title: Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694.
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.
authors.affiliation: Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Shiga, Japan.
authors.forename: Masashi
authors.initials: M
authors.lastname: Imaoka
authors.forename: Shigekazu
authors.initials: S
authors.lastname: Yano
authors.forename: Masashi
authors.initials: M
authors.lastname: Okumura
authors.forename: Takao
authors.initials: T
authors.lastname: Hibi
authors.forename: Mamoru
authors.initials: M
authors.lastname: Wakayama
mesh_terms: D000588:Amines / Q000378:metabolism; D000596:Amino Acids; D002384:Catalysis; D003001:Cloning, Molecular / Q000379:methods*; D006868:Hydrolysis; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D000588:Amines; D000596:Amino Acids; D005723:gamma-Glutamyltransferase