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
-
photoisomerization
- cis-retinols
-
electroretinography
-
11-cis-retinaldehyde
-
17beta-hydroxysteroid
-
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
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Cofactor
Cofactor on EC 1.1.1.315 - 11-cis-retinol dehydrogenase
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NAD+
microsomal preparations of RDH10 are not active in presence of NADP+
NAD+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NAD+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
NAD+
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
NAD+
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
NAD+
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
NAD+
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aspartic acid37 and threonine61 are important in the specificity of 11-cis retinol dehydrogenase for NAD+
NADH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NADP+
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH
NADP+
RDH10 can utilize both NAD+ and NADP+ as cofactors for 11-cis-retinol dehydrogenase activity. NAD+ cofactor confers more robust activity
NADP+
the addition of NADP+ resulted 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+
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+
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
NADPH
no significant difference in the binding constants of NADP+ and NADPH versus NAD+ and NADH