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(E)-4-hydroxy-2-nonenal + NADPH + H+
(E)-4-hydroxy-2-nonenol + NADP+
11-cis-retinal + NADH + H+
11-cis-retinol + NAD+
NADH much less efficient than NADPH
-
-
r
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
11-cis-retinol + NADP+
11-cis-retinal + NADPH
-
-
-
?
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
possibly involved in the production of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments
-
-
r
13-cis-retinal + NADPH
13-cis-retinol + NADP+
-
-
-
r
13-cis-retinal + NADPH + H+
13-cis-retinol + NADP+
-
4fold lower activity than with all-trans-retinal
-
-
?
13-cis-retinol + NADP+
13-cis-retinal + NADPH + H+
-
-
-
r
9-cis-retinal + NADPH
9-cis-retinol + NADP+
-
-
-
r
9-cis-retinal + NADPH + H+
9-cis-retinol + NADP+
-
60fold lower activity than with all-trans-retinal
-
-
?
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
all-trans retinal + NADH + H+
all-tans-retinol + NAD+
NADH much less efficient than NADPH
-
-
r
all-trans retinal + NADH + H+
all-trans-retinol + NAD+
prefers NADP+ and NADPH as cofactors
-
-
r
all-trans retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
r
all-trans retinal + NADPH + H+
all-trans-retinol + NADP+
prefers NADP+ and NADPH as cofactors
-
-
r
all-trans-3-hydroxyretinal + NADH + H+
all-trans-3-hydroxyretinol + NAD+
catalytic efficiency towards all-trans-3-hydroxyretinal is lower than that towards all-trans retinal, prefers NADP+ and NADPH as cofactors
-
-
?
all-trans-3-hydroxyretinal + NADPH + H+
all-trans-3-hydroxyretinol + NADP+
catalytic efficiency towards all-trans-3-hydroxyretinal is lower than that towards all-trans retinal, prefers NADP+ and NADPH as cofactors
-
-
?
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
low activity with NAD+ as cofactor
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
cis-6-nonenal + NADPH + H+
?
-
good substrate of RDH11 and RDH12, while RHD10 has very low activity towards this substrate
-
-
?
estrone + NADH + H+
estradiol + NAD+
n-nonanal + NADPH + H+
n-nonanol + NADP+
retinal + NAD+
retinoic acid + NADH + H+
-
-
-
-
?
retinal + NADH
retinol + NAD+
-
-
-
-
?
retinal + NADH + H+
retinol + NAD+
-
-
-
r
retinal + NADPH + H+
retinol + NADP+
retinol + NAD+
retinal + NADH
-
-
-
-
?
retinol + NAD+
retinal + NADH + H+
retinol + NADP+
retinal + NADPH
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
retinol bound to cellular retinol binding protein + NADP+
retinal bound to cellular retinol binding protein + NADPH
-
-
-
-
?
trans-2-nonenal + NADPH + H+
?
-
good substrate of RDH11 and RDH12, while RHD10 has very low activity towards this substrate
-
-
?
additional information
?
-
(E)-4-hydroxy-2-nonenal + NADPH + H+
(E)-4-hydroxy-2-nonenol + NADP+
-
-
-
?
(E)-4-hydroxy-2-nonenal + NADPH + H+
(E)-4-hydroxy-2-nonenol + NADP+
Rdh12 is able to efficiently detoxify 4-hydroxynonenal in cells, most probably through its ability to reduce it to a nontoxic alcohol
-
-
?
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
?
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
-
?
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
r
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
r
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
r
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
-
?
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
The reverse reaction, oxidation of all-trans-retinol, is not catalyzed by mRDH11
-
-
ir
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
-
-
-
?
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
-
-
-
r
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
possibly involved in the first step of 9-cis-retinoic acid production
-
-
r
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
-
-
-
?
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
?
