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

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

Stable Identifier

R-HSA-5362564

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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

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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
9228021	X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity Bosron, WF, Hurley, TD, Xie, P, Parsons, SH, Speckhard, DC	J. Biol. Chem.	1997
1889753	Cloning and characterization of the human ADH4 gene Höög, JO, Jörnvall, H, von Bahr-Lindström, H	Gene	1991
3013304	cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase Höög, JO, Kaiser, R, Larsson, K, Hempel, J, Fleetwood, L, Holmquist, B, Lake, M, Holmgren, A, Hedén, LO, von Bahr-Lindström, H	Biochemistry	1986
2935875	Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence Yoshida, A, Szeto, S, Ikuta, T	Proc. Natl. Acad. Sci. U.S.A.	1986