User:Krishna Reddy Ragupathi
From Proteopedia
(Difference between revisions)
m |
m |
||
Line 1: | Line 1: | ||
Gaduate student in Chemistry at University of Massachuesetts (Amherst). | Gaduate student in Chemistry at University of Massachuesetts (Amherst). | ||
In the CBI program. | In the CBI program. | ||
+ | <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' | ||
Line 8: | Line 9: | ||
- | The active site of the enzyme is depicted here, which has three histidine residues coordinated to the zinc metal. | + | The active site of the enzyme is depicted here, which has three histidine residues coordinated to the zinc metal. |
- | + | ||
- | + |
Revision as of 23:42, 29 April 2010
Gaduate student in Chemistry at University of Massachuesetts (Amherst). In the CBI program.
|
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.