1.1.1.105: all-trans-retinol dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about all-trans-retinol dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.1.1.105
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1.1.1.105
-
retinoids
-
dystrophy
-
amaurosis
-
photoreceptors
-
leber
-
retinaldehyde
-
pigmentosa
-
dehalogenase
-
all-trans-retinoic
-
retinol-binding
-
all-trans-retinal
-
raldhs
-
darwin
-
dehalococcoides
-
11-cis-retinal
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rpgrip1
-
retinyl
-
dechlorination
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aldh1a2
-
gucy2d
-
all-trans-retinaldehyde
-
cyp26b1
-
cone-rod
-
neurosteroidogenic
-
crabp2
-
albipunctatus
-
organohalide
-
3alpha-hydroxysteroids
-
srd5a1
-
hiding
-
synthesis
-
medicine
- 1.1.1.105
-
retinoids
- dystrophy
- amaurosis
- photoreceptors
-
leber
- retinaldehyde
- pigmentosa
-
dehalogenase
-
all-trans-retinoic
-
retinol-binding
- all-trans-retinal
- raldhs
-
darwin
- dehalococcoides
- 11-cis-retinal
-
rpgrip1
-
retinyl
-
dechlorination
- aldh1a2
-
gucy2d
- all-trans-retinaldehyde
-
cyp26b1
-
cone-rod
-
neurosteroidogenic
-
crabp2
-
albipunctatus
-
organohalide
-
3alpha-hydroxysteroids
- srd5a1
-
hiding
- synthesis
- medicine
Reaction
Synonyms
ADH, alcohol dehydrogenase, all-trans retinol dehydrogenase, all-trans-retinol dehydrogenase, dehydrogenase, retinol, DHRS9, epidermal retinol dehydrogenase 2, LOC100185899, MDR, microsomal retinol dehydrogenase, mRDH1, NAD+-dependent retinoid-active short-chain dehydrogenase/reductase, P32, PDHC, photoreceptor retinol dehydrogenase isoform C, RDH-E2, RDH-like SDR, Rdh1, RDH10, RDH10a, RDH10b, RDH10c, RDH12, RDH16, RDH2, RDH7, RDH8, RDHE2, RDHE2S, RDHL, retinal reductase, retinene reductase, retinoid dehydrogenase/reductase, retinol dehydrogenase (vitamin A1), retinol dehydrogenase 10, retinol dehydrogenase 12, retinol dehydrogenase 2, retinol dehydrogenase 4, retinol dehydrogenase epidermal 2, retinol dehydrogenase epidermal 2-similar, RL-HSD, RoDH-4, RoDH-like 3alpha-hydroxysteroid dehydrogenase, RoDH4, SDR16C5, SDR16C6, XP_2120364
ECTree
1.1.1.105 all-trans-retinol dehydrogenase (NAD+)Advanced search results
results (
results (Substrates Products
Substrates Products on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-didehydroretinol + NAD+
3,4-didehydroretinal + NADH
-
60% of the efficiency against all-trans-retinol
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
higher activity with all-trans-retinol versus 9-cis-retinol
-
-
?
all-trans retinal + NADH + H+
all-trans retinol + NAD+
26.8% of the activity with butan-1-ol
-
-
?
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
-
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
-
-
-
r
retinol bound to cellular retinol binding protein + NAD+
retinal bound to cellular retinol binding protein + NADH
-
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans retinal + NADH + H+
all-trans-retinol + NAD+
-
oxidative activity is below the detection limit
-
-
r
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
RDH5 has only a minor in vivo all-trans RDH activity
-
-
?
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
wild type RDH10 catalyzes both oxidation of all-trans retinol and reduction of all-trans retinal in vitro. On cultured cells, however, oxidation is the favored reaction catalyzed by RDH10.
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
26% activity compared to butyl alcohol
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
26% activity compared to butyl alcohol
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH
in intact cells, the enzyme functions as retinol dehydrogenase, and contributes to the oxidation of retinol, but not to the reduction of retinaldehyde
-
-
ir
all-trans-retinol + NAD+
all-trans-retinal + NADH
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
in intact cells, the enzyme functions as retinol dehydrogenase, and contributes to the oxidation of retinol, but not to the reduction of retinaldehyde
-
-
ir
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
30.2% activity compared to butyl alcohol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
30.2% activity compared to butyl alcohol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 has 811fold higher activity with NAD+ versus NADP+. Higher activity with all-trans-retinol versus 9-cis-retinol. Multifunctional enzyme. In addition to retinol dehydrogenase activity, RDH1 has strong 3alpha-hydroxy and weak 17beta-hydroxy steroid dehydrogenase activities
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1, except for RDH10 that does not access holo-CRBP1 as substrate
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1
-
-
ir
retinal + NADPH + H+
retinol + NADP+
-
activity is lower than with NADH
-
-
?
additional information
?
-
-
negligible activity with 9-cis-retinol
-
-
?
additional information
?
-
-
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid
-
-
?
additional information
?
-
-
substrate bound to cellular retinol binding protein is preferred
-
-
?
additional information
?
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
NAD+-dependent retinoid-active SDRs have higher catalytic efficiencies for the oxidation of 3alpha-hydroxysterols than of retinols
-
-
?
additional information
?
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
additional information
?
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
additional information
?
-
-
enzyme is an alcohol dehydrogenase, EC 1.1.1.1, with activity for all-trans-retinol using NAD+ as a cofactor
-
-
?
additional information
?
-
enzyme is an alcohol dehydrogenase, EC 1.1.1.1, with activity for all-trans-retinol using NAD+ as a cofactor
-
-
?
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
RDH10 is required for proper retinoic acid signalling in the early embryo, RDH10 cooperates with retinal dehydrogenase 2 during axis development and central nervous system patterning
-
-
?
