Molecular Cloning and Characterization of γ-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694

gamma-Glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694 (PnGGT) exhibited higher hydrolytic activity than transfer activity, as compared with other gamma-glutamyltranspeptidases (GGTs). PnGGT showed little activity towards most of L-amino acids and towards glycyl-glycine, which is often used as a standard gamma-glutamyl accepter in GGT transfer reactions. The preferred substrates for PnGGT as a gamma-glutamyl accepter were amines such as methylamine, ethylamine, and isopropylamine.