Carbonic anhydrase 5B, mitochondrial is an
enzyme that in humans is encoded by the CA5Bgene.[5][6]
Carbonic anhydrases (CAs) are a large family of
zincmetalloenzymes that catalyze the reversible hydration of
carbon dioxide. They participate in a variety of biological processes, including
respiration,
calcification,
acid-base balance,
bone resorption, and the formation of
aqueous humor,
cerebrospinal fluid,
saliva, and
gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA VB is localized in the
mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA VA. It has a wider tissue distribution than CA VA, which is restricted to the
liver. The differences in tissue distribution suggest that the two mitochondrial carbonic anhydrases evolved to assume different physiologic roles.[6]
Nishimori I, Onishi S (2001). "Carbonic anhydrase isozymes in the human pancreas". Digestive and Liver Disease. 33 (1): 68–74.
doi:
10.1016/s1590-8658(01)80138-9.
PMID11303978.
Vullo D, Nishimori I, Innocenti A, et al. (2007). "Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines". Bioorg. Med. Chem. Lett. 17 (5): 1336–40.
doi:
10.1016/j.bmcl.2006.11.075.
PMID17174092.
Carbonic anhydrase 5B, mitochondrial is an
enzyme that in humans is encoded by the CA5Bgene.[5][6]
Carbonic anhydrases (CAs) are a large family of
zincmetalloenzymes that catalyze the reversible hydration of
carbon dioxide. They participate in a variety of biological processes, including
respiration,
calcification,
acid-base balance,
bone resorption, and the formation of
aqueous humor,
cerebrospinal fluid,
saliva, and
gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA VB is localized in the
mitochondria and shows the highest sequence similarity to the other mitochondrial CA, CA VA. It has a wider tissue distribution than CA VA, which is restricted to the
liver. The differences in tissue distribution suggest that the two mitochondrial carbonic anhydrases evolved to assume different physiologic roles.[6]
Nishimori I, Onishi S (2001). "Carbonic anhydrase isozymes in the human pancreas". Digestive and Liver Disease. 33 (1): 68–74.
doi:
10.1016/s1590-8658(01)80138-9.
PMID11303978.
Vullo D, Nishimori I, Innocenti A, et al. (2007). "Carbonic anhydrase activators: an activation study of the human mitochondrial isoforms VA and VB with amino acids and amines". Bioorg. Med. Chem. Lett. 17 (5): 1336–40.
doi:
10.1016/j.bmcl.2006.11.075.
PMID17174092.