Bacteriophage-induced lytic enzyme which hydrolyzes L-alanine-D-glutamic acid peptide bond in peptidoglycan |
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Authors: | Akira Yanai Keijiro Kato Teruhiko Beppu Kei Arima |
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Affiliation: | Laboratory of Microbiology and Fermentaion Department of Agricultural Chemistry University of Tokyo, Tokyo, Japan |
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Abstract: | The mode of action of bacteriophage-induced lytic enzyme “LE95” was investigated. The LE95 hydrolyzed peptide portion in peptidoglycan of and . The exposed amino terminal amino acid was identified as glutamic acid by analysis of terminal amino acid by dinitrophenylation. This result suggested the LE95 hydrolyzed the peptide bond between L-alanine and D-glutamic acid in the peptidoglycan of and . The enzyme did not hydrolyze various peptides prepared from bacterial cell wall. This experimental result suggested that the glycan chain of peptidoglycan would be essential for the enzymic activity. |
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