1.1.1.315: 11-cis-retinol dehydrogenase
This is an abbreviated version!
For detailed information about 11-cis-retinol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.315
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1.1.1.315
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retinal
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retinoids
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11-cis-retinal
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chromophore
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fundus
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photoreceptors
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all-trans-retinol
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albipunctatus
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cralbp
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retinaldehyde-binding
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3alpha-hydroxysteroids
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retinaldehyde
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9-cis-retinol
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androsterone
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photoisomerization
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cis-retinols
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electroretinography
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11-cis-retinaldehyde
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17beta-hydroxysteroid
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17beta
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medicine
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punctata
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interphotoreceptor
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11-cis-retinoids
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retinoid-binding
- 1.1.1.315
- retinal
-
retinoids
- 11-cis-retinal
- chromophore
-
fundus
-
photoreceptors
- all-trans-retinol
-
albipunctatus
-
cralbp
-
retinaldehyde-binding
-
3alpha-hydroxysteroids
- retinaldehyde
- 9-cis-retinol
- androsterone
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photoisomerization
- cis-retinols
-
electroretinography
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11-cis-retinaldehyde
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17beta-hydroxysteroid
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17beta
- medicine
-
punctata
-
interphotoreceptor
-
11-cis-retinoids
-
retinoid-binding
Reaction
Synonyms
11-cis RD, 11-cis-RDH, 11-cis-retinol dehydrogenase, 11-cis-Ro-DH, atRDH, cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase, CRAD, CRAD2, cRDH, EC 5.2.1.3, RDH10, RDH5, retinol dehydrogenase 10
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.315 - 11-cis-retinol dehydrogenase
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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
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
S73F
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
additional information
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
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
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
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)