Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + 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+
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
microsomal preparations of RDH10 are not active in presence of NADP+
-
-
r
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-[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+
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 + 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+
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 + 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
-
-
?
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
-
-
?
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 + 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
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
?
-
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0025 - 0.0067
11-cis-retinol-[cellular retinaldehyde binding protein]
-
0.0063 - 0.06
11-cis-retinol
0.57
all-trans retinal
pH 7.4, 37°C, wild-type enzyme
0.00018 - 0.0041
all-trans retinol
0.11
NADH
pH 7.4, 37°C, wild-type enzyme
0.015
NADPH
pH 7.4, 37°C, wild-type enzyme
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
-
0.0063
11-cis-retinol
pH 8, 37°C
0.06
11-cis-retinol
microsomal preparations of RDH10
0.0066
9-cis-retinol
pH 8, 37°C
0.04
9-cis-retinol
microsomal preparations of RDH10
0.00018
all-trans retinol
pH 7.4, 37°, mutynt enzyme S197A
0.0011
all-trans retinol
pH 7.4, 37°C, mutant enzyme S197G
0.0041
all-trans retinol
pH 7.4, 37°C, wild-type enzyme
0.4
all-trans-retinal
-
0.4
all-trans-retinal
microsomal preparations of RDH10
0.035
all-trans-retinol
-
0.035
all-trans-retinol
microsomal preparations of RDH10, cofactor: NAD+
0.002
NAD+
pH 7.4, 37°C
0.036
NAD+
pH 7.4, 37°C, wild-type enzyme
0.1
NAD+
microsomal preparations of RDH10
0.00069
NADP+
pH 7.4, 37°C
0.027
NADP+
pH 7.4, 37°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
45% of the expression in liver
brenda
highest expression among extra-ocular tissues tested
brenda
97% of the expression in liver
brenda
43% of the expression in liver
brenda
-
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
8% 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
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
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
28% 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
-
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
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
26% mRNA expression of Rdh5 compared to liver
brenda
the 3 kb isoform is the most abundant one
brenda
37% mRNA expression of Rdh5 compared to liver
brenda
strong expression, the 3 kb isoform is the most abundant one
brenda
high mRNA expression of Rdh5
brenda
strong expression, the 3 kb isoform is the most abundant one
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
9% mRNA expression of Rdh5 compared to liver
brenda
strong expression, the 3 kb isoform is the most abundant one
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
additional information
-
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
G35S
naturally occuring mutation, 1.7% of wild-type activity in cell-reporter assay
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
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
D169A
mutant enzyme completely loses enzymatic activity
D169N
mutant enzyme completely loses enzymatic activity
G43A/G47A/G49A
mutant enzyme completely loses enzymatic activity
K214A
mutant enzyme completely loses enzymatic activity
K214R
mutant enzyme completely loses enzymatic activity
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
Y210A
mutant enzyme completely loses enzymatic activity
Y210F
mutant enzyme completely loses enzymatic activity
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)
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Belyaeva, O.V.; Johnson, M.P.; Kedishvili, N.Y.
Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase
J. Biol. Chem.
283
20299-20308
2008
Homo sapiens, Homo sapiens (Q8IZV5)
brenda
Wang, J.; Chai, X.; Eriksson, U.; Napoli, J.L.
Activity of human 11-cis-retinol dehydrogenase (Rdh5) with steroids and retinoids and expression of its mRNA in extra-ocular human tissue.
Biochem. J.
338
23-27
1999
Homo sapiens, Homo sapiens (Q92781)
brenda
Takahashi, Y.; Moiseyev, G.; Farjo, K.; Ma, J.X.
Characterization of key residues and membrane association domains in retinol dehydrogenase 10
Biochem. J.
419
113-122
2009
Homo sapiens (Q8IZV5)
brenda
Picozzi, P.; Marozzi, A.; Fornasari, D.; Benfante, R.; Barisani, D.; Meneveri, R.; Ginelli, E.
Genomic organization and transcription of the human retinol dehydrogenase 10 (RDH10) gene
FEBS Lett.
554
59-66
2003
Homo sapiens (Q8IZV5)
brenda
Wu, B.X.; Chen, Y.; Chen, Y.; Fan, J.; Rohrer, B.; Crouch, R.K.; Ma, J.X.
Cloning and characterization of a novel all-trans retinol short-chain dehydrogenase/reductase from the RPE
Invest. Ophthalmol. Vis. Sci.
43
3365-3372
2002
Bos taurus (Q8HZT6), Bos taurus, Homo sapiens (Q8IZV5), Homo sapiens, Mus musculus (Q8VCH7), Mus musculus
brenda
Farjo, K.M.; Moiseyev, G.; Takahashi, Y.; Crouch, R.K.; Ma, J.X.
RDH10 has 11-cis-retinol dehydrogenase activity and interacts with visual cycle proteins.
Invest. Ophthalmol. Vis. Sci.
50
5089-5097
2009
Bos taurus (Q8HZT6), Bos taurus, Homo sapiens (Q8IZV5), Homo sapiens
brenda
Liden, M.; Romert, A.; Tryggvason, K.; Persson, B.; Eriksson, U.
Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus
J. Biol. Chem.
276
49251-49257
2001
Homo sapiens (Q92781), Homo sapiens
brenda
Wu, Z.; Yang, Y.; Shaw, N.; Bhattacharya, S.; Yan, L.; West, K.; Roth, K.; Noy, N.; Qin, J.; Crabb, J.W.
Mapping the ligand binding pocket in the cellular retinaldehyde binding protein
J. Biol. Chem.
278
12390-12396
2003
Homo sapiens (Q92781), Homo sapiens
brenda
Huang, X.F.; Luu-The, V.
Modulation of the androgenic response by recombinant human 11-cis retinol dehydrogenase
J. Steroid Biochem. Mol. Biol.
77
129-133
2001
Homo sapiens
brenda
Gonzalez-Fernandez, F.; Kurz, D.; Bao, Y.; Newman, S.; Conway, B.; Young, J.; Han, D.; Khani, S.
11-cis Retinol dehydrogenase mutations as a major cause of the congenital night-blindness disorder known as fundus albipunctatus
Mol. Vis.
5
XI-XII
1999
Homo sapiens (Q92781)
-
brenda
Yamamoto, H.; Simon, A.; Eriksson, U.; Harris, E.; Berson, E.L.; Dryja, T.P.
Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
Nat. Genet.
22
188-191
1999
Homo sapiens (Q92781)
brenda
Sahu, B.; Sun, W.; Perusek, L.; Parmar, V.; Le, Y.Z.; Griswold, M.D.; Palczewski, K.; Maeda, A.
Conditional ablation of retinol dehydrogenase 10 in the retinal pigmented epithelium causes delayed dark adaption in mice
J. Biol. Chem.
290
27239-27247
2015
Homo sapiens, Mus musculus (Q8VCH7)
brenda