The Complete Amino Acid Sequence and Enzymatic Properties of an i-Type Lysozyme Isolated from the Common Orient Clam (Meretrix lusoria)

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概要

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• To determine the structure and functional relationships of invertebrate lysozymes, we isolated a new invertebrate (i)-type lysozyme from the common orient clam (Meretrix lusoria) and determined the complete amino acid sequence of two isozymes that differed by one amino acid. The determined sequence showed 65% similarity to a lysozyme from Venerupis philippinarum (Tapes japonica), and it was therefore classified as an i-type lysozyme. The lytic activities of this lysozyme were similar to those of previously reported bivalve i-type lysozymes, but unlike the V. philippinarum lysozyme, it did not exhibit an increase in activity in high ionic strength. Our data suggest that this lysozyme does not have a dimeric structure, due to the replacement of Lys108 which contributes to dimer formation in the V. philippinarum lysozyme. GlcNAc oligomer activities suggested an absence of transglycosilation activity and a higher number of subsites on this enzyme compared with hen egg lysozyme.

著者

• Araki Norie

  Department Of Tumor Genetics

• Araki Tomohiro

  Department Of Biochemistry School Of Agriculture Kyushu Tokai University

• KUWANO Yuko

  Department of Bioscience, School of Agriculture, Tokai University

• KAWAGUCHI Yuya

  Department of Bioscience, School of Agriculture, Tokai University

• YONEDA Kazunari

  Department of Bioscience, School of Agriculture, Tokai University

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