Open AccessCharacterization and properties of an LL-oligopeptidase from sporulating cells of Bacillus sphaericus
Author(s) -
MarieJeanne Vacheron,
Micheline Guinand,
George Michel
Publication year - 1981
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.145.2.675-680.1981
Subject(s) - biology , tripeptide , oligopeptidase , bacillus sphaericus , cytoplasm , lytic cycle , alanine , biochemistry , peptide sequence , amino acid , enzyme , microbiology and biotechnology , bacillales , bacteria , virology , genetics , virus , bacillus subtilis , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom