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Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694
Masashi Imaoka1, Shigekazu Yano, Masashi Okumura
1Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Shiga, Japan.
Abstract:
γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydrolytic activity than transfer activity, as compared with other γ-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard γ-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a γ-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.
