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Literature summary for 3.4.19.13 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
Search for more literature for 3.4.19.13

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Aspergillus nidulans
-
-

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
-
-
-
Aspergillus nidulans FGSC A26
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
culture condition fermentation broth of carbon stressed cultures Aspergillus nidulans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gamma-glutamyl-p-nitroanilide + H2O the enzyme has low hydrolase activity and high gamma-glutamyl transpeptidase activity Aspergillus nidulans L-glutamate + p-nitroaniline
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Aspergillus nidulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Aspergillus nidulans

General Information

General Information Comment Organism
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