| Literature DB >> 20834145 |
Masashi Imaoka1, Shigekazu Yano, Masashi Okumura, Takao Hibi, Mamoru Wakayama.
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.Entities:
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Year: 2010 PMID： 20834145 DOI： 10.1271/bbb.100199
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN： 0916-8451 Impact factor: 2.043