EC - all-trans-retinol dehydrogenase (NAD+)

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IntEnz Enzyme Nomenclature


Accepted name:
all-trans-retinol dehydrogenase (NAD+)
Other names:
all-trans retinol dehydrogenase
microsomal retinol dehydrogenase
retinal reductase
retinene reductase
retinol (vitamin A1) dehydrogenase
retinol dehydrogenase [misleading]
epidermal retinol dehydrogenase 2
SDR16C5 (gene name)
RDH16 (gene name)
Systematic name:
all-trans retinol:NAD+ oxidoreductase



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, 11-cis retinol dehydrogenase). Also active with 3α-hydroxysteroids [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004745
CAS Registry Number: 9033-53-8
UniProtKB/Swiss-Prot: (32) [show] [UniProt]


  1. Koen, A.L. and Shaw, C.R.
    Retinol and alcohol dehydrogenases in retina and liver.
    Biochim. Biophys. Acta 128 : 48-54 (1966). [PMID: 5972368]
  2. Gough, W. H., VanOoteghem, S., Sint, T., 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 : 19778-19785 (1998). [PMID: 9677409]
  3. Matsuzaka, Y., Okamoto, K., Tsuji, H., Mabuchi, T., Ozawa, A., Tamiya, G., 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 : 1171-1180 (2002). [PMID: 12372410]
  4. Lee, S. A., Belyaeva, O. V., Kedishvili, N. Y.
    Biochemical characterization of human epidermal retinol dehydrogenase 2.
    Chem. Biol. Interact. 178 : 182-187 (2009). [PMID: 18926804]

[EC created 1972, modified 2011]