1.1.1.315 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal Homo sapiens 11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ - r 416041 1.1.1.315 11-cis-retinol + NAD+ - Homo sapiens 11-cis-retinal + NADH - ? 186928 1.1.1.315 11-cis-retinol + NAD+ 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 Homo sapiens 11-cis-retinal + NADH - ? 186928 1.1.1.315 11-cis-retinol + NAD+ - Homo sapiens 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NAD+ - Bos taurus 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NAD+ 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 Homo sapiens 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NAD+ activity with NAD+ is about 10fold higher than with NADP+ Mus musculus 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NAD+ little preference between 9-cis-retinol and 11-cis-retinol. Uses NAD+ as its preferred cofactor Mus musculus 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NAD+ microsomal preparations of RDH10 are not active in presence of NADP+ Homo sapiens 11-cis-retinal + NADH + H+ - r 383590 1.1.1.315 11-cis-retinol + NAD+ RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity Homo sapiens 11-cis-retinal + NADH + H+ - ? 383590 1.1.1.315 11-cis-retinol + NADP+ - Homo sapiens 11-cis-retinal + NADPH - ? 383591 1.1.1.315 11-cis-retinol + NADP+ 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 Homo sapiens 11-cis-retinal + NADPH + H+ - ? 383592 1.1.1.315 11-cis-retinol + NADP+ activity with NAD+ is about 10fold higher than with NADP+ Mus musculus 11-cis-retinal + NADPH + H+ - ? 383592 1.1.1.315 11-cis-retinol + NADP+ RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity Homo sapiens 11-cis-retinal + NADPH + H+ - ? 383592 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ - Bos taurus 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ - ? 415527 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ - Homo sapiens 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ - ? 415527 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ - Homo sapiens 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ - r 415527 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+ 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 Homo sapiens 11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+ - ? 415527 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+ - Bos taurus 11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+ - ? 415528 1.1.1.315 11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+ - Homo sapiens 11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+ - ? 415528 1.1.1.315 11-cis-retinol-[retinal-binding-protein] + NAD+ - Mus musculus 11-cis-retinal-[retinol-binding-protein] + NADH + H+ - ? 424444 1.1.1.315 13-cis-retinol + NAD+ - Homo sapiens 13-cis-retinal + NADH - ? 186929 1.1.1.315 13-cis-retinol + NAD+ - Mus musculus 13-cis-retinal + NADH + H+ - ? 398629 1.1.1.315 9-cis-retinol + NAD+ - Homo sapiens 9-cis-retinal + NADH - ? 186927 1.1.1.315 9-cis-retinol + NAD+ Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism Homo sapiens 9-cis-retinal + NADH - ? 186927 1.1.1.315 9-cis-retinol + NAD+ 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 Mus musculus 9-cis-retinal + NADH + H+ - ? 384017 1.1.1.315 9-cis-retinol + NAD+ activity with NAD+ is about 8fold higher than with NADP+ Mus musculus 9-cis-retinal + NADH + H+ - ? 384017 1.1.1.315 9-cis-retinol + NAD+ 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+ Mus musculus 9-cis-retinal + NADH + H+ - ? 384017 1.1.1.315 9-cis-retinol + NAD+ microsomal preparations of RDH10 are not active in presence of NADP+ Homo sapiens 9-cis-retinal + NADH + H+ - r 384017 1.1.1.315 9-cis-retinol + NADP+ - Homo sapiens 9-cis-retinal + NADPH - ? 187639 1.1.1.315 9-cis-retinol + NADP+ - Homo sapiens 9-cis-retinal + NADPH + H+ - ? 372216 1.1.1.315 9-cis-retinol + NADP+ activity with NAD+ is about 8fold higher than with NADP+ Mus musculus 9-cis-retinal + NADPH + H+ - ? 372216 1.1.1.315 all-trans retinol + NAD+ no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH Homo sapiens all-trans-retinal + NADH + H+ - r 399901 1.1.1.315 all-trans retinol + NADP+ no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH Homo sapiens all-trans-retinal + NADPH + H+ - r 399902 1.1.1.315 all-trans-retinal + NADPH + H+ - Homo sapiens all-tans-retinol + NADP+ - r 384148 1.1.1.315 all-trans-retinol + NAD+ - Mus musculus all-trans-retinal + NADH + H+ - ? 384149 1.1.1.315 all-trans-retinol + NAD+ RDH10 is a more efficient retinol dehydrogenase than a retinaldehyde reductase. Microsomal preparations of RDH10 are not active in presence of NADP+ Homo sapiens all-trans-retinal + NADH + H+ - r 384149 1.1.1.315 all-trans-retinol + NAD+ 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 Homo sapiens all-trans-retinal + NADH + H+ - r 384149 1.1.1.315 all-trans-retinol + NAD+ 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 Mus musculus all-trans-retinal + NADH + H+ - r 384149 1.1.1.315 all-trans-retinol + NAD+ 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 Bos taurus all-trans-retinal + NADH + H+ - r 384149 1.1.1.315 all-trans-retinol + NADP+ - Homo sapiens all-trans-retinal + NADPH + H+ - ? 370852 1.1.1.315 all-trans-retinol + NADP+ 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 Homo sapiens all-trans-retinal + NADPH + H+ - r 370852 1.1.1.315 all-trans-retinol + NADP+ 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 Mus musculus all-trans-retinal + NADPH + H+ - r 370852 1.1.1.315 all-trans-retinol + NADP+ 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 Bos taurus all-trans-retinal + NADPH + H+ - r 370852 1.1.1.315 all-trans-retinol + NADPH - Homo sapiens all-trans-retinal + NADP+ - r 396373 1.1.1.315 additional information 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 Homo sapiens ? - ? 89 1.1.1.315 additional information 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 Homo sapiens ? - ? 89 1.1.1.315 additional information no significant activity with all-trans-retinol. Rdh5 recognizes 5alpha-androstan-3alpha,17beta-diol (3alpha-adiol) and androsterone as substrates Homo sapiens ? - ? 89 1.1.1.315 additional information 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 Homo sapiens ? - ? 89 1.1.1.315 additional information 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 Mus musculus ? - ? 89 1.1.1.315 additional information 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 Bos taurus ? - ? 89 1.1.1.315 additional information 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 Bos taurus ? - ? 89 1.1.1.315 additional information 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 Homo sapiens ? - ? 89 1.1.1.315 additional information 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 Homo sapiens ? - ? 89