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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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r
11-cis-retinol + NAD+
11-cis-retinal + NADH
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
11-cis-retinol + NADP+
11-cis-retinal + NADPH
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?
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
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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-
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?
13-cis-retinol + NAD+
13-cis-retinal + NADH
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-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
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-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
9-cis-retinol + NADP+
9-cis-retinal + NADPH
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?
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
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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-
r
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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-
r
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
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r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
all-trans-retinol + NADPH
all-trans-retinal + NADP+
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r
additional information
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11-cis-retinol + NAD+
11-cis-retinal + 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+
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?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
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-
-
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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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r
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-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. 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-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
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-
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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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-
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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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r
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-retinol-[cellular retinaldehyde binding protein] + NADP+
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
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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-retinol + NAD+
9-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
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r
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+
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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-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+
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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r
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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r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
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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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r
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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r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
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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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r
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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r
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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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
?
-
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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?
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NAD+
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NAD+
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NAD+ is preferred over NADP+
NAD+
isoform RDH10 is strictly NAD+-dependent
NAD+
activity with NAD+ is about 10fold higher than with NADP+
NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
NAD+
NAD+ is the preferred cofactor
NAD+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NAD+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
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
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
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
NAD+
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aspartic acid37 and threonine61 are important in the specificity of 11-cis retinol dehydrogenase for NAD+
NAD+
enzyme can use both NAD+ and NADP+
NADH
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NADH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NADP+
-
NAD+ is preferred over NADP+
NADP+
activity with NAD+ is about 10fold higher than with NADP+
NADP+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NADP+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
NADP+
the addition of NADP+ resulted 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
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
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
NADP+
enzyme can use both NAD+ and NADP+
NADPH
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NADPH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
additional information
-
no detectable activity with NADP+
-
additional information
no detectable activity with NADP+
-
additional information
no cofactor: NADP+
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brenda
17% mRNA expression of Rdh5 compared to liver
brenda
5% mRNA expression of Rdh5 compared to liver
brenda
26% mRNA expression of Rdh5 compared to liver
brenda
29% mRNA expression of Rdh5 compared to liver
brenda
11% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
6% mRNA expression of Rdh5 compared to liver
brenda
5% mRNA expression of Rdh5 compared to liver
brenda
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brenda
