Abstract

Under salt and toxic metal stress condition, genetic make-up and proteins including some enzymes undergo specific changes to combat the posed harsh environment. Carbonic anhydrase is ubiquitous enzyme associated with respiratory disorder and cancerous condition. Strategies investigated and adopted by microorganisms to cope with hypersaline by bioinformatics analysis including homology modeling, Zinc metal interaction prediction, sequence analysis for Carbonic Anhydrase. This study shows that carbonic anhydrase acquired more acidic residues on its surface as countermeasure and may form salt bridges with positive ions in response to hypersaline environment. It also reduced its surface area and had more polar residues. Zinc metal interaction with Nitrogen of Histidine residues were almost conserved in the studied and modelled structure with fewer changes in catalytic region of sequence pattern. Salt tolerance achieved by foster promising approaches at the genetic and proteomic level by modifying protein sequence. Surface residues are exposed to a hypersaline medium and are mainly composed of polar and acidic residues. The enzyme exists in its compact form and reduces its surface footprint exposed to outside environment. Beta pleated secondary structure configuration increases flexibility to counter, ions disruptive effect.