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Characterization of PepB, a Group B Streptococcal Oligopeptidase

Characterization of PepB, a Group B Streptococcal Oligopeptidase

B Lin, W F Averett, J Novak, W W Chatham, S K Hollingshead, J E Coligan, M L Egan, D G Pritchard

Infect Immun. 1996 Aug;64(8):3401-6.

PMID: 8757883

Abstract:

Group B streptococci were recently reported to possess a cell-associated collagenase. Although the enzyme hydrolyzed the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala, we found that neither the highly purified enzyme nor crude group B streptococcal cell lysate solubilized a film of reconstituted rat tail collagen, an activity regarded as obligatory for a true collagenase. We cloned and sequenced the gene for the enzyme (pepB). The deduced amino acid sequence showed 66.4% identity to the PepF oligopeptidase from Lactococcus lactis, a member of the M3 or thimet family of zinc metallopeptidases. The group B streptococcal enzyme also showed oligopeptidase activity and degraded a variety of small bioactive peptides, including bradykinin, neurotensin, and peptide fragments of substance P and adrenocorticotropin.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP78832652	N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala		78832-65-2	Price

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