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Literature summary extracted from

  • Spitzmüller, Z.; Gonda, S.; Kiss-Szikszai, A.; Vasas, G.; Pocsi, I.; Emri, T.
    Characterization of extracellular gamma-glutamyl transpeptidase from Aspergillus nidulans (2016), Mycoscience, 57, 400-403 .
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.2.2 additional information
-
 additional information Michaelis-Menten kinetics with L-gamma-glutamyl-4-nitroanilide as substrate, native extracellular enzyme Aspergillus nidulans
2.3.2.2 0.2
-
 L-gamma-glutamyl-4-nitroanilide pH 8.0, 37°C, native extracellular enzyme Aspergillus nidulans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.2.2 extracellular
-
 Aspergillus nidulans
-
-
3.4.19.13 extracellular
-
 Aspergillus nidulans
-
-

Natural Substrates/ Products (Substrates)

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 Aspergillus nidulans
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid Aspergillus nidulans FGSC A26
-
 a peptide + a 5-L-glutamyl amino acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.2 Aspergillus nidulans
-
-
-
3.4.19.13 Aspergillus nidulans
-
-
-
3.4.19.13 Aspergillus nidulans FGSC A26
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.2 native extracellular enzyme partially from carbon stressed cultures Aspergillus nidulans

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.2.2 cell culture carbon stressed cultures Aspergillus nidulans
-
3.4.19.13 culture condition fermentation broth of carbon stressed cultures Aspergillus nidulans
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Aspergillus nidulans a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 a (5-L-glutamyl)-peptide + an amino acid
-
 Aspergillus nidulans FGSC A26 a peptide + a 5-L-glutamyl amino acid
-
 ?
2.3.2.2 gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine GSH Aspergillus nidulans L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 gamma-L-glutamyl-L-cysteinyl-glycine + glycylglycine GSH Aspergillus nidulans FGSC A26 L-cysteinyl-glycine + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 glutathione disulfide + glycylglycine GSSG Aspergillus nidulans L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 glutathione disulfide + glycylglycine GSSG Aspergillus nidulans FGSC A26 L-Cys-Gly + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Aspergillus nidulans 4-nitroaniline + 5-L-glutamyl-glycyl-glycine
-
 ?
2.3.2.2 L-gamma-glutamyl-4-nitroanilide + glycylglycine
-
 Aspergillus nidulans FGSC A26 4-nitroaniline + 5-L-glutamyl-glycyl-glycine
-
 ?
2.3.2.2 L-glutamine + glycylglycine
-
 Aspergillus nidulans NH3 + 5-L-glutamyl-glycylglycine
-
 ?
2.3.2.2 additional information the enzyme utilizes Gln, glutathione, and less efficiently oxidized glutathione as gamma-glutamyl donors (beside of gamma-glutamyl-4-nitroanilide) and utilizes amino-acids and peptides (including Glu, Cys, Met, Gly-Gly and Cys-Gly), but not hydroxylamine, as gamma-glutamyl acceptors Aspergillus nidulans ?
-
-
2.3.2.2 additional information the enzyme utilizes Gln, glutathione, and less efficiently oxidized glutathione as gamma-glutamyl donors (beside of gamma-glutamyl-4-nitroanilide) and utilizes amino-acids and peptides (including Glu, Cys, Met, Gly-Gly and Cys-Gly), but not hydroxylamine, as gamma-glutamyl acceptors Aspergillus nidulans FGSC A26 ?
-
-
3.4.19.13 gamma-glutamyl-p-nitroanilide + H2O the enzyme has low hydrolase activity and high gamma-glutamyl transpeptidase activity Aspergillus nidulans L-glutamate + p-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.2 AngammaGT
-
 Aspergillus nidulans
2.3.2.2 gamma-glutamyl transpeptidase
-
 Aspergillus nidulans
2.3.2.2 gammaGT
-
 Aspergillus nidulans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.2 45
-
-
 Aspergillus nidulans
3.4.19.13 45
-
-
 Aspergillus nidulans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.2 8
-
-
 Aspergillus nidulans
3.4.19.13 8
-
-
 Aspergillus nidulans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.2 7 10 no significant activities are detected below pH 7.0 or above pH 10.0 Aspergillus nidulans

General Information

EC Number General Information Comment Organism
2.3.2.2 malfunction deletion of the ggtA (AN10444) encoding a putative gammaGT decreased the gammaGT activities below to the detection limit suggesting that GgtA is the only enzyme possessing significant gammaGT activity under carbon stressed conditions in Aspergillus nidulans Aspergillus nidulans
2.3.2.2 additional information enzyme AngammaGT has little hydrolase activity (cf. EC 3.4.19.13) Aspergillus nidulans
2.3.2.2 physiological function the function of this enzyme is not to degrade, but to produce, gamma-glutamyl compounds, which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures Aspergillus nidulans
3.4.19.13 physiological function it is proposed that the function of this enzyme is not to degrade, but to produce, gamma-glutamyl compounds which may be related to the utilization of extracellular peptides and amino-acids in carbon stressed cultures Aspergillus nidulans