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The fastest member of the carbonic anhydrase family catalysing the reversible hydration of carbon dioxide to bicarbonate ions has been recently reported to be SazCA. While thermostable, this enzyme shows exceptional activity at 353 K for the reaction. This study explores the molecular basis for the exceptional activity of SazCA, in contrast to SspCA, probed using molecular dynamics simulations. Our simulations, carried out at different temperatures, indicate the presence of efficient proton shuttle between the active zinc centre and His64 residue in the two enzymes. The proton accepting His64 residue was identified to have  in  and  out  conformations with the  in  conformations being supportive to proton acceptance. Our simulations show a large population of  in  conformations in SazCA making the enzyme exhibit an exceptional activity. The RMSF and H-bonds analysis confirmed the role of His2 and His207 in supporting the attainment of  in  conformations in SazCA resulting in exceptional activity. Communicated by Ramaswamy H. Sarma

Efficient proton shuttle makes SazCA an excellent CO 2 hydration enzyme