1.1.1.315: 11-cis-retinol dehydrogenase
This is an abbreviated version!
For detailed information about 11-cis-retinol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.315
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1.1.1.315
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retinal
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retinoids
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11-cis-retinal
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chromophore
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fundus
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photoreceptors
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all-trans-retinol
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albipunctatus
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cralbp
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retinaldehyde-binding
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3alpha-hydroxysteroids
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retinaldehyde
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9-cis-retinol
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androsterone
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photoisomerization
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cis-retinols
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electroretinography
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11-cis-retinaldehyde
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17beta-hydroxysteroid
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17beta
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medicine
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punctata
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interphotoreceptor
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11-cis-retinoids
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retinoid-binding
- 1.1.1.315
- retinal
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retinoids
- 11-cis-retinal
- chromophore
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fundus
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photoreceptors
- all-trans-retinol
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albipunctatus
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cralbp
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retinaldehyde-binding
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3alpha-hydroxysteroids
- retinaldehyde
- 9-cis-retinol
- androsterone
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photoisomerization
- cis-retinols
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electroretinography
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11-cis-retinaldehyde
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17beta-hydroxysteroid
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17beta
- medicine
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punctata
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interphotoreceptor
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11-cis-retinoids
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retinoid-binding
Reaction
Synonyms
11-cis RD, 11-cis-RDH, 11-cis-retinol dehydrogenase, 11-cis-Ro-DH, atRDH, cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase, CRAD, CRAD2, cRDH, EC 5.2.1.3, RDH10, RDH5, retinol dehydrogenase 10
ECTree
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Substrates Products
Substrates Products on EC 1.1.1.315 - 11-cis-retinol dehydrogenase
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REACTION DIAGRAM
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal
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11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
11-cis-retinol-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
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all-trans retinol + NAD+
all-trans-retinal + NADH + H+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
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all-trans retinol + NADP+
all-trans-retinal + NADPH + H+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
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11-cis-retinol + NAD+
11-cis-retinal + NADH
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism. Substrate specificity and expression locus of Rdh5 suggest that it could serve as both an 11-cis-retinol dehydrogenase in the RPE and a 9-cis-retinol dehydrogenase and/or an androgen dehydrogenase outside of the retinal pigment epithelium
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity. RDH10 may function in the RPE retinoid visual cycle as an 11-cis-retinol dehydrogenase, and thereby partially compensate for the loss of RDH5 function in human patients with fundus albipunctatus
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
activity with NAD+ is about 10fold higher than with NADP+
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
little preference between 9-cis-retinol and 11-cis-retinol. Uses NAD+ as its preferred cofactor
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11-cis-retinal + NADPH + H+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity. RDH10 may function in the RPE retinoid visual cycle as an 11-cis-retinol dehydrogenase, and thereby partially compensate for the loss of RDH5 function in human patients with fundus albipunctatus
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11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
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11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
activity with NAD+ is about 10fold higher than with NADP+
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11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
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11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
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11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
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11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
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11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
cellular retinaldehyde binding protein CRALBP serves as an 11-cis-retinol acceptor for the enzymatic isomerization of all-trans- to 11-cis-retinol and as a substrate carrier for 11-cis-retinol dehydrogenase RDH5. Altered kinetic parameters are observed for RDH5 oxidation of 11-cis-retinol bound to rCRALBP mutants M222A, M225A, and W244F, supporting impaired substrate carrier function. Data implicate Trp165, Met208, Met222, Met225, and Trp244 as components of the CRALBP ligand binding cavity
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11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
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11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
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9-cis-retinol + NAD+
9-cis-retinal + NADH
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
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9-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
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9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
the multifunctional cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase may catalyze the first step in an enzymatic pathway from 9-cis-retinol to generate the retinoid X receptor ligand 9-cis-retinoic acid and/or may regenerate dihydrotestosterone from its catabolite 5alpha-androstan-3alpha,17beta-diol
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9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
activity with NAD+ is about 8fold higher than with NADP+
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9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
little preference between 9-cis-retinol and 11-cis-retinol. Uses NAD+ as its preferred cofactor, activity with NADP+ is 4% of the activity with NAD+
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9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
activity with NAD+ is about 8fold higher than with NADP+
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all-trans-retinal + NADH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH10 is a more efficient retinol dehydrogenase than a retinaldehyde reductase. Microsomal preparations of RDH10 are not active in presence of NADP+
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all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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all-trans-retinal + NADPH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
the addition of NADP+ results in more efficient oxidation of all-trans retinol into all-trans retinal, when compared with the addition of NAD+, suggesting that RDH10 prefers NADP as the cofactor. At assay conditions (pH 5.5 and pH 7.6), and NADH or NADPH is used as the cofactor, only a low level of all-trans retinol is generated by RDH10
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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additional information
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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additional information
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cRDH does not react with endogenous all-trans-retinal bound to retinal G protein-coupled receptor RGR but reacts specifically with 11-cis-retinal that is generated by photoisomerization after irradiation of RGR. The reduction of 11-cis-retinal to 11-cis-retinol by cRDH enhances the net photoisomerization of all-trans-retinal bound to RGR
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additional information
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dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
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additional information
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dual physiological role of isoform RDH10: in the biosynthesis of 11-cis-retinaldehyde for vision and in the biosynthesis of all-trans-retinoic acid for differentiation and development
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additional information
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enzyme does not recognizes retinol bound to cellular retinol-binding protein type I as a substrate and functions exclusively in the oxidative reaction in cells
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additional information
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enzyme does not recognizes retinol bound to cellular retinol-binding protein type I as a substrate and functions exclusively in the oxidative reaction in cells
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additional information
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no significant activity with all-trans-retinol. Rdh5 recognizes 5alpha-androstan-3alpha,17beta-diol (3alpha-adiol) and androsterone as substrates
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additional information
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no significant activity with all-trans-retinol. Rdh5 recognizes 5alpha-androstan-3alpha,17beta-diol (3alpha-adiol) and androsterone as substrates
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additional information
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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additional information
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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additional information
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enzyme additionally exhibits an oxidative 3alpha-hydroxysteroid dehydrogenase activity that can convert 5alpha-androstane-3alpha,17beta-diol (3-diol) into dihydrotestosterone. 11-cis-RoDH could be involved in a non-classical pathway of androgen formation and might play a role in the modulation of the androgenic response in some peripheral tissues
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additional information
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Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism and recognizes 5alpha-androstan-3alpha,17beta-diol and androsterone as substrates, i.e. 3alpha-hydroxysteroid dehydrogenase activity, but not testosterone, dihydrotestosterone, oestradiol and corticosterone
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additional information
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Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism and recognizes 5alpha-androstan-3alpha,17beta-diol and androsterone as substrates, i.e. 3alpha-hydroxysteroid dehydrogenase activity, but not testosterone, dihydrotestosterone, oestradiol and corticosterone
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additional information
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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additional information
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RDH10 does not oxidize 11-cis retinol, 9-cis retinol, or 13-cis retinol into the respective retinal (pH 7.6, in the presence of NAD or NADP+), indicating the substrate specificity of RDH10
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