Journal
FEMS MICROBIOLOGY LETTERS
Volume 224, Issue 2, Pages 169-173Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0378-1097(03)00456-7
Keywords
gamma-glutamyltranspeptidase; hydrolysis; glutaminase; site-directed mutagenesis; salt tolerant; Bacillus subtilis
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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 wildtype GGT. These results indicate that D445A GGT will be highly useful as a 'glutaminase' in food industry. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
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