.e. AT-125; strong, irreversible
L-azaserine
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irreversible inactivation; not 5-carbon derivative; transpeptidase and hydrolase reaction, glutamyl-donor protects
NaCl
about 45% inhibition of the free enzyme at 2-18% w/v NaCl, about 20% inhibition of the immobilized enzyme
NaCl
at 10% NaCl, GgtBCg still retains 70% of its initial activity. Further addition of NaCl to concentrations of 15%, 20%, and 22.5% reduces the activity to 30%, 27%, and 20%, respectively. For all tested salt concentrations, activity is higher in the presence of glycyl-glycine than in its absence
Ni2+
inhibits the free enzyme by about 25% and the immobilized enzyme by about 20% at 5 mM
Pb2+
inhibits the free enzyme by about 65% and the immobilized enzyme by about 25% at 5 mM
Phenobarbital
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active site-directed, irreversible inactivation, optimal at pH 9.0, serine/borate or GSH protects, maleate protects slightly, kinetics
serine-borate
10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity; 10 mM serine-borate inhibits enzyme activity
serine-borate
competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5; competitive inhibitor which is 8fold more potent in inhibiting isoform GGT1 than in inhibiting isoform GGT5
Thiobarbituric acid
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active site-directed, irreversible inactivation, optimal at pH 9.5, serine/borate or GSH protects, maleate protects slightly, kinetics
Zn2+
inhibits the free enzyme by about 85% and the immobilized enzyme by about 5% at 5 mM
additional information
immobilized enzyme CMS-GGT is 10-20% less susceptibile to inhibition by PMSF, N-bromosuccinamide and GGT specific inhibitors azaserine and 6-diazo-5-oxo-L-norleucine as compared to free enzyme
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additional information
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inhibition by diverse amino acids, overview
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additional information
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L-threonine is a poor gamma-glutamyl acceptor but facilitates the generation of gamma-Glu-Gln-[13C10], whereas L-phenylalanine is a good gamma-glutamyl acceptor but seemed to suppress the generation of gamma-Glu-Gln-[13C10], indicating an inhibitory effect as reported for glutathione
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additional information
identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON). Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
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additional information
no inhibition of recombinant enzyme by 200 mM L-glutamylhydrazine
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additional information
evaluation of a phosphonate-based irreversible inhibitor, 2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid (GGsTop) and its analogues as a mechanism-based inhibitor of human GGT. GGsTop is a stable compound, but inactivates the human enzyme significantly faster than the other phosphonates, and importantly does not inhibit a glutamine amidotransferase. Structure-activity relationships, overview
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additional information
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evaluation of a phosphonate-based irreversible inhibitor, 2-amino-4-([3-(carboxymethyl)phenoxy](methoyl)phosphoryl)butanoic acid (GGsTop) and its analogues as a mechanism-based inhibitor of human GGT. GGsTop is a stable compound, but inactivates the human enzyme significantly faster than the other phosphonates, and importantly does not inhibit a glutamine amidotransferase. Structure-activity relationships, overview
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additional information
synthesis and evaluation of the inhibitory activity of the four stereoisomers of inhibitor GGsTop, binding structures of RP-isomer of L-GGsTop and of the SP-isomer of L-GGsTop to GGT active site, modeling, overview
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additional information
identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON), and are not toxic for human embryonic cells. Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
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additional information
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identification of ovothiols, 5(NPi)-methyl-thiohistidines of marine origin, as non-competitive-like inhibitors of GGT that are more potent than the GGT inhibitor, 6-diazo-5-oxo-L-norleucine (DON), and are not toxic for human embryonic cells. Interactions of 5-thiohistidines with enzyme GGT by molecular docking analysis and comparison with ergothioneine (a natural trimethyl-2-thiohistidine), physiological substrate glutathione, and DON inhibitor, overview. No inhibition by DTT
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additional information
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no inhibition by arsenite, citrate, cyanide and borate
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additional information
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not affected by Ni2+, K+, phtalate, pyruvate and fumarate
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additional information
the enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of most of divalent cations like Ba2+, Ca2+, Co2+, Cd2+, Fe2+, Hg2+, Mg2+, Mn2+ and Zn2+. The enzyme retains more than 90% of the gamma-L-glutamyl-4-nitroanilide hydrolase activity in the presence of 10 mM chelating agents like EDTA, EGTA and 1,10-phenanthroline and is not inhibited by N-bromosuccinimide and iodoacetic acid. Reducing agents like dithiothreitol and 2-mercaptoethanol have no significant effect on the activity
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additional information
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no inhibition by phorbol ester, polyamines, cAMP
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additional information
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no inhibition: 2-amino-3-(S-methylsulfonimidoyl)propanoic acid, 2-amino-4-(methylsulfonyl)butanoic acid, 5-hydroxy-DL-lysine
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additional information
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not affected by KCl, KNO3, KBr, NaCl, CaCl2, MgCl2, MnCl2, CoCl2, ZnCl2, DTT, EDTA
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