Cloned (Comment) | Organism |
---|---|
gene rdh11, quantitative enzyme expression analysis | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of RDH11 knockout (KO) mice, phenotypes, overview | Mus musculus |
additional information | generation of enzyme knockout Rdh11-/- mice | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Mus musculus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
all-trans-retinal + NADPH + H+ | Mus musculus | - |
all-trans-retinol + NADP+ | - |
? | |
retinol + NADP+ | Mus musculus | - |
retinal + NADPH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q9QYF1 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
embryonic fibroblast | MEF | Mus musculus | - |
epithelium | - |
Mus musculus | - |
eye | - |
Mus musculus | - |
hepatic stellate cell | quantitative PCR enzyme expression analysis | Mus musculus | - |
hepatocyte | - |
Mus musculus | - |
hepatocyte | primary, quantitative PCR enzyme expression analysis | Mus musculus | - |
hepatoma cell | reduced RDH11 expression level compared to hepatocytes | Mus musculus | - |
intestine | - |
Mus musculus | - |
intestine | low level expression | Mus musculus | - |
liver | - |
Mus musculus | - |
liver | low level expression. No differences are observed in the microsomal retinaldehyde reductase activities from livers of male versus female mice | Mus musculus | - |
lung | - |
Mus musculus | - |
lung | moderate level expression | Mus musculus | - |
additional information | RDH11 protein is most abundant in testis microsomes, with lower levels detectable in microsomes from liver, lung, and intestine. The rate of retinaldehyde reduction to retinol by the microsomes isolated from RDH11-null testis is 3fold lower compared with wild-type testis microsomes. Similarly to testis microsomes, liver microsomes lacking RDH11 show a lower rate (1.7fold) of retinaldehyde reduction. No differences are observed in the microsomal retinaldehyde reductase activities from livers of male versus female mice | Mus musculus | - |
retina | - |
Mus musculus | - |
retinal pigment epithelium | - |
Mus musculus | - |
testis | - |
Mus musculus | - |
testis | high level expression | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
all-trans-retinal + NADPH + H+ | - |
Mus musculus | all-trans-retinol + NADP+ | - |
? | |
retinol + NADP+ | - |
Mus musculus | retinal + NADPH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RDH11 | - |
Mus musculus |
retinaldehyde reductase | - |
Mus musculus |
retinol dehydrogenase 11 | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Mus musculus | |
NADPH | - |
Mus musculus | |
NADPH | preferred cofactor | Mus musculus |
General Information | Comment | Organism |
---|---|---|
evolution | retinol dehydrogenase 11 (RDH11) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. A mild reduction in retinoic acid signaling is observed in RDH11-null testis | Mus musculus |
evolution | RDH11 is co-expressed with BCO1 in several mouse tissues, and the retinaldehyde reductase activity of RDH11 is conserved in the mouse enzyme | Mus musculus |
malfunction | microsomes isolated from the testes and livers of Rdh11-/- mice fed a regular diet exhibit a 3 and 1.7fold lower rate of all-trans-retinaldehyde conversion to all-trans-retinol, respectively, than the microsomes of wild-type littermates. Testes and livers of Rdh11-/- mice fed a vitamin A-deficient diet have about 35% lower levels of all-trans-retinol than those of wild-type mice. Oxidative NAD+-dependent retinol dehydrogenase activity is not affected by inactivation of the rdh11 gene, while similarly to testis microsomes, liver microsomes lacking RDH11 show a lower rate (1.7fold) of retinaldehyde reduction. In lungs and intestines, the microsomal retinaldehyde reductase activities are comparable between RDH11-null mice and their wild-type littermates | Mus musculus |
malfunction | microsomes isolated from the testes and livers of Rdh11-/- mice fed a regular diet exhibited a 3 and 1.7fold lower rate of all-trans-retinaldehyde conversion to all-trans-retinol, respectively, than the microsomes of wild-type littermates. Testes and livers of Rdh11-/- mice fed a vitamin A-deficient diet have about 35% lower levels of all-trans-retinol than those of wild-type mice the conversion of beta-carotene to retinol via retinaldehyde as an intermediate appeared to be impaired in the testes of Rdh11-/-/retinol-binding protein 4-/- (Rbp4-/-) mice, which lack circulating holo RBP4 and rely on dietary supplementation with beta-carotene for maintenance of their retinoid stores. Overnight starvation results in a decrease in the amount of RDH11 in livers of fasted mice. Gene expression pattern indicates a mild reduction in retinoic acid signaling in RDH11-null testis. The oxidative NAD+-dependent retinol dehydrogenase activity is not affected by inactivation of the Rdh11 gene. The conversion of retinaldehyde to retinol in whole mouse embryonic fibroblasts (MEFs) lacking RDH11 occurs at a slower rate than in wild-type MEFs | Mus musculus |
metabolism | retinaldehyde can be produced in the cells by the oxidation of retinol or by the cleavage of beta-carotene at its central double bond (15,15') catalyzed by cytosolic BCO1. In rodents, cleavage of beta-carotene to retinaldehyde with subsequent conversion of retinaldehyde to retinol occurs mainly in the small intestine. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet | Mus musculus |
physiological function | retinol dehydrogenase 11 (RDH11) is a microsomal short-chain dehydrogenase/reductase that recognizes all-trans- and cis-retinoids as substrates and prefers NADPH as a cofactor. RDH11 contributes to the oxidation of 11-cis-retinol to 11-cis-retinaldehyde during the visual cycle in the eye's retinal pigment epithelium. The intestinal microsomes produce two products within the short 15-min incubations with retinaldehyde: retinol and retinyl esters. This suggests that, in the intestinal microsomes, the retinaldehyde reductase activity is coordinated with the retinol esterifying activity, possibly to ensure a highly efficient processing of retinaldehyde into retinyl esters for packaging into chylomicrons. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet, and RDH11 is essential for the maintenance of retinol levels in liver and testis of mice during dietary vitamin A deficiency | Mus musculus |
physiological function | RDH11 contributes to the oxidation of 11-cis-retinol to 11-cis-retinaldehyde during the visual cycle in the eye's retinal pigment epithelium. In mouse testis and liver, RDH11 functions as an all-trans-retinaldehyde reductase essential for the maintenance of physiological levels of all-trans-retinol under reduced vitamin A availability. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet | Mus musculus |