Carbonic anhydrase (KA) enzymes are zinc-containing metalloenzymes commonly found in both prokaryotes and eukaryotes. There are 16 CA isoforms in humans that differ greatly in their cellular location and biophysical properties. These are: KA-I, II, III, IV, V (VA and VB), VI, VII, VIII, IX, X, XI, XII, XIII, XIV, XV. CA enzymes catalyze the reversible conversion of carbon dioxide to bicarbonate and hydrogen ions. They are involved in important biochemical reactions such as acid-base balance, carbon dioxide homeostasis, ureogenesis, gluconeogenesis and lipogenesis and physiological processes such as bone resorption, calcification, regulation of seminal fluid, tumorigenicity, and electrolyte secretion. Due to their important role in the organism, KA enzymes are therapeutic targets for many diseases such as glaucoma, epilepsy, sleep apnea, obesity, osteoporosis, high altitude sickness, neuropathic pain and cancer. In this study, the properties of carbonic anhydrase enzymes, their physiological roles in the organism and their terapeutical importance are mentioned.