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
r
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
The reverse reaction, oxidation of all-trans-retinol, is not catalyzed by mRDH11
-
-
ir
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
involved in the regeneration of bleached visual pigments in photoreceptor cells, involved in retinol metabolism outside of photoreceptor cells
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
greater catalytic efficiency in the reductive than in the oxidative direction. Localization of RDH13 at the entrance to the mitochondrial matrix suggests that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
prefers NADPH to NADH as a cofactor. Activity in presence of 1 mM NADPH is about 20fold greater than that in the presence of 1 mM NADH
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
RDH12 is dispensable in support of the visual cycle but appears to be a key component in clearance of free all-trans-retinal, thereby preventing accumulation of N-retinylidene-N-retinylethanolamine (a toxic substance known to contribute to retinal degeneration) and photoreceptor cell death
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
the enzyme plays a role in retinoid metabolism
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
involved in retinoid homeostasis in the prostate
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
possibly involved in the first step of all-trans-retinoic acid production
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
more efficient in the reductive direction
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
?
estrone + NADH + H+
estradiol + NAD+
-
no substrate for wild-type isoforms prRDH1 and prRDH2, but substrate for mutants M146G of prRDH1 and M147G of prRDH2
-
-
?
estrone + NADH + H+
estradiol + NAD+
no substrate for wild-type, but substrate for mutant M144G
-
-
?
n-nonanal + NADPH + H+
n-nonanol + NADP+
might play a role in detoxification of lipid peroxidation products
-
-
r
n-nonanal + NADPH + H+
n-nonanol + NADP+
-
substrate of RDH11 and RDH12
-
-
?
retinal + NADPH + H+
retinol + NADP+
-
-
-
-
?
retinal + NADPH + H+
retinol + NADP+
-
-
-
-
?
retinal + NADPH + H+
retinol + NADP+
reaction of the retinoid oxidoreductive complex (ROC) composed of RDH10 (SDR16C4)and DHRS3 (EC 1.2.1.36)
-
-
ir
retinal + NADPH + H+
retinol + NADP+
reaction of the retinoid oxidoreductive complex (ROC) composed of RDH10 (SDR16C4)and DHRS3 (EC 1.2.1.36)
-
-
ir
retinol + NAD+
retinal + NADH + H+
-
-
-
-
?
retinol + NAD+
retinal + NADH + H+
reaction of RDH10 (SDR16C4)
-
-
ir
retinol + NAD+
retinal + NADH + H+
reaction of RDH10 (SDR16C4)
-
-
ir
retinol + NADP+
retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
important for the maintenance of retinoid homeostasis
-
-
r
retinol + NADP+
retinal + NADPH + H+
important for the maintenance of retinoid homeostasis, low activity of the NRDRB1 splice variant possibly contributes to a disturbed retinoid homeostasis leading to abnormal differentiation and high susceptibility to human papilloma virus in the cervical epithelium
-
-
r
retinol + NADP+
retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
additional information
?
-
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
?
additional information
?
-
-
clear specificity for pro-S hydrogen of NADPH and for pro-R-hydrogen on C15 of the retinols, no steroid dehydrogenase activity
-
-
?
additional information
?
-
clear specificity for pro-S hydrogen of NADPH and for pro-R-hydrogen on C15 of the retinols, no steroid dehydrogenase activity
-
-
?
additional information
?
-
clear specificity for pro-S hydrogen of NADPH and for pro-R-hydrogen on C15 of the retinols, no steroid dehydrogenase activity
-
-
?
additional information
?
-
-
prefers NADP+ over NAD+
-
-
?
additional information
?
-
-
although bi-directional in vitro, in living cells, RDH12 acts exclusively as a retinaldehyde reductase, shifting the retinoid homeostasis toward the increased levels of retinol and decreased levels of bioactive retinoic acid. The retinaldehyde reductase activity of RDH12 protects the cells from retinaldehyde-induced cell death
-
-
?
additional information
?
-
-
isoform RDH12 additionally cataylzes the reduction of dihydrotestosterone to androstanediol
-
-
?
additional information
?
