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Enzyme Nomenclature
Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.315
Word Map on EC 1.1.1.315
- 1.1.1.315
- retinal
-
retinoids
- 11-cis-retinal
-
chromophore
-
fundus
-
photoreceptors
- all-trans-retinol
-
albipunctatus
-
cralbp
- retinaldehyde
-
retinaldehyde-binding
-
3alpha-hydroxysteroids
- 9-cis-retinol
-
electroretinography
- cis-retinols
-
photoisomerization
- androsterone
-
17beta-hydroxysteroid
-
11-cis-retinaldehyde
-
17beta
-
retinoid-binding
-
interphotoreceptor
-
11-cis-retinoids
-
punctata
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.315
-
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RECOMMENDED NAME
GeneOntology No.
11-cis-retinol dehydrogenase
-
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
11-cis retinol oxidation occurs at a reduced rate in retinal pigment epithelium membranes from Rdh5-/- mice
metabolism
-
RDH11, which can can utilize both cis and trans-retinoid substrates, plays a minor but complementary role to RDH5 in the flow of retinoids during dark adaptation
physiological function
physiological function
-
reconstitution of the visual cycle in HEK-293A cells by co-expressing RDH10, cellular retinaldehyde-binding protein CRALBP, RPE-specific 65-kDa protein RPE65 and lecithin retinol acyltransferase LRAT leads to generation of 11-cis-retinol from all-trans-retinal
physiological function
-
cRDH is involved in the processing of 11-cis-retinal after irradiation of retinal G protein-coupled receptor RGR opsin and plays a role in the visual cycle
physiological function
-
isomerization of 11-cis retinal to all-trans retinal in photoreceptors is the first step in vision. In the retinal pigment epithelium, all-trans retinol is converted to 11-cis retinol, and in the final enzymatic step, 11-cis-retinol is oxidized to 11-cis retinal, catalyzed by the enzyme RDH5. RDH5 does play a significant role in 11-cis retinol oxidation in the retinal pigment epithelium
physiological function
-
mice with a conditional knock-out of isoform Rdh10 in retinal pigmented epithelium cells display delayed 11-cis-retinal regeneration and dark adaption after bright light illumination. Retinal function after light exposure is also delayed in Rdh10 KO mice as compared with controls. Double deletion of isoforms Rdh5 and Rdh10 in mice causes elevated 11/13-cis-retinyl ester content also seen in Rdh5-/- Rdh11-/- mice as compared with Rdh5-/- mice. Normal retinal morphology is observed in 6-month-old Rdh10 KO and Rdh5 and Rdh10 KO mice
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
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+
-
in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal
-
-
r
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+
-
-
-
-
?
all-trans retinol + NAD+
all-trans-retinal + NADH + H+
-
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
-
-
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
-
-
r
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
-
-
?
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
-
-
?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
-
-
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
-
-
?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
activity with NAD+ is about 10fold higher than with NADP+
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
activity with NAD+ is about 10fold higher than with NADP+
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + 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] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
-
-
-
-
r
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
-
-
-
-
?
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
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
-
-
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
-
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
-
-
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
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
activity with NAD+ is about 8fold higher than with NADP+
-
-
?
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+
-
-
?
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
activity with NAD+ is about 8fold higher than with NADP+
-
-
?
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
-
-
r
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+
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
r
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
no significant activity with all-trans-retinol. Rdh5 recognizes 5alpha-androstan-3alpha,17beta-diol (3alpha-adiol) and androsterone as substrates
-
-
-
additional information
?
-
no significant activity with all-trans-retinol. Rdh5 recognizes 5alpha-androstan-3alpha,17beta-diol (3alpha-adiol) and androsterone as substrates
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-cis-retinol + NAD+
11-cis-retinal + NADH
Q92781
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
-
-
?
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
-
-
?
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
-
-
?
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+
-
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
Q92781
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
O54909
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
-
-
?
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
-
-
-
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
-
-
-
additional information
?
