EC Number | Application | Comment | Organism |
---|---|---|---|
3.4.19.13 | pharmacology | the enzyme is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target | Homo sapiens |
3.4.19.13 | pharmacology | the enzyme is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target | Escherichia coli |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.2.2 | gene ggt, recombinant expression of wild-type and K562S mutant enzymes in Spodoptera frugiperda Sf9 cells via baculovirus transfection method | Homo sapiens |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.19.13 | X-ray crystallography of the enzyme in complex with inhibitor 2-amino-4-[[3-(carboxymethyl)phenoxy](methoyl)phosphoryl] butanoic acid | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.2.2 | 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 | Homo sapiens |
2.3.2.2 | K568S | site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type | Homo sapiens |
2.3.2.2 | additional information | the N-terminal anchor domain of enzyme GGT is truncated, human GGT protein without the 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. The wild-type human GGT is expressed as a mature protein by autocatalytic processing during the period of infection. The autocatalytic process of K562S mutant is somewhat slow and is not enough under the same conditions, but the successful processing is attained by giving additional processing period for the purification step | Homo sapiens |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.3.2.2 | (2RS,RPSP)-2-amino-4-(diphenoxyphosphoryl)butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[(3-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[(4-carboxyphenoxy)(methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[bis[(3-carboxymethy)lphenoxy]phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[[3-(2-carboxyethyl)phenoxy](methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[[3-(carbamoylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[[3-(ethoxycarbonylmethyl)phenoxy](methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | (2RS,RPSP)-2-amino-4-[[3-nitrophenoxy](methoxy)phosphoryl]butanoic acid | - |
Homo sapiens | |
2.3.2.2 | 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 | Escherichia coli | |
2.3.2.2 | 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 | Homo sapiens | |
2.3.2.2 | acivicin | - |
Escherichia coli | |
2.3.2.2 | acivicin | - |
Homo sapiens | |
2.3.2.2 | 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 | Homo sapiens | |
3.4.19.13 | 2-amino-4-[[3-(carboxymethyl)phenoxy](methoxy)phosphoryl] butanoic acid | the mechanism-based inhibitor | Escherichia coli | |
3.4.19.13 | 2-amino-4-[[3-(carboxymethyl)phenoxy](methoxy)phosphoryl] butanoic acid | the mechanism-based inhibitor is a stable compound. It inactivates the human enzyme significantly faster than the other phosphonates, and does not inhibit a glutamine amidotransferase. The inhibitor shows no cytotoxicity toward human fibroblasts and hepatic stellate cells up to 1 mM. It serves as a non-toxic, selective and highly potent irreversible inhibitor that can be used for various in vivo as well as in vitro biochemical studies. Critical electrostatic interaction between the terminal carboxylate of the inhibitor and the active-site residue Lys562 of human enzyme for potent inhibition | Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.3.2.2 | extracellular | - |
Homo sapiens | - |
- |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Homo sapiens | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Escherichia coli | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | Escherichia coli K12 | - |
a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | additional information | Homo sapiens | GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation) | ? | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.2 | Escherichia coli | P18956 | - |
- |
2.3.2.2 | Homo sapiens | P19440 | - |
- |
3.4.19.13 | Escherichia coli | P18956 | - |
- |
3.4.19.13 | Escherichia coli K12 | P18956 | - |
- |
3.4.19.13 | Homo sapiens | P19440 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Homo sapiens | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Escherichia coli | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | a (5-L-glutamyl)-peptide + an amino acid | - |
Escherichia coli K12 | a peptide + a 5-L-glutamyl amino acid | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycine methylester | very low activity | Homo sapiens | 4-nitroaniline + 5-L-glutamyl-glycyl methylester | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine | - |
Homo sapiens | 4-nitroaniline + 5-L-glutamyl-glycylglycine | - |
? | |
2.3.2.2 | L-gamma-glutamyl-4-nitroanilide + glycylglycine methylester | low activity | Homo sapiens | 4-nitroaniline + 5-L-glutamyl-glycylglycine methylester | - |
? | |
2.3.2.2 | additional information | GGT is an extracellular enzyme and catalyzes the cleavage of the gamma-glutamyl amide bond of glutathione by a modified ping-pong mechanism via a gamma-glutamyl-enzyme ester intermediate to transfer the c-glutamyl group to water (hydrolysis) or amino acids and peptides (transpeptidation) | Homo sapiens | ? | - |
- |
|
2.3.2.2 | additional information | GGT not only catalyzes the transfer of gamma-glutamyl group of gamma-Glu-PNA to acceptors, but also hydrolyzes the gamma-glutamyl bond of gamma-Glu-PNA to give glutamate and 4-nitroaniline (EC 3.4.19.13) | Homo sapiens | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.2.2 | heterodimer | - |
Homo sapiens |
2.3.2.2 | heterodimer | - |
Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.2 | gamma-glutamyl transpeptidase | - |
Homo sapiens |
2.3.2.2 | gamma-glutamyl transpeptidase | - |
Escherichia coli |
2.3.2.2 | GGT | - |
Homo sapiens |
2.3.2.2 | GGT | - |
Escherichia coli |
2.3.2.2 | More | cf. EC 3.4.19.13 | Homo sapiens |
3.4.19.13 | gamma-glutamyl transpeptidase | - |
Homo sapiens |
3.4.19.13 | gamma-glutamyl transpeptidase | - |
Escherichia coli |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.2.2 | additional information | - |
additional information | inhibition kinetics, overview | Homo sapiens | |
2.3.2.2 | additional information | - |
additional information | inhibition kinetics, overview | Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.2.2 | 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 | Homo sapiens |
2.3.2.2 | physiological function | gamma-glutamyl transpeptidase (GGT) catalyzes the hydrolysis (EC 3.4.19.13) and transpeptidation of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione metabolism | Homo sapiens |