| Literature DB >> 7873564 |
Abstract
An aminopeptidase P (E.C. 3.4.11.9) that cleaves the Arg-1-Pro-2 bond of bradykinin has been isolated for the first time from Lactococcus lactis. The peptidase was purified to homogeneity in a 3-step procedure and characterized. It is a monomeric metalloenzyme with a 43 kDa molecular mass, activated by Mn2+ and inhibited by DTT. It differs from the majority of aminopeptidases P already described by displaying a specificity for X-Pro-Pro N-terminal and probably an extended binding site that could accommodate amino acid residues beyond the P'2 position of the substrate.Entities:
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Year: 1995 PMID： 7873564 DOI： 10.1016/0304-4165(94)00028-v
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002