Search results for ADH4

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Species

Types

Compartments

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-71713
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: ADH4: P08319

Complex (1 results from a total of 1)

Identifier: R-HSA-71714
Species: Homo sapiens
Compartment: cytosol

Reaction (2 results from a total of 2)

Identifier: R-HSA-5362564
Species: Homo sapiens
Compartment: cytosol
Some alcohol dehydrogenases (ADHs) utilise NAD+ as cofactor to reversibly oxidise all-trans-retinol (atROL) to all-trans-retinal (atRAL), a retinoid aldehyde, in vitro (von Bahr-Lindstrom et al. 1986, Ikuta et al. 1986, von Bahr-Lindstrom et al. 1991, Xie et al. 1997). ADH1A (ADH1) and ADH4 have high activity and ADH1C (ADH3) has low activity with non-physiological amounts of retinol in vitro. ADH1A and ADH1C metabolize toxic amounts of retinol in vivo, but ADH4 does not. Physiological contributions of ADHs to retinol metabolism have not been demonstrated, in contrast to RDHs.
Identifier: R-HSA-71707
Species: Homo sapiens
Compartment: cytosol
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).

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