Bacteriolytic activity and specificity of Achromobacter beta-lytic protease.
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, 157-162]. 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.
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan. lishao@protein.osaka-u.ac. jp
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D000421:Alcaligenes / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis; D001433:Bacteriolysis / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis / Q000187:drug effects; D013058:Mass Spectrometry; D009994:Osmolar Concentration; D010455:Peptides / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity
D000596:Amino Acids; D004791:Enzyme Inhibitors; D010455:Peptides; D010457:Peptidoglycan; D012697:Serine Endopeptidases; C036813:lysyl endopeptidase