An aminopeptidase P from Lactococcus lactis with original specificity
Biochimica et Biophysica Acta (BBA) - General Subjects, ISSN: 0304-4165, Vol: 1243, Issue: 2, Page: 209-215
1995
- 33Citations
- 8Captures
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Metrics Details
- Citations33
- Citation Indexes33
- 33
- CrossRef27
- Captures8
- Readers8
Article Description
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 Mn 2+ and inhibited by DTT. It differs from the majority of aminopeptidases P already described by displaying a specificity for X-Pro-Pro N-termini and probably an extended binding site that could accommodate amino acid residues beyond the P′2 position of the substrate.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/030441659400028V; http://dx.doi.org/10.1016/0304-4165(94)00028-v; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0028836016&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/7873564; http://linkinghub.elsevier.com/retrieve/pii/030441659400028V; http://api.elsevier.com/content/article/PII:0304-4165(94)00028-V?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:0304-4165(94)00028-V?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/030441659400028V; http://dx.doi.org/10.1016/0304-4165%2894%2900028-v; https://dx.doi.org/10.1016/0304-4165%2894%2900028-v
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