Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694.

@article{Imaoka2010MolecularCA,
  title={Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694.},
  author={Masashi Imaoka and Shigekazu Yano and Masashi Okumura and Takao Hibi and Mamoru Wakayama},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2010},
  volume={74 9},
  pages={1936-9}
}
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.