A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme

K. Takeshita, Y. Hashimoto, Tadashi Ueda, T. Imoto

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The lysozyme of the marine bilave Tapes japonica (13.8 kDa) is a novel protein. The protein has 46% homology with the destabilase from medicinal leech that has isopeptidase activity. Based on these data, we confirmed hydrolysis activity of T. japonica lysozyme against three substrates: L-γ-Glu-pNA, D-γ-Glu-pNA, and ε-(γ-Glu)-L-Lys. The optimal pH of chitinase and isopeptidase activity was 5.0 and 7.0, respectively. The isopeptidase activity was inhibited with serine protease inhibitor, but the lytic and chitinase activities were not. Moreover, only isopeptidase activity is decreased by lyophilization, but lytic and chitinase activities were not. We conclude that T. japonica lysozyme expresses isopeptidase and chitinase activity at different active sites.

Original languageEnglish
Pages (from-to)1944-1951
Number of pages8
JournalCellular and Molecular Life Sciences
Issue number9
Publication statusPublished - Sep 1 2003


All Science Journal Classification (ASJC) codes

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

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