Chitin deacetylase (CDA; EC 3. 5. 1. 41) catalyzes the deacetylation of chitin.\nIn this study, we successfully cloned and sequenced a chitin deacetylase gene\nfrom the red snow crab Chionoecetes japonicus . By using reverse transcription-\npolymerase chain reaction (RT-PCR) and 5' and 3' rapid amplification of\ncDNA ends, we obtained a 2141-bp amplicon containing a chitin deacetylase\ngene (CjCDA) from the epidermis of C. japonicus . The amplicon contains a\n1575-bp open reading frame that is predicted to encode a 525-amino acid\nprotein. The structure predicted from the deduced amino acid sequence included\nan N-terminal signal peptide, chitin-binding domain (CBD),\nlow-density lipoprotein receptor class A domain (LDL-A), and catalytic domain.\nComparative analysis of the deduced amino acid sequence of CjCDA\nrevealed the highest homology (74%) to gastrolith protein 59 of Cherax quadricarinatus\n. We used RT-PCR to evaluate the expression of CjCDA in various\ntissues of C. japonicus , and we observed that CjCDA was expressed only\nin the epidermis. A phylogenetic analysis, using the amino acid sequences of\nCjCDA and other known chitin deacetylases, showed that CjCDA belonged to\na group of crustacean chitin deacetylases. To our knowledge, this is the first\nstudy reporting the cDNA cloning of a chitin deacetylase from a crab.
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