Carbonic Anhydrases: Versatile and Useful Biocatalysts in Chemistry and Biochemistry

Abstract

Metalloenzymes such as the carbonic anhydrases (CAs, EC 4.2.1.1) possess highly specialized active sites that promote fast reaction rates and high substrate selectivity for the physiologic reaction that they catalyze, hydration of CO2 to bicarbonate and a proton. Among the eight genetic CA macrofamilies, α-CAs possess rather spacious active sites and show catalytic promiscuity, being esterases with many types of esters, but also acting on diverse small molecules such as cyanamide, carbonyl sulfide (COS), CS2, etc. Although artificial CAs have been developed with the intent to efficiently catalyse non-biologically related chemical transformations with high control of stereoselectivity, the activities of these enzymes were much lower when compared to natural CAs. Here, we report an overview on the catalytic activities of α-CAs as well as of enzymes which were mutated or artificially designed by incorporation of transition metal ions. In particular, the distinct catalytic mechanisms of the reductase, oxidase and metatheses-ase such as de novo designed CAs are discussed.