Abstract
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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 25 February 2003; received after revision 29 May 2003; accepted 12 June 2003
Rights and permissions
About this article
Cite this article
Takeshita, K., Hashimoto, Y., Ueda, T. et al. A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme. CMLS, Cell. Mol. Life Sci. 60, 1944–1951 (2003). https://doi.org/10.1007/s00018-003-3082-z
Issue Date:
DOI: https://doi.org/10.1007/s00018-003-3082-z