Characterization of Two N-Acetylmuramidases from Streptomyces globisporus 1829
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概要
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Two kinds of N-acetylmuramidase, M-l and M-2 enzymes, that were isolated from the cultural broth of Stm. globisporus 1829, were remarkably different in amino acid composition, immunological properties and modes of lytic action from each other. The M-l enzyme was composed of 186 amino acid residues of which two moles were of half cystine, while the M-2 enzyme was composedof 99 amino acid residues with no cysteine. The hydrolyzing action of the M-2 enzyme was suppressed by the presence of an N-acetyl group on muramic acid residues in the peptidoglycan moiety, while that of the M-l enzyme was independent of the presence of N-acetyl groups. However, the hydrolyzing activity of both enzymes was enhanced when some muramicacid residues were substituted with stem peptides containing alanine, isoglutamine and lysine.
- 社団法人 日本農芸化学会の論文
著者
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YOKOGAWA Kanae
Research Laboratory, Dainippon Pharmaceutical Co., Ltd.
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Kawata Shigeo
Research Information Center Institute Of Plasma Physics Nagoya University
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TAKEMURA Tadashi
Research Laboratories, Dainippon Pharmaceutical Co., Ltd.
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