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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Characterization of PepB, a group B streptococcal oligopeptidase.

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.[1]

References

  1. Characterization of PepB, a group B streptococcal oligopeptidase. Lin, B., Averett, W.F., Novak, J., Chatham, W.W., Hollingshead, S.K., Coligan, J.E., Egan, M.L., Pritchard, D.G. Infect. Immun. (1996) [Pubmed]
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