Solution structure and activity of mouse lysozyme M

T. Obita, Tadashi Ueda, T. Imoto

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)176-184
Number of pages9
JournalCellular and Molecular Life Sciences
Volume60
Issue number1
DOIs
Publication statusPublished - Jan 1 2003

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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