Affiliation: Osaka University
- Bacteriolytic activity and specificity of Achromobacter beta-lytic proteaseS Li
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka, 565 0871, Japan jp
J Biochem 124:332-9. 1998..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...
- Purification, characterization, and primary structure of a novel cell wall hydrolytic amidase, CwhA, from Achromobacter lyticusS Li
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita, Osaka 565 0871, Japan
J Biochem 127:1033-9. 2000..Its sequence identity with BPT7 is 35%, but the amino acid residues functioning as zinc ligands in BPT7 are absent in CwhA. These results suggest that CwhA is a new type of N-acetylmuramoyl-L-alanine amidase...
- Purification, staphylolytic activity, and cleavage sites of alpha-lytic protease from Achromobacter lyticusS Li
Division of Protein Chemistry, Institute for Protein Research, Osaka University, Suita
J Biochem 122:772-8. 1997..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...