User:Krishna Reddy Ragupathi
From Proteopedia
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| - | + | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | |
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| + | <scene name='User:Krishna_Reddy_Ragupathi/Carbonic_anhydrase/2'>CBI Carbonic Anhydrase Model</scene> | ||
<applet size='[450,338]' frame='true' align='right' | <applet size='[450,338]' frame='true' align='right' | ||
| - | caption='Carbonic Anhydrase' /> | + | caption='Carbonic Anhydrase' scene='User:Krishna_Reddy_Ragupathi/Carbonic_anhydrase/2' /> |
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| + | Shown is the enzyme Carbonic Anhydrase II which falls under α-Family of Carbonic Anhydrases. As the name suggest Carbonic Anhydrases are a class of enzymes which catalyze the reversible conversion of carbondioxide to the bicarbonate and proton. Due to this unique property they play a key role in maintaining the acid-base balance of blood and several other tissues. | ||
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| - | + | The active site of the enzyme is depicted here, which has three histidine residues coordinated to the zinc metal. | |
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Current revision
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
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Shown is the enzyme Carbonic Anhydrase II which falls under α-Family of Carbonic Anhydrases. As the name suggest Carbonic Anhydrases are a class of enzymes which catalyze the reversible conversion of carbondioxide to the bicarbonate and proton. Due to this unique property they play a key role in maintaining the acid-base balance of blood and several other tissues.
The active site of the enzyme is depicted here, which has three histidine residues coordinated to the zinc metal.
