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Carbonic anhydrase 13 is a human zinc-dependent cytosolic enzyme encoded by the CA13 gene. As a member of the carbonic anhydrase family, it catalyzes the reversible hydration of carbon dioxide, assisting in regulation of acid-base and ion balance in various tissues. CA13 is notably expressed in the reproductive organs and the intestinal tract and may play roles in local pH homeostasis. Its active site architecture resembles other α-carbonic anhydrases, enabling inhibition by classical sulfonamides such as acetazolamide. Like other carbonic anhydrases, it is implicated in certain physiological and disease processes, including idiopathic intracranial hypertension and sleep apnea.
Inhibition of carbonate dehydratase activity (prevents formation of bicarbonate and proton from CO₂ by blocking zinc-dependent active site) Competitive binding to active site zinc (typical of sulfonamide inhibitors)
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