# Carbonic anhydrase

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Main article: Enzymes
Carbonic anhydrase
Systematic name carbonate hydrolyase
Other names carbonate dehydratase;
carbonate anhydrase;
carbonic acid anhydrase
EC number EC 4.2.1.1
CAS number 9001-03-0
EINECS 232-576-6
Disclaimer and references

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.[1] 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.[2] The active site of most carbonic anhydrases contains a zinc ion.

## Structure and function of CAEdit

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.

Reaction catalyzed by carbonic anhydrase:

$\rm CO_2 + H_2O \rightarrow^{Carbonic\ anhydrase} HCO_3^- + H^+$[3] (in tissues - high CO2 concentration)

The reaction rate of carbonic anhydrase is one of the fastest of all enzymes, and its rate is typically limited by the diffusion rate of its substrates.

The reverse reaction is fast and does not require a catalyst.

$\rm HCO_3^- + H^+ \rightarrow H_2CO_3 \rightarrow CO_2 + H_2O$ (in lungs and nephrons of the kidney - low CO2 concentration, in plant cells)

## Mechanism Edit

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.

A fourth histidine is placed close to the substrate of water and accepts a proton, in an example of general acid-general base catalysis. This leaves a hydroxide attached to the zinc.

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.

## CA familiesEdit

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.

### α-CAEdit

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)

### β-CAEdit

Most prokaryotic and plant chloroplast CAs belong to the beta family. Two signature patterns for this family have been identified:

• C-[SA]-D-S-R-[LIVM]-x-[AP]
• [EQ]-[YF]-A-[LIVM]-x(2)-[LIVM]-x(4)-[LIVMF](3)-x-G-H-x(2)-C-G

### γ-CAEdit

The gamma class of CAs come from methane-producing bacteria that grow in hot springs.

### δ-CAEdit

The delta class of CAs has been described in diatoms. The distinction of this class of CA has recently[4] come into question, however.

### ε-CAEdit

The epsilon class of CAs occurs exclusively in bacteria in a few chemolithotrophs and marine cyanobacteria that contain cso-carboxysomes.[5] Recent 3-dimensional analyses[4] 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 CAEdit

See Carbonic anhydrase inhibitors

## ReferencesEdit

1. Badger MR, Price GD. 1994. The role of carbonic anhydrase in photosynthesis. Annu Rev Plant Physiol Plant Mol Biol. 45:369–392
2. Lindskog S. 1997. Structure and mechanism of carbonic anhydrase. PHARMACOLOGY & THERAPEUTICS. 74:1-20
3. 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+ $\rightleftharpoons$ H2CO3 and H2CO3 $\rightleftharpoons$ CO2 + H2O
4. 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
5. 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.

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