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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

Territories

Select a territory to bring it forward.

Reading the map

Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

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

EtOH + NAD+ → CH3CHO + NADH + H+

Reactome: R-HSA-71707
Compartment: cytosol
Rhea: RHEA:25291

Inputs

EtOHCHEBI:16236, C2H6O, cytosol
NAD+CHEBI:57540, C21H26N7O14P2, cytosol

Outputs

CH3CHOCHEBI:15343, C2H4O, cytosol
NADHCHEBI:57945, C21H27N7O14P2, cytosol
H+CHEBI:15378, H, cytosol

Catalysed by

alcohol dehydrogenase (NAD+) activity of alcohol dehydrogenase complex [cytosol]EC 1.1.1.1

Literature

Human liver pi-alcohol dehydrogenase: kinetic and molecular properties. Biochemistry, 1979
Enzymatic properties of the protein encoded by newly cloned human alcohol dehydrogenase ADH6 gene Biochem Biophys Res Commun, 1991
Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism. Am J Hum Genet, 1999
Regulation of the mammalian alcohol dehydrogenase genes. Prog Nucleic Acid Res Mol Biol, 2000
Human liver alcohol dehydrogenase: purification, composition, and catalytic features. Biochemistry, 1976
Isolation of pi-alcohol dehydrogenase of human liver: is it a determinant of alcoholism? Proc Natl Acad Sci U S A, 1978