User:Gisselle Medina/Sandbox 1
From Proteopedia
(→Alcohol Dehydrogenase) |
|||
| Line 1: | Line 1: | ||
| - | |||
== Alcohol Dehydrogenase == | == Alcohol Dehydrogenase == | ||
| - | + | Alcohol dehydrogenase (ADH), which can be found in many forms within the liver and stomach of humans, is categorized into varying classes depending on its function. Looking specifically at class III ADH, we see that they focus their energy on formaldehyde dehydrogenase and fatty acid oxidation activities. In addition, the class III ADH can also carry out the oxidation of ethanol, however exhibiting a lower binding affinity for the substrate as compared to class I ADH (which are specifically designed to oxidize ethanol) (Engeland 1994). Studies show that there is one particular amino acid in the conformation of the class III ADH, which is very important in formaldehyde dehydrogenase and fatty acid oxidation activities within the active site. This is the charged residue Arginine 115. In studies this residue was replaced with Asparginine, which is the residue found at that site on class I ADH, and with the residue Alanine in order to remove the charge. Data showed that the function of formaldehyde dehydrogenase and fatty acid oxidation was greatly reduced when these mutations were expressed, but the oxidation of ethanol was not affected (Engeland 1994). | |
<applet load='1adc' size='300' frame='true' align='right' caption='Insert caption here' /> | <applet load='1adc' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
Revision as of 00:17, 4 March 2009
Alcohol Dehydrogenase
Alcohol dehydrogenase (ADH), which can be found in many forms within the liver and stomach of humans, is categorized into varying classes depending on its function. Looking specifically at class III ADH, we see that they focus their energy on formaldehyde dehydrogenase and fatty acid oxidation activities. In addition, the class III ADH can also carry out the oxidation of ethanol, however exhibiting a lower binding affinity for the substrate as compared to class I ADH (which are specifically designed to oxidize ethanol) (Engeland 1994). Studies show that there is one particular amino acid in the conformation of the class III ADH, which is very important in formaldehyde dehydrogenase and fatty acid oxidation activities within the active site. This is the charged residue Arginine 115. In studies this residue was replaced with Asparginine, which is the residue found at that site on class I ADH, and with the residue Alanine in order to remove the charge. Data showed that the function of formaldehyde dehydrogenase and fatty acid oxidation was greatly reduced when these mutations were expressed, but the oxidation of ethanol was not affected (Engeland 1994).
|
