| Literature DB >> 7574624 |
M C Montel1, M P Seronie, R Talon, M Hébraud.
Abstract
A dipeptidase was purified from cell extracts of Lactobacillus sake. This compound was a monomer having a molecular weight of 50,000 and a pI of 4.7 and exhibited broad specificity against all dipeptides except those with proline or glycine at the N terminus. The enzyme was inhibited by EDTA or 1,10-phenanthroline but could be reactivated with CoCl2 and MnCl2.Entities:
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Year: 1995 PMID: 7574624 PMCID: PMC167347 DOI: 10.1128/aem.61.2.837-839.1995
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792