ADH1A,1C,4 oxidise atROL to atRAL in vitro

Stable Identifier
R-HSA-5362564
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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.

Literature References
PubMed ID Title Journal Year
1889753 Cloning and characterization of the human ADH4 gene

von Bahr-Lindström, H, Jörnvall, H, Höög, JO

Gene 1991
9228021 X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity

Xie, P, Parsons, SH, Speckhard, DC, Bosron, WF, Hurley, TD

J. Biol. Chem. 1997
3013304 cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase

von Bahr-Lindström, H, Höög, JO, Hedén, LO, Kaiser, R, Fleetwood, L, Larsson, K, Lake, M, Holmquist, B, Holmgren, A, Hempel, J

Biochemistry 1986
2935875 Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence

Ikuta, T, Szeto, S, Yoshida, A

Proc. Natl. Acad. Sci. U.S.A. 1986
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
retinol dehydrogenase activity of ADH1A,1C,4 dimers [cytosol]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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