Birrer Sandbox 2
Alcohol DehydrogenaseAlcohol 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.
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| 1htb, resolution 2.40Å () | |||||||||
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| Ligands: | , , , | ||||||||
| Gene: | HUMAN BETA3 CDNA (Homo sapiens) | ||||||||
| Activity: | Alcohol dehydrogenase, with EC number 1.1.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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)
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.
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