Sandbox 66: Difference between revisions
Carbonic Anhydrase |
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'''Carbonic Anhydrase''' | '''Carbonic Anhydrase''' | ||
Carbonic anhydrase enzymes are found in mammals, plants and bacteria. The alpha class relates to mammals. Carbonic Anhydrase enzymes are found in red blood cells and converts carbon dioxide to carbonic acid and bicarbonate ions. This enzyme also converts the acid and ions back to carbon dioxide which we breath out. This enzyme is not imperative for breathing process however it increases the rate of these conversions up to a million fold. | Carbonic anhydrase enzymes are found in mammals, plants and bacteria. The alpha class relates to mammals. | ||
Carbonic Anhydrase enzymes are found in red blood cells and converts carbon dioxide to carbonic acid and | |||
bicarbonate ions. This enzyme also converts the acid and ions back to carbon dioxide which we breath out. | |||
This enzyme is not imperative for breathing process however it increases the rate of these conversions up | |||
to a million fold. Carbonic Anhydrase is classified as a metalloprotein because of its active site which contains a <scene name='Sandbox_66/Zinc_ion/1'>Zinc ion</scene> | |||
'''History of Carbonic Anhydrase''' | |||
Carbonic Anhydrase was found in the red blood cells of cows in 1933. | |||
Throughout the years they have found three new classes of the enzyme. | |||
Alpha, beta and gamma are classes related to mammalian, plants and | |||
bacterial class. | |||
'''Structure of Carbonic Anhydrase''' | |||
The structure of carbonic anhydrase is unique. Its active site which is a zinc ion is the key to the enzymes function. Zinc is a positive charged ion which allows it to break down the carbon dioxide. In the center of the structure there is a <scene name='Sandbox_66/Beta_sheets/1'>beta sheet</scene> which is bound to three nitrogen atoms (<scene name='Sandbox_66/66/1'>94</scene>,<scene name='Sandbox_66/106/1'>96</scene>, and <scene name='Sandbox_66/199/1'>119</scene>). | |||
Carbonic Anhydrase Structure | |||
[http://proteopedia.org/wiki/index.php/Image:CA-rasmol.gif] | |||
Latest revision as of 14:21, 11 May 2009
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| 1ca2, resolution 2.00Å (default scene) | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Carbonic Anhydrase
Carbonic anhydrase enzymes are found in mammals, plants and bacteria. The alpha class relates to mammals. Carbonic Anhydrase enzymes are found in red blood cells and converts carbon dioxide to carbonic acid and bicarbonate ions. This enzyme also converts the acid and ions back to carbon dioxide which we breath out. This enzyme is not imperative for breathing process however it increases the rate of these conversions up to a million fold. Carbonic Anhydrase is classified as a metalloprotein because of its active site which contains a Zinc ion
History of Carbonic Anhydrase Carbonic Anhydrase was found in the red blood cells of cows in 1933. Throughout the years they have found three new classes of the enzyme. Alpha, beta and gamma are classes related to mammalian, plants and bacterial class.
Structure of Carbonic Anhydrase The structure of carbonic anhydrase is unique. Its active site which is a zinc ion is the key to the enzymes function. Zinc is a positive charged ion which allows it to break down the carbon dioxide. In the center of the structure there is a beta sheet which is bound to three nitrogen atoms (94,96, and 119).
Carbonic Anhydrase Structure
[1]
![[1]](https://proteopedia.org/wiki/index.php/Image:CA-rasmol.gif){kind=link}