Birrer Sandbox 2

Alcohol Dehydrogenase

Ligands:

, , ,

Gene:

HUMAN BETA3 CDNA (Homo sapiens)

Activity:

Alcohol dehydrogenase, with EC number 1.1.1.1

Structural annotation:
Resources:	CATH : 1Htba01, 1Htba02, 1Htbb02, 1Htbb01 InterPro : Ipr013149, Ipr002328, Ipr011032, Ipr013154, Ipr002085 Pfam : PF00107, PF08240 SCOP : d1htba1, d1htba2, d1htbb2, d1htbb1 UniProt : P00325

Functional annotation:
Cellular component:	cytoplasm
Biological process:	ethanol oxidation
Molecular function:	metal ion binding alcohol dehydrogenase activity, zinc-dependent electron carrier activity oxidoreductase activity alcohol dehydrogenase activity zinc ion binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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 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.

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1htb, resolution 2.40Å ()