Birrer Sandbox 2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 1: Line 1:
==Alcohol Dehydrogenase==
==Alcohol Dehydrogenase==
Alcohol dehydrogenase (ADH) is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen. {{STRUCTURE_1htb |  PDB=1htb  |  SCENE=  }}
Alcohol dehydrogenase (ADH) is an enzyme that catalyzes the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones through a mechanism that involves the removal of hydrogen.  
  In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The mechanism of the reaction is below:
 
{{STRUCTURE_1htb |  PDB=1htb  |  SCENE=  }}
 
  In the oxidation mechanism, ADH is momentarily associated with nicontinamide adenine dinucleotide (NAD+), which functions as a cosubstrate. The reaction is shown below:
CH3CH2OH + NAD+ → CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) (citation needed)
CH3CH2OH + NAD+ → CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) (citation needed)
The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.   
The alcohol dehydrogenase reaction is a bisubstrate reaction, where ADH catalyzed the transfer of a hydride ion from ethanol to NAD+. In metabolic reactions within the human liver, glyceraldehyde is reduced to glycerol through a mechanism in which NADH is reduced to NAD+, and this whole process is catalyzed by alcohol dehydrogenase.