MISC

1998年8月

Bacteriolytic activity and specificity of Achromobacter beta-lytic protease

JOURNAL OF BIOCHEMISTRY
  • SL Li
  • ,
  • S Norioka
  • ,
  • F Sakiyama

124
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.

Web of Science ® 被引用回数 : 27

リンク情報
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000075449500013&DestApp=WOS_CPL