-
Q8IZV5
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
isoform RDH10 is strictly NAD+-dependent; 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+
-
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+
-
enzyme can use both NAD+ and NADP+; RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
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+
-
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+ 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+
-
enzyme can use both NAD+ and NADP+; RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
NADPH
-
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
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INHIBITORS
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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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
-
0.0067
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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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
-
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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
45% mRNA expression of Rdh5 compared to liver; 45% of the expression in liver
-
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)
-
97% mRNA expression of Rdh5 compared to liver; 97% of the expression in liver
-
43% mRNA expression of Rdh5 compared to liver; 43% of the expression in liver
additional information
-
highest expression among extra-ocular tissues tested; high mRNA expression of Rdh5
-
a weak but detectable signal is present in normal lung, the 3 kb isoform is the most abundant one
-
RDH10 colocalizes with retinal pigment protein RPE65 and with cellular retinaldehyde-binding protein CRALBP in vivo
additional information
-
mRNA expression is widespread in extra-ocular tissues with human liver and mammary gland showing the most intense signals
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)
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
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pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
the majority of 11-cis retinol dehydrogenase is associated with the smooth ER in retinal pigment epithelial cells. The enzyme is an integral membrane protein, anchored to membranes by two hydrophobic peptide segments. The catalytic domain of the enzyme is confined to a lumenal compartment and is not present on the cytosolic aspect of membranes
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wild-type. All tested RDH5 mutants, including A294P, show an abnormal perinuclear localization in transfected cells and induce a redistribution of the ER marker calnexin
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pronounced 11-cis-retinol dehydrogenase activity is associated with both endoplasmic reticulum- and plasma membrane-enriched membrane fractions. In contrast, 11-cis-retinyl ester hydrolase activity is mostly recovered in plasma membrane-enriched fractions, while lecithin retinol acyl transferase LRAT activity is found only in endoplasmic reticulum-enriched membranes
associated to membrane, and ssequence displays several potential membrane-spanning segments
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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RDH10 physically interacts with RPE65 and with cellular retinaldehyde-binding protein CRALBP
additional information
enzyme associates with p63, an abundant membrane protein in retinal pigment epithelium
additional information
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enzyme copurifies with retinal G protein coupled receptor from microsomes
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
N-terminal 18 amino acids of sequence have the characteristics of a classigal signal sequence
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alignment of Streptomyces hydrogenans 20beta-hydroxysteroid dehydrogenase with rat retinol dehydrogenase and cow 11-cis retinol dehydrogenase. Lysine64 of the rat enzyme is important in stabilizing binding of 2'-phosphate on NADP+ in two ways: lysine's positively charged side chain has a coulombic attraction to the 2'-phosphate and partially compensates for the negative charge of aspartic acid-38. Cow 11-cis retinol dehydrogenase has threonine61 at the position homologous to lysine64. Threonine61 does not have a stabilizing coulombic interaction with NADP+, nor can threonine61 counteract the repulsive interaction between NADP+ and aspartic acid37 in 11-cis retinol dehydrogenase
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modeling of the amino acid sequence of human RDH5 into the known three-dimensional structure of 17-hydroxysteroid dehydrogenase, Protein Data Bank code 1bhs
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of His-tagged enzyme using nickel affinity chromatography results in an inactive enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Cos-1 cells
expression in Sf9 cell
expression in Sf9 cell; RDH10 is expressed the enzyme in insect Sf9 cells using the Baculovirus expression system. Purification of RDH10-His6 from Sf9 cells using nickel affinity chromatography produces an inactive enzyme. Therefore, microsomal preparations of RDH10 are used for its kinetic characterization
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA289-318
results show that the N-terminal hydrophobic domain is a membrane-anchoring domain
A294P
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naturally occuring mutation, 52% of wild-type activity in cell-reporter assay, active in vitro
D128N
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naturally occuring mutation, less than 1% of wild-type activity in cell-reporter assay
G238W
G35S
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naturally occuring mutation, 1.7% of wild-type activity in cell-reporter assay
L105I
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naturally occuring mutation, 1% of wild-type activity in cell-reporter assay
L310EV
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naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
R157W
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naturally occuring mutation, less than 1% of wild-type activity in cell-reporter assay
R280H
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naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
S73F
V212
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naturally occuring mutation with 4bp deletion, frame shift mutant with premature stop codon at position 246
V264G
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naturally occuring mutation, 4% of wild-type activity in cell-reporter assay
additional information
G238W
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naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
G238W
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natural mutation identiied in patient with fundus albipunctatus, about 10% residual activity
S73F
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naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
S73F
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natural mutation identiied in patient with fundus albipunctatus, about 20% residual activity
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
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deletion of the two hydrophobic domains dissociates RDH10 from the membrane and abolishes its activity (mutants DELTA2–23, DELTA293–329 and the double mutant lacking both of these regions)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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mutations in gene RDH5 are associated with fundus albipunctatus, an autosomal recessive eye disease. Characterization of 11 mutants shows that all RDH5 mutants show decreased protein stability and subcellular mislocalization and, in most cases, loss of enzymatic activity in vitro and in vivo. The mutated enzymes, in a transdominant-negative manner, influence the in vivo enzymatic properties of functional variants of the enzyme. Under certain conditions, nonfunctional alleles act in a dominant-negative way on functional but relatively unstable mutated alleles. In heterozygous individuals carrying one wild-type allele, the disease is recessive, probably due to the stability of the wild-type enzyme
medicine
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examination of two unrelated families, each family with two affected members with typical fundus albipunctatus. RDH5 mutations were found in the affected siblings in both families. The proband in one has a homozygotic Gly238Trp missense mutation (GGG to TGG) involving exon 4 and in the other carries compound heterozygotic changes Arg280His (CGC to CAC) and Ala294Pro (GCC to CCC) in exon 5. The disease phenotype is only manifested in family members with two abnormal RDH5 alleles consistent with autosomal recessive inheritance in both pedigrees
medicine
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evaluation of patients with hereditary retinal diseases featuring subretinal spots, i.e. retinitis punctata albescens and fundus albipunctatus, and patients with typical dominant or recessive retinitis pigmentosa for mutations in RDH5. Mutations are found only in two unrelated patients, both with fundus albipunctatus. Mutations segregate with disease in the respective families. Recombinant mutant 11-cis retinol dehydrogenases have reduced activity compared with recombinant enzyme with wild-type sequence
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.315)
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