Substrate Specificity of the N, 6-ο-Diacetylmuramidase from Streptomyces globisporus
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概要
- 論文の詳細を見る
We found that the N,6-ο-diacetylmuramidase from Streptomyces globisporus (M-1) hydrolyzed the cell walls from Micrococcus lysodeikticus and Staphylococcus aureus. In contrast, hen egg white lysozyme (HEWL) was only able to hydrolyze the cell walls from M. lysodeikticus. 6-ο-Acetylation of the muramoyl moieties, as found in the S. aureus cell walls, did not inhibit the activity of the M-1 enzyme whereas it was sufficient to inhibit HEWL. The disaccharide GlcNAc-MurNAc was not observed in the M. lysodeikticus cell wall hydrolyzate produced by the M-1, indicating that M-1 acts on the MurNAc moiety which are linked by peptides at the lactyl groups of the MurNAc moiety. M-1 displays both N-acetylmuramidase and N,6-ο-diacerylmuramidase activity and has a different substrate specificity from HEWL.
- 社団法人日本生物工学会の論文
- 2003-03-25
著者
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Kitaoka Motomitsu
National Food Research Institute, National Agriculture and Food Research Organization
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Ohmiya K
Graduate School Of Bioresources Mie Univ.
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Ohmiya Kunio
Department Of Food Science And Technology Faculty Of Agriculture Nagoya University
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KITAOKA Motomitsu
Enzyme Laboratory, National Food Research Institute, National Agriculture and Food Research Organiza
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Kitaoka M
Enzyme Laboratory National Food Research Institute
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Kitaoka M
Chubu Univ. Aichi Jpn
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Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute National Agriculture And Food Research Organizati
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Hayashi K
Enzyme Laboratory National Food Research Institute
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HAYASHI Kiyoshi
Enzyme Applications Laboratory, National Food Research Institute
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Kitaoka Motomitsu
Enzyme Laboratory National Food Research Institute
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切畑 光統
大阪府立大学 農学部
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Kitaoka Motomitsu
Department Of Biological Chemistry Chubu University
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Seo Hyo
Enzyme Laboratory National Food Research Institute:department Of Bioscience Faculty Of Bioresources
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Ohmiya Kunio
Department Of Bioresources School Of Bioresources Mie University
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