Carbonic anhydrase
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 4: | Line 4: | ||
'''Carbonic anhydrase''' (CA) are enzymes which catalyze the interconversion of CO2 and water to bicarbonate and proton. The active site contains Zn atom.<ref>PMID:9336012</ref> CA enzymes are divided into several classes:<br /> | '''Carbonic anhydrase''' (CA) are enzymes which catalyze the interconversion of CO2 and water to bicarbonate and proton. The active site contains Zn atom.<ref>PMID:9336012</ref> CA enzymes are divided into several classes:<br /> | ||
| - | * '''α-carbonic anhydrase''' are found in mammals.<br /> | + | * '''α-carbonic anhydrase''' are found in mammals and the human enzyme has 15 isoforms.<br /> |
* '''β-carbonic anhydrase''' are found in prokaryotes.<br /> | * '''β-carbonic anhydrase''' are found in prokaryotes.<br /> | ||
* '''γ-carbonic anhydrase''' are found in methane-producing bacteria. For full entry on γ-carbonic anhydrase see [[Gamma Carbonic Anhydrase]].<br /> | * '''γ-carbonic anhydrase''' are found in methane-producing bacteria. For full entry on γ-carbonic anhydrase see [[Gamma Carbonic Anhydrase]].<br /> | ||
| + | * '''iota-carbonic anhydrase''' shows catalytic activity without metal ions<ref>PMID:34482770</ref>.<br /> | ||
For more details on carbonic anhydrase II see [[Carbonic Anhydrase IX With Saccharin]], [[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]], and [[Acetazolamide]]. | For more details on carbonic anhydrase II see [[Carbonic Anhydrase IX With Saccharin]], [[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]], and [[Acetazolamide]]. | ||
== Disease == | == Disease == | ||
| - | Carbonic anhydrase II deficiency syndrome is a recessive disorder that causes osteopetrosis, renal acidosis and cerebral calcification. | + | Carbonic anhydrase II deficiency syndrome is a recessive disorder that causes osteopetrosis, renal acidosis and cerebral calcification. |
== Structural highlights == | == Structural highlights == | ||
Current revision
| |||||||||||
References
- ↑ 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
