| Gene Set | Qualifiers | Information Source | Evidence | Pentacon Note |
|---|---|---|---|---|
| AAP | Gold Standard | KEGG: hsa00590 Reactome: REACT_147851.3 |
21447318|E |
Kinetic analysis of GGT1 and GGT5 using LTC4 as a substrate, includes kinetic information |
| Function | Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive. PubMed UniProt |
| Isoforms |
3 isoform(s):
Isoform 1;
Isoform 2;
Isoform 3;
UniProt |
| Natural variants |
6 in vivo variant(s): V435A; In dbSNP: rs16986465 N419D; In dbSNP: rs17004876 S51L; In dbSNP: rs2330837 K52E; In dbSNP: rs2330838 A177V; In dbSNP: rs3895576 V272A; In dbSNP: rs4049829 UniProt |
| Mutagenesis sites |
22 in vitro variant(s): C454A; No effect on activity. D422A; Reduces enzyme activity by 90%. D423A; Abolishes enzyme activity. Increases KM by over 1000-fold. E102Q; No effect on activity. E108Q; Reduces enzyme activity by 98%. H383A; Reduces enzyme activity by 66%. H505A; Reduces enzyme activity by 90%. K100N; No effect on activity. R107{QH}; Abolishes enzyme activity. R107K; Reduces enzyme activity by 99%. R112Q; No effect on activity. R139Q; No effect on activity. R147Q; No effect on activity. R150Q; No effect on activity. S385A; No effect on activity. S413A; No effect on activity. S425A; No effect on activity. S451A; Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452. S452A; Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451. E193Y; Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with W-192. Q545K; Reduces enzyme activity by 97%. C192W; Loss of autocatalytic cleavage, cell membrane localization and decrease in catalytic activity; when associated with Y-193. UniProt |
| Tissues/Cell Types |
bile [BTO:0000121];
blood [BTO:0000089];
intestine [BTO:0000648];
kidney [BTO:0000671];
liver [BTO:0000759];
lung [BTO:0000763];
lymph [BTO:0000855];
mammary gland [BTO:0000817];
pancreas [BTO:0000988];
placenta [BTO:0001078];
stomach [BTO:0001307];
UniProt |
| Localization |
plasma membrane [GO:0005886];
UniProt |
| Diseases |
amino acid metabolic disorder [DOID:9252];
gamma-Glutamyltransferase deficiency [SNOMEDCT:78586005];
UniProt |
| Orthologs | Ggt1 (Mus musculus)i, Ggt1 (Rattus norvegicus)i, ggt1a (Danio rerio)i, ggt1b (Danio rerio)i, ECM38 (Saccharomyces cerevisiae)i, |
| Pentacon Resources | AAP Figure, NSAIDnet, GIANT |
| Protein and Genetic Interaction: | BioGRID |
| CRISPR Screens | BioGRID ORCS CRISPR Screen Phenotypes |
| Data Type | Value | ChEBI Term A | ChEBI Term B | 1° Note | 1° Source | 2° Source |
|---|---|---|---|---|---|---|
| 0.008 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | water [CHEBI:15377] | <67> Ikeda, Y.; Fujii, J.; Taniguchi, N.: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J. Biochem. (1996) 119, 1166-1170. {Pubmed:8827453}; PENTACON Notes: Request ChEBI ID:L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:8827453 | Brenda | |
| KM | 12.4 mM | glycylglycine [CHEBI:17201] | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | <45> Huseby, N.: Purification and some properties of gamma-glutamyltransferase from human liver. Biochim. Biophys. Acta (1977) 483, 46-56. {Pubmed:18197}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:18197 | Brenda |
| KM | 0.81 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | <45> Huseby, N.: Purification and some properties of gamma-glutamyltransferase from human liver. Biochim. Biophys. Acta (1977) 483, 46-56. {Pubmed:18197}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:18197 | Brenda |
| KM | 1.5 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | <46> Indirani, N.; Hill, P.G.: Partial purification and some properties of gamma-glutamyl transpeptidase from human bile. Biochim. Biophys. Acta (1977) 483, 57-62. {Pubmed:18198}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Enzyme was purified from bile and not recombinant | PubMed:18198 | Brenda | |
| KM | 1.09 mM | L-Glu-3-carboxy-4-nitroanilide [CHEBI:NONE_148559] | <1> Yoshida, K.I.; Arai, K.; Kobayashi, N.; Saitoh, H.: Purification and properties of gamma-glutamyl transpeptidase from human testis. Andrologia (1990) 22, 239-246. {Pubmed:}; PENTACON Notes: Request ChEBI ID: gamma-glutamyl-3-carboxy-4-nitroanilide: CID 104545; Not a rat kidney enzyme as indicated in Secondary Source Notes, but a GGT isolated from human testis, results consistent with GGT1 | PubMed:1978610 | Brenda | |
| KM | 0.8 mM | gamma-L-Glutamyl-p-nitroanilide [CHEBI:NONE_148541] | glycylglycine [CHEBI:17201] | Added by PENTACON; PENTACON Notes: Request ChEBI ID: gamma-L-Glutamyl-p-nitroanilide: CID 16219428 | PubMed:4442 | Pentacon |
| KM | 3.4 mM | glycylglycine [CHEBI:17201] | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | <65> 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 (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Mutant:deltaSign | PubMed:7816801 | Brenda |
| KM | 2.1 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | <65> 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 (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Mutant:deltaSign | PubMed:7816801 | Brenda |
| KM | 2.9 mM | glycylglycine [CHEBI:17201] | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | <65> 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 (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; Human protein, not from rat kidney as indicated in Secondary Source notes. | PubMed:7816801 | Brenda |
| KM | 1.5 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | <65> 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 (1995) 92, 126-130. {Pubmed:7816801}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:7816801 | Brenda |
| KM | 10.0 mM | glycylglycine [CHEBI:17201] | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | Added by PENTACON; PENTACON Notes: recombinant wild-type, transpeptidation | PubMed:8827453 | Pentacon |
| KM | 1.4 mM | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | <67> Ikeda, Y.; Fujii, J.; Taniguchi, N.: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J. Biochem. (1996) 119, 1166-1170. {Pubmed:8827453}; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:8827453 | Brenda |
| Vmax | 640.0 umol/min/mg | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:7816801 | Pentacon |
| Vmax | 1100.0 umol/min/mg | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855 | PubMed:7816801 | Pentacon |
| Vmax | 5.5 umol/min/mg | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | water [CHEBI:15377] | Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; hydrolysis reaction | PubMed:8827453 | Pentacon |
| Vmax | 1200.0 umol/min/mg | L-Glutamic acid gamma-(4-nitroanilide) [CHEBI:NONE_148551] | glycylglycine [CHEBI:17201] | Added by PENTACON; PENTACON Notes: Request ChEBI ID: L-Glutamic acid gamma-(4-nitroanilide): CID 57369855; transpeptidation | PubMed:8827453 | Pentacon |
