Carbonic anhydrase 1, 2, 3, 4, 7, 12, 14 (CA1; CA2; CA3; CA4; CA7; CA12; CA14)

Carbonic anhydrases are a superfamily of zinc metalloenzymes (EC 4.2.1.1) that catalyze the reversible hydration of carbon dioxide to bicarbonate and protons. There are multiple carbonic anhydrase isoforms in humans (at least 16), including CA1, CA2, CA3, CA4, CA7, CA12, and CA14, among others, each encoded by a separate gene but sharing catalytic mechanism. These enzymes play crucial roles in acid-base regulation, respiration, fluid secretion, and pH homeostasis in various tissues. Carbonic anhydrase inhibition is targeted in the management of disorders like glaucoma, epilepsy, edema, and some rare hereditary diseases, and certain isoforms are investigated as cancer biomarkers or therapeutic targets. The protein class includes structurally unrelated but functionally convergent enzymes with a Zn²⁺ ion in the active site. Most clinically used inhibitors are sulfonamide derivatives. If you require information on a specific isoform, such as "Carbonic anhydrase 2," it is best to separate out the exact target to ensure structural accuracy and avoid grouping, as each isoform has distinct tissue distribution and disease relevance.

Other names

Carbonate dehydrataseCA (general family abbreviation)Specific isoform aliases (e.g., CA II for Carbonic anhydrase 2)

Inhibition of the reversible hydration of carbon dioxide to bicarbonate and protons by binding to the zinc-containing active site of the enzyme (competitive inhibition)