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

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...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2013, Vol.77 (11), p.2269-2277
Main Authors: KUWANO, Yuko, YONEDA, Kazunari, KAWAGUCHI, Yuya, ARAKI, Norie, ARAKI, Tomohiro
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bivalvia
Bivalvia - chemistry
Bivalvia - enzymology
Chickens - metabolism
clam
Enzyme Stability
Glycosylation
Hydrogen-Ion Concentration
i-type lysozyme
invertebrate
Isoenzymes - classification
Isoenzymes - genetics
Isoenzymes - isolation & purification
Isoenzymes - metabolism
Kinetics
Meretrix lusoria
Molecular Sequence Data
Muramidase - classification
Muramidase - genetics
Muramidase - isolation & purification
Muramidase - metabolism
Osmolar Concentration
Phylogeny
Sequence Analysis, DNA
Substrate Specificity
Tapes japonica
Venerupis philippinarum
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Summary: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 transglycosylation activity and a higher number of subsites on this enzyme compared with hen egg lysozyme.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.130534