Solution structure and activity of mouse lysozyme M

T. Obita, Tadashi Ueda, T. Imoto

研究成果: ジャーナルへの寄稿学術誌査読

14 被引用数 (Scopus)


The three-dimensional structure of mouse lysozyme M, glycoside hydrolase, with 130 amino acids has been determined by heteronuclear NMR spectroscopy. We found that mouse lysozyme M had four α-helices, two 310 helices, and a double- and a triple-stranded anti-parallel β-sheet, and its structure was very similar to that of hen lysozyme in solution and in the crystalline state. The pH activity profile of p-nitrophenyl penta N-acetyl-β-D-chitopentaoside hydrolysis by mouse lysozyme M was similar to that of hen lysozyme, but the hydrolytic activity of mouse lysozyme M was lower. From analyses of binding affinities of lysozymes to a substrate analogue and internal motions of lysozymes, we suggest that the lower activity of mouse lysozyme M was due to the larger dissociation constant of its enzyme-substrate complex and the restricted internal backbone motions in the molecule.

ジャーナルCellular and Molecular Life Sciences
出版ステータス出版済み - 1月 1 2003

!!!All Science Journal Classification (ASJC) codes

  • 分子医療
  • 分子生物学
  • 薬理学
  • 細胞および分子神経科学
  • 細胞生物学


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