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Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.315
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.315 11-cis-retinol dehydrogenase
IUBMB Comments
This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal while the substrate is bound to the retinal-binding protein . This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.1.1.315
- retinal
-
retinoids
- 11-cis-retinal
- chromophore
-
fundus
-
photoreceptors
- all-trans-retinol
-
albipunctatus
-
cralbp
-
retinaldehyde-binding
-
3alpha-hydroxysteroids
- retinaldehyde
- 9-cis-retinol
- androsterone
-
photoisomerization
- cis-retinols
-
electroretinography
-
11-cis-retinaldehyde
-
17beta-hydroxysteroid
-
17beta
- medicine
-
punctata
-
interphotoreceptor
-
11-cis-retinoids
-
retinoid-binding
Reaction Schemes
show11-cis-retinol-[retinal-binding-protein]
+
=
11-cis-retinal-[retinol-binding-protein]
+
+
Synonyms
11-cis-retinol dehydrogenase, 11-cis-rdh, crad2, atrdh, 11-cis rd, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
11-cis-RDH
11-cis-retinol dehydrogenase
atRDH
cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase
EC 5.2.1.3
-
-
formerly, part transferred
-
RDH10
RDH5
cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase
multifunctional enzyme
cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase
multifunctional enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
the visual cycle I (vertebrates)
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SYSTEMATIC NAME
IUBMB Comments
11-cis-retinol:NAD+ oxidoreductase
This enzyme, abundant in the retinal pigment epithelium, catalyses the reduction of 11-cis-retinol to 11-cis-retinal [1] while the substrate is bound to the retinal-binding protein [4]. This is a crucial step in the regeneration of 11-cis-retinal, the chromophore of rhodopsin. The enzyme can also accept other cis forms of retinol [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
Substrates: in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal
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r
11-cis-retinol + NADP+
11-cis-retinal + NADPH
Substrates: -
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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+
-
Substrates: -
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?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
Substrates: -
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?
all-trans retinol + NAD+
all-trans-retinal + NADH + H+
Substrates: 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+
Substrates: 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+
Substrates: -
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r
all-trans-retinol + NADPH
all-trans-retinal + NADP+
Substrates: -
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r
11-cis-retinol + NAD+
11-cis-retinal + NADH
Substrates: 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+
Substrates: -
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?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
Substrates: 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+
Substrates: 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+
Substrates: 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+
Substrates: activity with NAD+ is about 10fold higher than with NADP+
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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
Substrates: 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+
Substrates: 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+
Substrates: 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+
Substrates: 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+
-
Substrates: -
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
Substrates: -
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
Substrates: -
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r
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
Substrates: -
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
Substrates: 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+
-
Substrates: -
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
Substrates: -
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH
Substrates: 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+
Substrates: 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+
Substrates: 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+
Substrates: activity with NAD+ is about 8fold higher than with NADP+
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
Substrates: 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+
Substrates: activity with NAD+ is about 8fold higher than with NADP+
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all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
Substrates: 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+
Substrates: 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+
Substrates: 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+
Substrates: -
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?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
Substrates: 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+
Substrates: 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+
-
Substrates: -
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?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
Substrates: 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+
Substrates: 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
?
-
Substrates: 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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-
-
Substrates: 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
?
-
-
Substrates: 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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-
Substrates: 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
?
-
Substrates: 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
?
-
-
Substrates: 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
?
-
Substrates: 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
?
-
-
Substrates: 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
?
-
Substrates: 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
?
-
Substrates: 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
?
-
-
Substrates: 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
?
-
-
Substrates: 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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-
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Substrates: 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
?
-
Substrates: 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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Products: -
?
additional information
?
-
Substrates: 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
?
-
-
Substrates: 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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-cis-retinol + NAD+
11-cis-retinal + NADH
Substrates: 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
Products: -
Products: -
?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
Substrates: 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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Products: -
?
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
Substrates: 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-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
-
Substrates: -
Products: -
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
-
Substrates: -
Products: -
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?
11-cis-retinol-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
-
Substrates: -
Products: -
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH
Substrates: Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
Products: -
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
Substrates: 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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?
additional information
?
-
-
Substrates: 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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Products: -
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additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
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+
-
aspartic acid37 and threonine61 are important in the specificity of 11-cis retinol dehydrogenase for NAD+
NADH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
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
NADPH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellular retinaldehyde-binding protein
RDH10 oxidizes 11-cis-retinol to generate 11-cis-retinaldehyde in vitro in the presence of cellular retinaldehyde-binding protein
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Eye Diseases
Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus.
Night Blindness
Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus.
Night Blindness
Treatment of a retinal dystrophy, fundus albipunctatus, with oral 9-cis-{beta}-carotene.
Retinal Dystrophies
Treatment of a retinal dystrophy, fundus albipunctatus, with oral 9-cis-{beta}-carotene.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
11-cis-retinol-[cellular retinaldehyde binding protein]
wild-type cellular retinaldehyde binding protein, recombinant wild-type RDH5, pH 7.5, temperature not specified in the publication
-
0.0063
11-cis-retinol-[cellular retinaldehyde binding protein]
pH 8.0, 37°C
-
0.0067
11-cis-retinol-[cellular retinaldehyde binding protein]
wild-type, pH not specified in the publication, temperature not specified in the publication
-
additional information
additional information
the enzyme exhibits cooperative kinetics for 9-cis-retinol with a K0.5 value of 0.0054 mM and a Hill coefficient of 1.7. The enzyme recognized 11-cis-retinol as substrate with a K0.5 value of 0.0076 and a Hill coefficient of 2.8
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additional information
additional information
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the enzyme exhibits cooperative kinetics for 9-cis-retinol with a K0.5 value of 0.0054 mM and a Hill coefficient of 1.7. The enzyme recognized 11-cis-retinol as substrate with a K0.5 value of 0.0076 and a Hill coefficient of 2.8
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
wild-type, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
specific activity is sevenfold higher in the presence of NAD+ cofactor, 69.44 picomoles/mg membrane protein/min, than in the presence of NADP+ cofactor, 9.66 picomoles/mg membrane protein/min, pH 7.4, 37°C
additional information
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specific activity is sevenfold higher in the presence of NAD+ cofactor, 69.44 picomoles/mg membrane protein/min, than in the presence of NADP+ cofactor, 9.66 picomoles/mg membrane protein/min, pH 7.4, 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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