ExplorEnz: EC 1.1.1.105

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1.1.1.105

Accepted name:

all-trans-retinol dehydrogenase (NAD⁺)

Reaction:

all-trans-retinol—[cellular-retinol-binding-protein] + NAD⁺ = all-trans-retinal—[cellular-retinol-binding-protein] + NADH + H⁺

For diagram of retinal and derivatives biosynthesis, click here

Other name(s):

retinol (vitamin A₁) dehydrogenase; MDR; microsomal retinol dehydrogenase; retinol dehydrogenase (misleading); retinal reductase (ambiguous); retinene reductase; epidermal retinol dehydrogenase 2; SDR16C5 (gene name); RDH16 (gene name)

Systematic name:

all-trans retinol:NAD⁺ oxidoreductase

Comments:

The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD⁺/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis-retinol dehydrogenase). Also active with 3α-hydroxysteroids [2].

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9033-53-8

References:

1.	Koen, A.L. and Shaw, C.R. Retinol and alcohol dehydrogenases in retina and liver. Biochim. Biophys. Acta 128 (1966) 48–54. [PMID: 5972368]
2.	Gough, W.H., VanOoteghem, S., Sint, T. and Kedishvili, N.Y. cDNA cloning and characterization of a new human microsomal NAD⁺-dependent dehydrogenase that oxidizes all-trans-retinol and 3α-hydroxysteroids. J. Biol. Chem. 273 (1998) 19778–19785. [DOI] [PMID: 9677409]
3.	Matsuzaka, Y., Okamoto, K., Tsuji, H., Mabuchi, T., Ozawa, A., Tamiya, G. and Inoko, H. Identification of the hRDH-E2 gene, a novel member of the SDR family, and its increased expression in psoriatic lesion. Biochem. Biophys. Res. Commun. 297 (2002) 1171–1180. [DOI] [PMID: 12372410]
4.	Lee, S.A., Belyaeva, O.V. and Kedishvili, N.Y. Biochemical characterization of human epidermal retinol dehydrogenase 2. Chem. Biol. Interact. 178 (2009) 182–187. [DOI] [PMID: 18926804]

[EC 1.1.1.105 created 1972, modified 2011]