fetal brain (5% mRNA expression of Rdh5 compared to adult liver), fetal heart (6% mRNA expression of Rdh5 compared to adultliver), fetal kidney (17% mRNA expression of Rdh5 compared to adult liver), fetal liver (20% mRNA expression of Rdh5 compared to adult liver), fetal spleen (5% mRNA expression of Rdh5 compared to adult liver), fetal thymus (7% mRNA expression of Rdh5 compared to adult liver), fetal lung (14% mRNA expression of Rdh5 compared to liver)
brenda
3% mRNA expression of Rdh5 compared to liver
brenda
7% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
21% mRNA expression of Rdh5 compared to liver
brenda
7% mRNA expression of Rdh5 compared to liver
brenda
8% mRNA expression of Rdh5 compared to liver
brenda
25% mRNA expression of Rdh5 compared to liver
brenda
20% mRNA expression of Rdh5 compared to liver
brenda
21% mRNA expression of Rdh5 compared to liver
brenda
10% mRNA expression of Rdh5 compared to liver
brenda
24% mRNA expression of Rdh5 compared to liver
brenda
28% mRNA expression of Rdh5 compared to liver
brenda
21% mRNA expression of Rdh5 compared to liver
brenda
11% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
6% mRNA expression of Rdh5 compared to liver
brenda
22% mRNA expression of Rdh5 compared to liver
brenda
7% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
17% mRNA expression of Rdh5 compared to liver
brenda
25% mRNA expression of Rdh5 compared to liver
brenda
24% mRNA expression of Rdh5 compared to liver
brenda
low activity
brenda
8% mRNA expression of Rdh5 compared to liver
brenda
45% mRNA expression of Rdh5 compared to liver
brenda
45% of the expression in liver
brenda
26% mRNA expression of Rdh5 compared to liver
brenda
the 3 kb isoform is the most abundant one
brenda
low mRNA expression
brenda
low activity
brenda
37% mRNA expression of Rdh5 compared to liver
brenda
strong expression, the 3 kb isoform is the most abundant one
brenda
mRNA is expressed intensely
brenda
low activity
brenda
high mRNA expression of Rdh5
brenda
strong expression, the 3 kb isoform is the most abundant one
brenda
highest expression among extra-ocular tissues tested
brenda
intense expression of CRAD2 mRNA
brenda
mRNA is expressed intensely
brenda
low activity
brenda
10% mRNA expression of Rdh5 compared to liver
brenda
a weak but detectable signal is present in normal lung, the 3 kb isoform is the most abundant one
brenda
expression of CRAD2 mRNA is 3% of that in liver
brenda
97% mRNA expression of Rdh5 compared to liver
brenda
97% of the expression in liver
brenda
low activity
brenda
28% mRNA expression of Rdh5 compared to liver
brenda
9% mRNA expression of Rdh5 compared to liver
brenda
strong expression, the 3 kb isoform is the most abundant one
brenda
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brenda
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brenda
pigment epithelium and sclera, low mRNA expression
brenda
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brenda
RDH10 colocalizes with retinal pigment protein RPE65 and with cellular retinaldehyde-binding protein CRALBP in vivo
brenda
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-
brenda
high activity
brenda
specific expression
brenda
-
brenda
-
-
brenda
-
brenda
low activity
brenda
5% mRNA expression of Rdh5 compared to liver
brenda
the 3 kb isoform is the most abundant one
brenda
39% mRNA expression of Rdh5 compared to liver
brenda
the 3 kb isoform is the most abundant one
brenda
low mRNA expression
brenda
43% mRNA expression of Rdh5 compared to liver
brenda
43% of the expression in liver
brenda
additional information
no expression in H-460 cells (non-small-cell lung cancer). Very low level of expression is detected in cell lines SKMES (squamous lung cancer) and SCLC (small-cell lung carcinoma)
brenda
additional information
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mRNA expression is widespread in extra-ocular tissues with human liver and mammary gland showing the most intense signals
brenda
additional information
mRNA expression is widespread in extra-ocular tissues with human liver and mammary gland showing the most intense signals
brenda
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DELTA289-318
results show that the N-terminal hydrophobic domain is a membrane-anchoring domain
A294P
naturally occuring mutation, 52% of wild-type activity in cell-reporter assay, active in vitro
D128N
naturally occuring mutation, less than 1% of wild-type activity in cell-reporter assay
D169A
mutant enzyme completely loses enzymatic activity
D169N
mutant enzyme completely loses enzymatic activity
G35S
naturally occuring mutation, 1.7% of wild-type activity in cell-reporter assay
G43A/G47A/G49A
mutant enzyme completely loses enzymatic activity
K214A
mutant enzyme completely loses enzymatic activity
K214R
mutant enzyme completely loses enzymatic activity
L105I
naturally occuring mutation, 1% of wild-type activity in cell-reporter assay
L310EV
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
R157W
naturally occuring mutation, less than 1% of wild-type activity in cell-reporter assay
R280H
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
S197A
mutation does not abolish activity
S197C
mutant enzyme completely loses enzymatic activity
S197G
mutation does not abolish activity
S197T
mutant enzyme completely loses enzymatic activity
S197V
mutant enzyme completely loses enzymatic activity
V212
naturally occuring mutation with 4bp deletion, frame shift mutant with premature stop codon at position 246
V264G
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay
Y210A
mutant enzyme completely loses enzymatic activity
Y210F
mutant enzyme completely loses enzymatic activity
G238W
natural mutation identiied in patient with fundus albipunctatus, about 10% residual activity
G238W
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
S73F
natural mutation identiied in patient with fundus albipunctatus, about 20% residual activity
S73F
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
additional information
introduction of a glycosylation site in mutant 11-cis RDH GM71-73 at positions 71-73, residues NIS. Construction of a mutant protein, 11-cis RDH-HA, with a C-terminal extension of 12 amino acid residues consisting of the hemagglutinin antigenic epitope and a glycosylation site. Results suggest that residues 289-310 of 11-cis RDH are a transmembrane domain and that amino acid residues 311-318 are located in the cytosol
additional information
deletion of the two hydrophobic domains dissociates RDH10 from the membrane and abolishes its activity (mutants DELTA223, DELTA293329 and the double mutant lacking both of these regions)
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