The Enzyme Database

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EC 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, KEGG, MetaCyc, 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]
 
 
EC 1.1.1.315     
Accepted name: 11-cis-retinol dehydrogenase
Reaction: 11-cis-retinol—[retinal-binding-protein] + NAD+ = 11-cis-retinal—[retinol-binding-protein] + NADH + H+
Glossary: 11-cis-retinal = 11-cis-retinaldehyde
Other name(s): RDH5 (gene name)
Systematic name: 11-cis-retinol:NAD+ oxidoreductase
Comments: This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal [1] while the substrate is bound to the retinal-binding protein [4]. This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Simon, A., Hellman, U., Wernstedt, C. and Eriksson, U. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270 (1995) 1107–1112. [DOI] [PMID: 7836368]
2.  Wang, J., Chai, X., Eriksson, U. and Napoli, J.L. Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue. Biochem. J. 338 (1999) 23–27. [PMID: 9931293]
3.  Liden, M., Romert, A., Tryggvason, K., Persson, B. and Eriksson, U. Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus. J. Biol. Chem. 276 (2001) 49251–49257. [DOI] [PMID: 11675386]
4.  Wu, Z., Yang, Y., Shaw, N., Bhattacharya, S., Yan, L., West, K., Roth, K., Noy, N., Qin, J. and Crabb, J.W. Mapping the ligand binding pocket in the cellular retinaldehyde binding protein. J. Biol. Chem. 278 (2003) 12390–12396. [DOI] [PMID: 12536149]
[EC 1.1.1.315 created 2011]
 
 
EC 5.2.1.3      
Deleted entry: retinal isomerase. Now known to be catalysed by a pathway involving EC 1.1.1.300, NADP-retinol dehydrogenase; EC 2.3.1.135, phosphatidylcholine—retinol O-acyltransferase; EC 3.1.1.64, retinoid isomerohydrolase; and EC 1.1.1.315, 11-cis-retinol dehydrogenase.
[EC 5.2.1.3 created 1961, modified 1976, deleted 2011]
 
 


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