Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase and Organism(s) Homo sapiens and UniProt Accession Q92781

for references in articles please use BRENDA:EC1.1.1.315
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q92781
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
11-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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11-cis-RDH
-
11-cis-retinol dehydrogenase
11-cis-Ro-DH
-
-
RDH10
RDH5
-
-
retinol dehydrogenase 10
-
PATHWAY SOURCE
PATHWAYS
-
-
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].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
show the reaction diagram
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+
show the reaction diagram
11-cis-retinol + NAD+
11-cis-retinal + NADH
show the reaction diagram
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
show the reaction diagram
11-cis-retinol + NADP+
11-cis-retinal + NADPH
show the reaction diagram
-
-
-
?
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
show the reaction diagram
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
show the reaction diagram
-
-
-
?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
show the reaction diagram
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH
show the reaction diagram
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
show the reaction diagram
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
show the reaction diagram
microsomal preparations of RDH10 are not active in presence of NADP+
-
-
r
9-cis-retinol + NADP+
9-cis-retinal + NADPH
show the reaction diagram
-
-
-
?
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
show the reaction diagram
-
-
-
-
?
all-trans retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
show the reaction diagram
all-trans-retinol + NADPH
all-trans-retinal + NADP+
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
11-cis-retinol + NAD+
11-cis-retinal + NADH
show the reaction diagram
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+
show the reaction diagram
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+
show the reaction diagram
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
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH
show the reaction diagram
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
additional information
-
no detectable activity with NADP+
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11-cis-retinol
substrate inhibition above 0.005 mM
9-cis-retinol
substrate inhibition above 0.001 mM
all-trans-retinol
substrate inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 0.0067
11-cis-retinol-[cellular retinaldehyde binding protein]
-
0.0063 - 0.06
11-cis-retinol
0.0066 - 6
9-cis-retinol
0.57
all-trans retinal
pH 7.4, 37°C, wild-type enzyme
0.00018 - 0.0041
all-trans retinol
0.4
all-trans-retinal
0.035
all-trans-retinol
0.002 - 0.1
NAD+
0.11
NADH
pH 7.4, 37°C, wild-type enzyme
0.00069 - 0.027
NADP+
0.015
NADPH
pH 7.4, 37°C, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
wild-type, pH not specified in the publication, temperature not specified in the publication
124000
-
substrate all-trans-retinol, pH 7.4, 37°C
24000
-
substrate 11-cis-retinol, pH 7.4, 37°C
81000
-
substrate 9-cis-retinol, pH 7.4, 37°C
additional information
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
45% of the expression in liver
Manually annotated by BRENDA team
highest expression among extra-ocular tissues tested
Manually annotated by BRENDA team
97% of the expression in liver
Manually annotated by BRENDA team
43% of the expression in liver
Manually annotated by BRENDA team
17% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
5% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
26% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
29% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
11% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
8% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
6% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
5% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
45% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
3% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
97% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
8% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
25% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
28% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
20% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
10% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
24% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
28% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
11% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
6% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
22% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
43% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
17% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
25% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
24% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RDH5_HUMAN
318
0
34979
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
2 * 32000, SDS-PAGE
60000
chemical cross-linking
38087
x * 38087, calculated from sequence
38090
calculated from sequence
39600
x * 39600, SDS-PAGE and calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 32000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
modeling of the amino acid sequence of human RDH5 into the known three-dimensional structure of 17-hydroxysteroid dehydrogenase, Protein Data Bank code 1bhs
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
G238W
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 DELTA2–23, DELTA293–329 and the double mutant lacking both of these regions)
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, some loss of activity after repeated freeze-thawing cycles
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of His-tagged enzyme using nickel affinity chromatography results in an inactive enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in CHO-K1 cells
expression in Cos-1 cells
expression in Hi-5 insect cells
expressed in COS1 cells
expression in CHO cells
expression in Cos-1 cells
expression in HEK-293 cell
-
expression in Sf9 cell
RDH10 is expressed in COS cells
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team