A novel carbonic anhydrase from the giant clam Tridacna gigas contains two carbonic anhydrase domains

Leggat, William, Dixon, Ross, Saleh, Said, and Yellowlees, David (2005) A novel carbonic anhydrase from the giant clam Tridacna gigas contains two carbonic anhydrase domains. FEBS journal, 272 (13). pp. 3297-3305.

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This report describes the presence of a unique dual domain carbonic anhydrase (CA) in the giant clam, Tridacna gigas. CA plays an important role in the movement of inorganic carbon (Ci) from the surrounding seawater to the symbiotic algae that are found within the clam's tissue. One of these isoforms is a glycoprotein which is significantly larger (70 kDa) than any previously reported from animals (generally between 28 and 52 kDa). This α-family CA contains two complete carbonic anhydrase domains within the one protein, accounting for its large size; dual domain CAs have previously only been reported from two algal species. The protein contains a leader sequence, an N-terminal CA domain and a C-terminal CA domain. The two CA domains have relatively little identity at the amino acid level (29%). The genomic sequence spans in excess of 17 kb and contains at least 12 introns and 13 exons. A number of these introns are in positions that are only found in the membrane attached/secreted CAs. This fact, along with phylogenetic analysis, suggests that this protein represents the second example of a membrane attached invertebrate CA and it contains a dual domain structure unique amongst all animal CAs characterized to date.

Item ID: 1467
Item Type: Article (Research - C1)
ISSN: 1742-4658
Keywords: dual domain carbonic anhydrase, CA, clam, Tridacna gigas, symbiotic algae, amino acid, invertebrate CA
Date Deposited: 01 Jun 2007
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060199 Biochemistry and Cell Biology not elsewhere classified @ 100%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
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