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Literature summary for 1.1.1.300 extracted from

  • Belyaeva, O.V.; Wu, L.; Shmarakov, I.; Nelson, P.S.; Kedishvili, N.Y.
    Retinol dehydrogenase 11 is essential for the maintenance of retinol homeostasis in liver and testis in mice (2018), J. Biol. Chem., 293, 6996-7007 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene rdh11, quantitative enzyme expression analysis Mus musculus

Protein Variants

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

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Mus musculus
-
-

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Mus musculus Q9QYF1
-
-

Source Tissue

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 and Products (Substrate)

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

Synonyms Comment Organism
RDH11
-
Mus musculus
retinaldehyde reductase
-
Mus musculus
retinol dehydrogenase 11
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Mus musculus
NADPH
-
Mus musculus
NADPH preferred cofactor Mus musculus

General Information

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