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. 1996 Aug;64(8):3401–3406. doi: 10.1128/iai.64.8.3401-3406.1996

Characterization of PepB, a group B streptococcal oligopeptidase.

B Lin 1, W F Averett 1, J Novak 1, W W Chatham 1, S K Hollingshead 1, J E Coligan 1, M L Egan 1, D G Pritchard 1
PMCID: PMC174237  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.

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Selected References

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