Molecular cloning and characterization of γ-glutamyltranspeptidase from Pseudomonas nitroreducens IFO12694.
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.
Imaoka
Masashi
M
Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Shiga, Japan.
Yano
Shigekazu
S
Okumura
Masashi
M
Hibi
Takao
T
Wakayama
Mamoru
M
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
D000588:Amines; D000596:Amino Acids; D005723:gamma-Glutamyltransferase