MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:
retinol dehydrogenase 12 Inferred from experiment : RDH12 ( Homo sapiens )
retinol dehydrogenase 9 Inferred from experiment : DHRS9 ( Homo sapiens )
retinol dehydrogenase 11 Inferred from experiment : RDH11 ( Homo sapiens )
retinol dehydrogenase 3 Inferred from experiment : DHRS3 ( Homo sapiens )
retinol dehydrogenase 10 Inferred from experiment : RDH10 ( Homo sapiens )
retinol dehydrogenase 8 Inferred from experiment : RDH8 ( Homo sapiens )

In Pathway: the visual cycle I (vertebrates) , retinol biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: NADP-retinol dehydrogenase

Enzyme Commission Synonyms: all-trans retinal reductase (ambiguous), 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

Standard Gibbs Free Energy (ΔrG in kcal/mol): -0.25645447 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Greater catalytic efficiency in the reductive, rather than in the oxidative, direction and localization at the entrance to the mitochondrial matrix suggests that this enzyme may function to protect mitochondria against oxidative stress associated with the highly reactive all-trans-retinal produced from dietary all-trans-β-carotene by EC [Belyaeva08]. Km-values for NADP+ and NADPH are at least 800-fold lower than those for NAD+ and NADH [Kedishvili02, Belyaeva05]. This enzyme differs from EC, retinol dehydrogenase, which prefers NAD+ and NADH.

Citations: [Haeseleer98]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [allopregnanolone + NAD(P)+ ↔ 5-α-pregnane-3,20-dione + NAD(P)H + H+] (
i1: allopregnanolone + NAD+ → 5-α-pregnane-3,20-dione + NADH + H+ (1.1.-.-)

i2: allopregnanolone + NADP+ ← 5-α-pregnane-3,20-dione + NADPH + H+ (

Instance reactions of [testosterone + NAD(P)+ → androst-4-ene-3,17-dione + NAD(P)H + H+] (
i3: testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ (

i4: testosterone + NADP+ ← androst-4-ene-3,17-dione + NADPH + H+ (

Unification Links: KEGG:R08379 , Rhea:25033

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC:

Created 28-Aug-2009 by Caspi R , SRI International


Belyaeva05: Belyaeva OV, Korkina OV, Stetsenko AV, Kim T, Nelson PS, Kedishvili NY (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);7035-47. PMID: 15865448

Belyaeva08: Belyaeva OV, Korkina OV, Stetsenko AV, Kedishvili NY (2008). "Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity." FEBS J 275(1);138-47. PMID: 18039331

Haeseleer98: Haeseleer F, Huang J, Lebioda L, Saari JC, Palczewski K (1998). "Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal." J Biol Chem 273(34);21790-9. PMID: 9705317

Kedishvili02: Kedishvili NY, Chumakova OV, Chetyrkin SV, Belyaeva OV, Lapshina EA, Lin DW, Matsumura M, Nelson PS (2002). "Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1)." J Biol Chem 277(32);28909-15. PMID: 12036956

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed Apr 1, 2015, biocyc13.