Characterization and properties of an LL-oligopeptidase from sporulating cells of Bacillus sphaericus.
An LL-oligopeptidase was characterized in the cell cytoplasm of sporulating Bacillus sphaericus 9602. Its activity showed a threefold increase throughout sporulation. The enzyme has lytic activity on various LL-dipeptides, especially on dipeptides with N-terminal L-alanine. Lytic activity was also found on some tripeptides and larger peptides which contain the sequence L-Ala-L-Ala. The role of this oligopeptidase in relation to sporulation may be to supply the cell with L-alanine for the biosynthesis of the peptide chains of the spore cortex.
D001407:Bacillus / Q000201:enzymology* / Q000502:physiology; D020689:Exopeptidases; D009842:Oligopeptides; D010447:Peptide Hydrolases / Q000378:metabolism*; D010458:Peptidyl Transferases / Q000378:metabolism; D013171:Spores, Bacterial / Q000201:enzymology; D013379:Substrate Specificity
D009842:Oligopeptides; D010458:Peptidyl Transferases; D020689:Exopeptidases; D010447:Peptide Hydrolases; C028759:oligopeptidase