期刊
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
卷 73, 期 22, 页码 7150-7154出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.01783-07
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资金
- NIAID NIH HHS [R21 AI054897, AI054897] Funding Source: Medline
Putative N-acetylmuramyl-L-alanine amidase genes from LambdaSa1 and LambdaSa2 prophages of Streptococcus agalactiae were cloned and expressed in Escherichia coli. The purified enzymes lysed the cell walls of Streptococcus agalactiae, Streptococcus pneumoniae, and Staphylococcus aureus. The peptidoglycan digestion products in the cell wall lysates were not consistent with amidase activity. Instead, the structure of the muropeptide digestion fragments indicated that both the LambdaSa1 and LambdaSa2 lysins exhibited gamma-D-glutaminyl-L-lysine endopeptidase activity. The endopeptidase cleavage specificity of the lysins was confirmed using a synthetic peptide substrate corresponding to a portion of the stem peptide and cross bridge of Streptococcus agalactiae peptidoglycan. The LambdaSa2 lysin also displayed beta-D-N-acetylglucosaminidase activity.
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