NADP-retinol dehydrogenase

NADP-retinol dehydrogenase (EC 1.1.1.300, all-trans retinal reductase, all-trans-retinol dehydrogenase, NADP(H)-dependent retinol dehydrogenase/reductase, RDH11, RDH12, RDH13, RDH14, retinol dehydrogenase 12, retinol dehydrogenase 14, retinol dehydrogenase (NADP⁺), RalR1, PSDR1) is an enzyme with systematic name retinol:NADP⁺ oxidoreductase.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

retinol + NADP⁺

\rightleftharpoons

retinal + NADPH + H⁺

This enzyme has greater catalytic efficiency in the reductive direction.

References

↑ Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V., Kim, T., Nelson, P.S. and Kedishvili, N.Y. (2005). "Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C₉ aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids". Biochemistry 44 (18): 7035–7047. doi:10.1021/bi050226k. PMC 2679700. PMID 15865448.
↑ Belyaeva, O.V., Korkina, O.V., Stetsenko, A.V. and Kedishvili, N.Y. (2008). "Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity". FEBS J. 275 (1): 138–147. doi:10.1111/j.1742-4658.2007.06184.x. PMC 2573044. PMID 18039331.
↑ Haeseleer, F., Huang, J., Lebioda, L., Saari, J.C. and Palczewski, K. (1998). "Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal". J. Biol. Chem. 273 (34): 21790–21799. doi:10.1074/jbc.273.34.21790. PMID 9705317.
↑ Kedishvili, N.Y., Chumakova, O.V., Chetyrkin, S.V., Belyaeva, O.V., Lapshina, E.A., Lin, D.W., Matsumura, M. and Nelson, P.S. (2002). "Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1)". J. Biol. Chem. 277: 28909–28915. doi:10.1074/jbc.M202588200. PMID 12036956.

External links

NADP-retinol dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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