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Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase and Organism(s) Mus musculus and UniProt Accession Q8VCH7

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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 .
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Mus musculus
UNIPROT: Q8VCH7
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
-
-
cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase
RDH5
-
-
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
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
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+
show the reaction diagram
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
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
show the reaction diagram
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
show the reaction diagram
activity with NAD+ is about 10fold higher than with NADP+
-
-
?
11-cis-retinol-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
show the reaction diagram
-
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
show the reaction diagram
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
show the reaction diagram
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
show the reaction diagram
activity with NAD+ is about 8fold higher than with NADP+
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
-
-
-
?
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-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
show the reaction diagram
-
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
show the reaction diagram
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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+
activity with NAD+ is about 10fold higher than with NADP+
additional information
no detectable activity with NADP+
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylpyrazole
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
low mRNA expression
Manually annotated by BRENDA team
mRNA is expressed intensely
Manually annotated by BRENDA team
expression of CRAD2 mRNA is 3% of that in liver
Manually annotated by BRENDA team
low mRNA expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
malfunction
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RDH10_MOUSE
341
2
38075
Swiss-Prot
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sf9 cell
expressed in CHO cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Chai, X.; Zhai, Y.; Napoli, J.L.
cDNA cloning and characterization of a cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase
J. Biol. Chem.
272
33125-33131
1997
Mus musculus (O54909), Mus musculus
Manually annotated by BRENDA team
Su, J.; Chai, X.; Kahn, B.; Napoli, J.L.
cDNA cloning, tissue distribution, and substrate characteristics of a cis-Retinol/3alpha-hydroxysterol short-chain dehydrogenase isozyme.
J. Biol. Chem.
273
17910-17916
1998
Mus musculus (O88451), Mus musculus
Manually annotated by BRENDA team
Parker, R.O.; Crouch, R.K.
Retinol dehydrogenases (RDHs) in the visual cycle
Exp. Eye Res.
91
788-792
2010
Mus musculus
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
Xue, Y.; Sato, S.; Razafsky, D.; Sahu, B.; Shen, S.Q.; Potter, C.; Sandell, L.L.; Corbo, J.C.; Palczewski, K.; Maeda, A.; Hodzic, D.; Kefalov, V.J.
The role of retinol dehydrogenase 10 in the cone visual cycle
Sci. Rep.
7
2390
2017
Mus musculus
Manually annotated by BRENDA team