Carbonic anhydrase 1 and 2 (CA1 and CA2)

Carbonic anhydrase 1 and 2 are zinc-dependent hydrolase enzymes found primarily in erythrocytes (CA1 and CA2), kidneys, eyes, and other tissues. They catalyze the reversible hydration of carbon dioxide into bicarbonate and protons, which is a fundamental process for pH regulation, maintenance of acid-base homeostasis, and carbon dioxide transport in the blood. Inhibition of these enzymes is therapeutically useful for conditions such as glaucoma, epilepsy, heart failure, and altitude sickness, as it leads to reduction of aqueous humor, decreases in intraocular pressure, and mild diuresis. CA2 is the more catalytically efficient isoform and is widely studied as a drug target. Both isoforms are targeted by sulfonamide-based drugs[1][2][4][5][6]. Carbonic anhydrase I and II are among the most characterized of the carbonic anhydrase family, with well-known structure, function, and clinical importance in several disease states. Both are single-chain polypeptides with a conserved tertiary structure dominated by β-strands and a zinc ion in the active site[1][2][3][4][6].

Other names

Carbonic anhydrase ICarbonic anhydrase IICA-ICA-IICA1CA2Carbonate hydro-lyase 1Carbonate hydro-lyase 2

Competitive inhibition of the zinc-containing active site by sulfonamides and related compounds, preventing the enzyme from catalyzing the hydration of carbon dioxide[1][4][5].