Carbonic anhydrase
FunctionCarbonic anhydrase (CA) are enzymes which catalyze the interconversion of CO2 and water to bicarbonate and proton. The active site contains Zn atom.[1] CA enzymes are divided into several classes:
For more details on carbonic anhydrase II see Carbonic Anhydrase IX With Saccharin, Molecular Playground/Carbonic Anhydrase, and Acetazolamide. DiseaseCarbonic anhydrase II deficiency syndrome is a recessive disorder that causes osteopetrosis, renal acidosis and cerebral calcification. Structural highlightsof the of carbonic anhydrase from Dunaliella salina (dCA II) structure. The regions corresponding to conserved regions (CRs, blue), variable regions (VRs, green), and variable conserved regions (VCRs, red), are positioned on the dCA II structure. The catalytic Zn2+, insertions and deletions in VCRs including L1 (the Zn binding loop), L4 (the Na-binding loop), L5, and two extended α-helices (E and G) are marked. N and C termini are labeled. .[3] 3D Structures of Carbonic anhydraseCarbonic anhydrase 3D structures
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ReferencesReferences
- ↑ Lindskog S. Structure and mechanism of carbonic anhydrase. Pharmacol Ther. 1997;74(1):1-20. PMID:9336012
- ↑ Nocentini A, Supuran CT, Capasso C. An overview on the recently discovered iota-carbonic anhydrases. J Enzyme Inhib Med Chem. 2021 Dec;36(1):1988-1995. PMID:34482770 doi:10.1080/14756366.2021.1972995
- ↑ Premkumar L, Greenblatt HM, Bageshwar UK, Savchenko T, Gokhman I, Sussman JL, Zamir A. Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog. Proc Natl Acad Sci U S A. 2005 May 24;102(21):7493-8. Epub 2005 May 13. PMID:15894606 doi:0502829102