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|Systematic name||carbonate hydrolyase|
|Other names|| carbonate dehydratase;|
carbonic acid anhydrase
|EC number||EC 18.104.22.168|
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Carbonic anhydrase (carbonate dehydratase) is a family of metalloenzymes (enzymes that contain one or more metal atoms as a functional component of the enzyme) that catalyze the rapid conversion of carbon dioxide to bicarbonate and protons, a reaction that occurs rather slowly in the absence of a catalyst. Carbonic anhydrase greatly increases the rate of the reaction, with typical catalytic rates of the different forms of this enzyme ranging between 104 and 106 reactions per second. The active site of most carbonic anhydrases contains a zinc ion.
Structure and function of CA
Several forms of carbonic anhydrase occur in nature. In the best studied α-carbonic anhydrase form present in animals, this zinc ion is coordinated by the imidazole rings of 3 histidine residues, His94, His96 and His119. The primary function of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues and to help transport carbon dioxide out of tissues. Plants contain a different form called β-carbonic anhydrase which is an evolutionarily distinct enzyme but participates in the same reaction and also uses a zinc ion in its active site. In plants, carbonic anhydrase helps raise the concentration of CO2 within the chloroplast to increase the carboxylation rate of the enzyme Rubisco. This is the reaction which integrates CO2 into organic carbon sugars during photosynthesis, and can only use the CO2 form of carbon, not carbonic acid nor bicarbonate.
In 2000, a cadmium containing carbonic anhydrase was found to be expressed in marine diatoms during zinc limitation. In the open ocean, zinc is often in such low concentrations that it can limit the growth of phytoplankton like diatoms, thus a carbonic anhydrase using a different metal ion would be beneficial in these environments. Before this discovery, cadmium has generally been thought of as a very toxic heavy metal without biological function. As of 2005, this peculiar carbonic anhydrase form hosts the only known beneficial cadmium-dependent biological reaction.
Reaction catalyzed by carbonic anhydrase:
The reverse reaction is fast and does not require a catalyst.
A zinc prosthetic group in the enzyme is coordinated in three positions by histidine side chains. The fourth coordination position is occupied by water. This causes polarisation of the hydrogen-oxygen bond, making the oxygen slightly more negative, thereby weakening it.
The active site also contains specificity pocket for carbon dioxide, bringing it close to the hydroxide group. This allows the electron rich hydroxide to attack the carbon dioxide, forming bicarbonate.
There are at least five distinct CA families (α, β, γ, δ and ε). These families have no significant amino acid sequence similarity and in most cases are thought to be an example of convergent evolution.
The CA enzymes found in mammals are divided into four broad subgroups:
- the cytosolic CAs (CA-I, CA-II, CA-III, CA-VII and CA XIII)
- mitochondrial CAs (CA-VA and CA-VB)
- secreted CAs (CA-VI)
- membrane-associated CAs (CA-IV, CA-IX, CA-XII, CA-XIV and CA-XV)
The gamma class of CAs come from methane-producing bacteria that grow in hot springs.
The epsilon class of CAs occurs exclusively in bacteria in a few chemolithotrophs and marine cyanobacteria that contain cso-carboxysomes. Recent 3-dimensional analyses suggest that ε-CA bears some structural resemblance to β-CA, particularly near the metal ion site. Thus, the two forms may be distantly related, even though the underlying amino acid sequence has since diverged considerably.
Pharmacological agents affecting CA
- ↑ Badger MR, Price GD. 1994. The role of carbonic anhydrase in photosynthesis. Annu Rev Plant Physiol Plant Mol Biol. 45:369–392
- ↑ Lindskog S. 1997. Structure and mechanism of carbonic anhydrase. PHARMACOLOGY & THERAPEUTICS. 74:1-20
- ↑ Carbonic acid has a pKa of around 6.36 (the exact value depends on the medium) so at pH 7 a small percentage of the bicarbonate is protonated. See carbonic acid for details concerning the equilibria HCO3- + H+ H2CO3 and H2CO3 CO2 + H2O
- ↑ 4.0 4.1 Sawaya MR, Cannon GC, Heinhorst S, Tanaka S, Williams EB, Yeates TO, Kerfeld CA. 2006. The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two. J Biol Chem. 281(11):7546-55
- ↑ So AK, Espie GS, Williams EB, Shively JM, Heinhorst S, Cannon GC. 2004. A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell. J Bacteriol. 186(3):623-30.
Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)
Carbonic anhydrase - Fumarase - Aconitase - Enolase (Alpha) - Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase - Methylglutaconyl-CoA hydratase - Tryptophan synthase - Cystathionine beta synthase - Porphobilinogen synthase - 3-isopropylmalate dehydratase - Urocanate hydratase - Uroporphyrinogen III synthase - Nitrile hydratase
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