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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
-
-
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
-
-
-
?
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+
-
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
-
-
-
?
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
-
-
-
?
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
-
-
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
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
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+
-
-
-
r
additional information
?
-
11-cis-retinol + NAD+

11-cis-retinal + NADH
-
-
-
?
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+
-
-
-
?
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
-
-
-
-
?
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
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
?
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+
-
-
-
-
?
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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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+
NAD+ is the preferred cofactor
NAD+
activity with NAD+ is about 10fold higher than with NADP+
NAD+
-
aspartic acid37 and threonine61 are important in the specificity of 11-cis retinol dehydrogenase for NAD+
NAD+
-
NAD+ is preferred over NADP+
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
NADP+
activity with NAD+ is about 10fold higher than with NADP+
NADP+
-
NAD+ is preferred over NADP+
NADPH

-
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
additional information

no cofactor: NADP+
-
additional information
-
no detectable activity with NADP+
-
additional information
-
no detectable activity with 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
-
45% mRNA expression of Rdh5 compared to liver; 45% of the expression in liver
brenda
-
-
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
-
97% mRNA expression of Rdh5 compared to liver; 97% of the expression in 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
-
43% mRNA expression of Rdh5 compared to liver; 43% of the expression in 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
-
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
-
highest expression among extra-ocular tissues tested; high mRNA expression of Rdh5
brenda
-
strong expression, the 3 kb isoform is the most abundant one
brenda
mRNA is expressed intensely
brenda
intense expression of CRAD2 mRNA
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
-
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
-
-
brenda
pigment epithelium and sclera, low mRNA expression
brenda
-
RDH10 colocalizes with retinal pigment protein RPE65 and with cellular retinaldehyde-binding protein CRALBP in vivo
brenda
-
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
additional information

-
mRNA expression is widespread in extra-ocular tissues with human liver and mammary gland showing the most intense signals
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
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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

-
naturally occuring mutation, 4% of wild-type activity in cell-reporter assay, no activity in vitro
G238W
-
natural mutation identiied in patient with fundus albipunctatus, about 10% residual activity
S73F

-
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
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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