title: Characterization of PepB, a group B streptococcal oligopeptidase.
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.
authors: Department of Microbiology, University of Alabama at Birmingham, 35294, USA.
authors: B
authors: B
authors: Lin
authors: W F
authors: WF
authors: Averett
authors: J
authors: J
authors: Novak
authors: W W
authors: WW
authors: Chatham
authors: S K
authors: SK
authors: Hollingshead
authors: J E
authors: JE
authors: Coligan
authors: M L
authors: ML
authors: Egan
authors: D G
authors: DG
authors: Pritchard
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D016133:Polymerase Chain Reaction; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013292:Streptococcus agalactiae / Q000201:enzymology / Q000235:genetics*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; C101033:PepB oligopeptidase, Streptococcus; D010447:Peptide Hydrolases