ethanol + NAD+ => acetaldehyde + NADH + H+

Stable Identifier
R-HSA-71707
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Ethanol is oxidized by NAD+ to form acetaldehyde, NADH, and H+
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Cytosolic alcohol dehydrogenase catalyzes the reaction of ethanol and NAD+ to form acetaldehyde and NADH + H+. The active form of the enzyme is a dimer with one zinc ion bound to each protein subunit. In the body, alcohol dehydrogenase is present in the liver, kidney, lung and gastric mucosa.

Six genes encode proteins active in ethanol oxidation: ADH1A, ADH1B, ADH1C, ADH4, ADH6, and ADH7 (Lange et al. 1976; Yin et al. 1985; Li et al. 1978; Bosron et al. 1979; Moreno and Pares 1991; Yokoyama et al. 1994; Chen and Yoshida 1991). ADH1A, B and C proteins can associate to form homodimers or heterodimers; ADH4, 6, and 7 proteins each form homodimers. Expression of ADH1A, B and C is developmentally regulated: ADH1A protein is abundant in the fetus, but expressed only at low levels in adulthood, when ADH1B and C proteins are abundant (Edenberg 2000). The various dimers differ substantially in the efficiency with which they oxidize ethanol. The ADH1B homodimer and heterodimers containing at least one 1B monomer are the most active towards ethanol (Yin et al. 1985). In addition, common polymorphic variants of ADH1B and C proteins differ substantially in this respect (Murray and Price 1972).

Literature References
PubMed ID Title Journal Year
10441588 Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism.

Chen, CC, Lu, RB, Chen, YC, Wang, MF, Chang, YC, Li, TK, Yin, SJ

Am J Hum Genet 1999
8074657 Molecular cloning of human class IV alcohol dehydrogenase cDNA.

Yokoyama, H, Baraona, E, Lieber, CS

Biochem Biophys Res Commun 1994
1755855 Enzymatic properties of the protein encoded by newly cloned human alcohol dehydrogenase ADH6 gene

Chen, CS, Yoshida, A

Biochem Biophys Res Commun 1991
6395883 Human liver alcohol dehydrogenase: purification and kinetic characterization of the beta 2 beta 2, beta 2 beta 1, alpha beta 2, and beta 2 gamma 1 "Oriental" isoenzymes.

Yin, SJ, Bosron, WF, Magnes, LJ, Li, TK

Biochemistry 1985
1985938 Purification and characterization of a new alcohol dehydrogenase from human stomach.

Moreno, A, Parés, X

J Biol Chem 1991
9982 Human liver alcohol dehydrogenase: purification, composition, and catalytic features.

Lange, LG, Sytkowski, AJ, Vallee, BL

Biochemistry 1976
4504607 Ontogenetic, polymorphic, and interethnic variation in the isoenzymes of human alcohol dehydrogenase.

Murray, RF, Price, PH

Ann N Y Acad Sci 1972
4748759 Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1, ADH2, and ADH3.

Smith, M, Hopkinson, DA, Harris, H

Ann Hum Genet 1974
270680 Isolation of pi-alcohol dehydrogenase of human liver: is it a determinant of alcoholism?

Li, TK, Bosron, WF, Dafeldecker, WP, Lange, LG, Vallee, BL

Proc Natl Acad Sci U S A 1978
427099 Human liver pi-alcohol dehydrogenase: kinetic and molecular properties.

Bosron, WF, Li, TK, Dafeldecker, WP, Vallee, BL

Biochemistry 1979
10697413 Regulation of the mammalian alcohol dehydrogenase genes.

Edenberg, HJ

Prog Nucleic Acid Res Mol Biol 2000
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
alcohol dehydrogenase activity, zinc-dependent of alcohol dehydrogenase complex [cytosol]
Physical Entity
Activity
Orthologous Events
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