The complete amino acid sequence and enzymatic properties of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria).
Biosci Biotechnol Biochem
; 77(11): 2269-77, 2013.
Article
en En
| MEDLINE
| ID: mdl-24200802
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Filogenia
/
Muramidasa
/
Bivalvos
Límite:
Animals
Idioma:
En
Revista:
Biosci Biotechnol Biochem
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2013
Tipo del documento:
Article
Pais de publicación:
Reino Unido