| Literature DB >> 12892879 |
Hiromichi Minami1, Hideyuki Suzuki, Hidehiko Kumagai.
Abstract
gamma-Glutamyltranspeptidase (GGT) catalyzes the hydrolysis of gamma-glutamyl compounds and the transfer of their gamma-glutamyl moieties to amino acids and peptides. The transpeptidation activity of Bacillus subtilis GGT is about 10-fold higher than its hydrolysis activity. In B. subtilis GGT, substitution of Asp-445 with Ala abolished its transpeptidation activity. The specific activity for hydrolysis of D445A GGT was 40.2% of that of the wild-type GGT. The K(m) value for L-glutamine was 15.3 mM. D445A GGT was salt tolerant like the wild-type GGT. These results indicate that D445A GGT will be highly useful as a 'glutaminase' in food industry.Entities:
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Year: 2003 PMID： 12892879 DOI： 10.1016/S0378-1097(03)00456-7
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN： 0378-1097 Impact factor: 2.742