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Literature summary for 2.3.2.2 extracted from

  • Hsu, W.H.; Ong, P.L.; Chen, S.C.; Lin, L.L.
    Contribution of Ser463 residue to the enzymatic and autoprocessing activities of Escherichia coli gamma-glutamyltranspeptidase (2009), Indian J. Biochem. Biophys., 46, 281-288.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
S463D complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391 Escherichia coli
S463K complete loss of activity, impaired autoproteolytic processing, increase in the critical bond distance of residues Q390-T391 Escherichia coli
S463T 40% decrease in ratio kcat/KM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.045
-
5-L-glutamyl-4-nitroanilide wild-type, pH 9.0, 37°C Escherichia coli
0.058
-
5-L-glutamyl-4-nitroanilide mutant S463T, pH 9.0, 37°C Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P18956
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1
-
mutant S463T, pH 9.0, 37°C Escherichia coli
6.8
-
wild-type, pH 9.0, 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-L-glutamyl-4-nitroanilide + Gly-Gly
-
Escherichia coli 4-nitroaniline + 5-L-glutamyl-Gly-Gly
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.49
-
5-L-glutamyl-4-nitroanilide mutant S463T, pH 9.0, 37°C Escherichia coli
0.62
-
5-L-glutamyl-4-nitroanilide wild-type, pH 9.0, 37°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.008
-
5-L-glutamyl-4-nitroanilide mutant S463T, pH 9.0, 37°C Escherichia coli
0.014
-
5-L-glutamyl-4-nitroanilide wild-type, pH 9.0, 37°C Escherichia coli