MISC

1997年10月

Purification, staphylolytic activity, and cleavage sites of alpha-lytic protease from Achromobacter lyticus

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

122
4
開始ページ
772
終了ページ
778
記述言語
英語
掲載種別
出版者・発行元
JAPANESE BIOCHEMICAL SOC

alpha-lytic protease (alp) was purified from a bacteriolytic agent, Achromopeptidase from Achromobacter lyticus M497-1, and has been shown to possess staphylolytic activity, Cleavage sites of this enzyme on the peptidoglycan of Staphylococcus aureus were determined by N-terminal amino acid sequence and amino acid composition analyses, Alp cleaved the N-acetylmuramoyl-L-alanine amide bond, the junction between the polysaccharide and peptide moieties, in addition to the D-Ala-Gly and Gly-Gly peptide bonds, implying that this enzyme recognizes the amino acid of D-configuration at the P1 site and possesses N-acetylmuramoyl-L-alanine amidase activity. However, alp could not cleave the D-Ala-Gly peptide bond in a synthetic peptide, suggesting that this hydrolytic activity of alp is peptidoglycan-specific. The results obtained from different consecutive actions of alp and glycosidase on S. aureus peptidoglycan indicate that the presence of polysaccharide in the peptidoglycan is necessary for the bacteriolytic activity of alp.

Web of Science ® 被引用回数 : 23

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:A1997YA00500015&DestApp=WOS_CPL