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

To determine the structure and functional relationships of invertebrate lysozymes, we isolated a new invertebrate (i)-type lysozyme from the common orient clam (<i>Meretrix lusoria</i>) 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 <i>Venerupis philippinarum</i> (<i>Tapes japonica</i>), 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 <i>V. philippinarum</i> 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 <i>V. philippinarum</i> lysozyme. GlcNAc oligomer activities suggested an absence of transglycosylation activity and a higher number of subsites on this enzyme compared with hen egg lysozyme.