1998年8月
Bacteriolytic activity and specificity of Achromobacter beta-lytic protease
JOURNAL OF BIOCHEMISTRY
- ,
- ,
- 巻
- 124
- 号
- 2
- 開始ページ
- 332
- 終了ページ
- 339
- 記述言語
- 英語
- 掲載種別
- 出版者・発行元
- JAPANESE BIOCHEMICAL SOC
Achromobacter beta-lytic protease (blp), one of the bacteriolytic proteases secreted by Achromobacter lyticus, exhibited both peptidase and bacteriolytic activities at alkaline pH. The protease was strongly inhibited by 1,10-phenanthroline, and one zinc atom was detected in the molecule by ion-spray mass spectrometry. The zinc-protease specifically cleaved Gly-X bonds in peptides and possibly possessed subsites S2, S1, S1', and S2' for binding substrate [Schecter, I. and Berger, A. (1967) Biochem. Biophys, Res. Commun. 27, 1.57-1.62]. Blp lysed Staphylococcus aureus and Micrococcus luteus cells more efficiently than Achromobacter alpha-lytic protease (alp) and lysozyme, thus being responsible for the high bacteriolytic activity of A. lyticus. In the lysis of bacterial cell walls, blp hydrolyzed both the D-Ala-Gly/Ala bond at the linkage between the peptide subunit and the interpeptide and the Gly-Gly bond in the interpeptide bridge, These results indicate that blp is a highly active bacteriolytic enzyme with a broad bacteriolytic spectrum, which acts primarily by splitting the linkage between the peptide subunit and the interpeptide in the peptidoglycan.
- リンク情報
- ID情報
-
- ISSN : 0021-924X
- Web of Science ID : WOS:000075449500013