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Literature summary extracted from

  • 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 (2011), J. Biol. Chem., 286, 28876-28888.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.2 expressed in Pichia pastoris and in HEK-293 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.2 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 Homo sapiens
2.3.2.2 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 Homo sapiens
2.3.2.2 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 Homo sapiens
2.3.2.2 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 Homo sapiens
2.3.2.2 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 Homo sapiens
2.3.2.2 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 Homo sapiens
2.3.2.2 N95Q the mutation results in an 8fold decrease in the cleavage efficiency of the propeptide Homo sapiens
2.3.2.2 N95Q/N120Q/N230Q/N266Q/N297Q/N344Q/N511Q total N-glycosylation knock-out mutant Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 1.1
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N266Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.2
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N95Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N120Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N230Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N297Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N344Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide mutant enzyme N511Q, at 37°C, pH 7.4 Homo sapiens
2.3.2.2 1.3
-
 5-L-glutamyl-4-nitroanilide wild type enzyme, at 37°C, pH 7.4 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 membrane
-
 Homo sapiens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.2 22000
-
 1 * 64000 + 1 * 22000, SDS-PAGE Homo sapiens
2.3.2.2 64000
-
 1 * 64000 + 1 * 22000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.2 additional information Homo sapiens in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Homo sapiens P19440
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.2 glycoprotein autocatalytic cleavage of human gamma-glutamyl transpeptidase is highly dependent on N-glycosylation at asparagine 95. The large subunit of the enzyme contains six N-glycosylation sites (Asn-95, -120, -230, -266, -297, and -344), and the small subunit contains a single site (Asn-511) Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Homo sapiens 5-L-glutamyl-glycylglycine + 4-nitroaniline
-
 ?
2.3.2.2 additional information in vivo, the primary reaction catalyzed by gamma-glutamyl transpeptidase is the hydrolysis reaction, in which water, rather than amino acids, acts as the acceptor molecule during the cleavage of the gamma-glutamyl bond of glutathione Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.2 heterodimer 1 * 64000 + 1 * 22000, SDS-PAGE Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 gamma-glutamyl transpeptidase
-
 Homo sapiens
2.3.2.2 GGT
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.2.2 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 Homo sapiens