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Alcohol dehydrogenase (PDB id [[1htb]]), or 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. | Alcohol dehydrogenase (PDB id [[1htb]]), or 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 reaction is shown below: CH3CH2OH + NAD+ -> CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) <ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.<ref> 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. | 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) <ref>Voet, et. al. ''Fundamentals of Biochemistry: 3rd Edition''. Hoboken: Wiley & Sons, Inc, 2008.</ref> 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. | ||
Revision as of 23:30, 1 March 2010
Alcohol Dehydrogenase
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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 | ||||||||
Alcohol dehydrogenase (PDB id 1htb), or 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 reaction is shown below: CH3CH2OH + NAD+ -> CH3COH (acetaldehyde) + NADH + H+ (Note: The reaction is actually reversible although the arrow does not show it) [1] 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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ReferencesReferences
- ↑ Voet, et. al. Fundamentals of Biochemistry: 3rd Edition. Hoboken: Wiley & Sons, Inc, 2008.