Vacheron M J, Guinand M, Michel G
J Bacteriol. 1981 Feb;145(2):675-80. doi: 10.1128/jb.145.2.675-680.1981.
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.
在球形芽孢杆菌9602的芽孢形成细胞质中鉴定出一种LL-寡肽酶。其活性在整个芽孢形成过程中增加了三倍。该酶对各种LL-二肽具有裂解活性,特别是对N端为L-丙氨酸的二肽。在一些含有L-Ala-L-Ala序列的三肽和更大的肽上也发现了裂解活性。这种寡肽酶在芽孢形成中的作用可能是为细胞提供L-丙氨酸,用于芽孢皮层肽链的生物合成。