Information on EC 1.1.1.315 - 11-cis-retinol dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.315
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RECOMMENDED NAME
GeneOntology No.
11-cis-retinol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
11-cis-retinol-[retinal-binding-protein] + NAD+ = 11-cis-retinal-[retinol-binding-protein] + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
the visual cycle I (vertebrates)
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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11-cis retinol oxidation occurs at a reduced rate in retinal pigment epithelium membranes from Rdh5-/- mice
metabolism
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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
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
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in presence of excess NADH, wild-type catalyzes the reduction of 11-cis-retinal
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r
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 + H+
show the reaction diagram
activity with NAD+ is about 10fold higher than with NADP+
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?
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
11-cis-retinol-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
show the reaction diagram
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?
13-cis-retinol + NAD+
13-cis-retinal + NADH
show the reaction diagram
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?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
show the reaction diagram
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?
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
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
show the reaction diagram
activity with NAD+ is about 8fold higher than with NADP+
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?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NAD+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADH + H+
show the reaction diagram
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?
11-cis-retinol-[cellular retinaldehyde binding protein] + NADP+
11-cis-retinal-[cellular retinaldehyde binding protein] + NADPH + H+
show the reaction diagram
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?
11-cis-retinol-[retinal-binding-protein] + NAD+
11-cis-retinal-[retinol-binding-protein] + NADH + H+
show the reaction diagram
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH
show the reaction diagram
Q92781
Rdh5 catalyses 9-cis-retinol metabolism equally efficiently as 11-cis-retinol metabolism
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?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
show the reaction diagram
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
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?
additional information
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
no cofactor: NADP+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylpyrazole
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0063
11-cis-retinol
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pH 8, 37C
0.0025 - 0.0067
11-cis-retinol-[cellular retinaldehyde binding protein]
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0.0066
9-cis-retinol
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pH 8, 37C
0.002
NAD+
pH 7.4, 37C
0.00069
NADP+
pH 7.4, 37C
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.4
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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, 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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17% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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5% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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26% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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29% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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11% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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8% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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6% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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5% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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45% mRNA expression of Rdh5 compared to liver; 45% of the expression in liver
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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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
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3% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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97% mRNA expression of Rdh5 compared to liver; 97% of the expression in liver
Manually annotated by BRENDA team
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7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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8% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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25% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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28% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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20% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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10% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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5% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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24% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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28% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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21% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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11% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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6% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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22% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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7% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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43% mRNA expression of Rdh5 compared to liver; 43% of the expression in liver
Manually annotated by BRENDA team
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9% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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17% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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25% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
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24% mRNA expression of Rdh5 compared to liver
Manually annotated by BRENDA team
additional information
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mRNA expression is widespread in extra-ocular tissues with human liver and mammary gland showing the most intense signals
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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chemical cross-linking
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 32000, SDS-PAGE
dimer
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2 * 32000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
N-terminal 18 amino acids of sequence have the characteristics of a classigal signal sequence
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme copurifies with retinal G protein coupled receptor from microsomes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in CHO cells
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expression in CHO cells; expression in CHO-K1 cells
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expression in Cos-1 cells
expression in HEK-293 cell
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expression in Hi-5 insect cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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
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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine