Find in Library

Carbonic anhydrase (CA) is widely distributed enzyme which plays a crucial role in hydration of carbon dioxide. CA of Anopheles gambiae, a common vector that transmits the malaria disease in tropical countries is not well studies. CA is essential for the normal physiological function and inhibition of it can lead to lethal effect. Recently, CA was identified as a potential drug target for developing mosquito larvicidal drugs. CA of A. gambiae was characterized and compared with 12 other members of the class insecta. CA of A. gambiae comprised of 309 amino acid residues with 34.56 kDa and theoretical pI of 6.34. The Leu rich protein had more of negatively charged residues and was classified as a stable protein. Mitochondrial targeting peptide containing enzyme had about 46.28% random coils, 28.16% α-helix and 3.24% β-turns. The homology model for the CA of A. gambiae was predicted using template 4lu3.1.A and the model quality was validated by least RMSD score, Z-score and Ramachandran plot analysis. The present study is a preliminary report exploring proteomics aspects of CA of A. gambiae using in silico tools.