-
no significant conversion of 17beta-, 3alpha- and 11beta-hydroxysteroids
-
-
?
additional information
?
-
-
no significant conversion of 17beta-, 3alpha- and 11beta-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
?
-
-
RDH10 is essential for retinoic acid biosynthesis during embryogenesis
-
-
?
additional information
?
-
it is unlikely that 11-cis retinal is metabolised by RDH12 in vivo, as according to the visual cycle, 11-cis retinal that enters the photoreceptors is likely to be sequestered by opsins. Binding of cellular-retinol-binding-protein, CRBP1, to all-trans retinol prevents its oxidation by RDH12
-
-
-
additional information
?
-
-
it is unlikely that 11-cis retinal is metabolised by RDH12 in vivo, as according to the visual cycle, 11-cis retinal that enters the photoreceptors is likely to be sequestered by opsins. Binding of cellular-retinol-binding-protein, CRBP1, to all-trans retinol prevents its oxidation by RDH12
-
-
-
additional information
?
-
purified RDH12 displays a about 2000fold higher affinity for NADP+ and NADPH than for NAD+ and NADH, and has a greater affinity for retinaldehydes than retinols. RDH12 functions as a retinal reductase, with highest activity towards all-trans retinal, followed by 11-cis retinal. RDH12 has also been shown to convert dihydrotestosterone (DHT) to androstanediol
-
-
-
additional information
?
-
-
purified RDH12 displays a about 2000fold higher affinity for NADP+ and NADPH than for NAD+ and NADH, and has a greater affinity for retinaldehydes than retinols. RDH12 functions as a retinal reductase, with highest activity towards all-trans retinal, followed by 11-cis retinal. RDH12 has also been shown to convert dihydrotestosterone (DHT) to androstanediol
-
-
-
additional information
?
-
RDH11 is able to reduce both all-trans- and cis-retinaldehydes into all-trans- and -cis-retinol (Vitamin A)
-
-
-
additional information
?
-
-
RDH11 is able to reduce both all-trans- and cis-retinaldehydes into all-trans- and -cis-retinol (Vitamin A)
-
-
-
additional information
?
-
-
dihydrotestosterone is not a substrate for mouse isoform RDH12
-
-
?
additional information
?
-
-
the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
-
-
?
additional information
?
-
the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
-
-
?
additional information
?
-
the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
-
-
?
additional information
?
-
-
the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
-
-
?
additional information
?
-
the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
-
-
?
additional information
?
-
the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
-
-
?
additional information
?
-
-
recombinant RRD functions with both unbound and CRBP(I) (cellular retinol-binding protein)-bound retinal
-
-
?
additional information
?
-
-
no activity with decanal
-
-
?
additional information
?
-
the rod outer segment enzyme retinol dehydrogenase RDH8 uses NADPH as a cofactor. 11-cis retinal is not a substrate of RDH8. Narrow substrate specificity of RDH8
-
-
-
additional information
?
-
-
the rod outer segment enzyme retinol dehydrogenase RDH8 uses NADPH as a cofactor. 11-cis retinal is not a substrate of RDH8. Narrow substrate specificity of RDH8
-
-
-
additional information
?
-
-
no activity with decanal
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
11-cis-retinal + NADPH + H+
11-cis-retinol + NADP+
-
-
-
r
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
possibly involved in the production of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments
-
-
r
9-cis-retinol + NADP+
9-cis-retinal + NADPH + H+
possibly involved in the first step of 9-cis-retinoic acid production
-
-
r
all-trans retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
r
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
n-nonanal + NADPH + H+
n-nonanol + NADP+
might play a role in detoxification of lipid peroxidation products
-
-
r
retinol + NAD+
retinal + NADH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
additional information
?
-
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
involved in the regeneration of bleached visual pigments in photoreceptor cells, involved in retinol metabolism outside of photoreceptor cells
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
greater catalytic efficiency in the reductive than in the oxidative direction. Localization of RDH13 at the entrance to the mitochondrial matrix suggests that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
RDH12 is dispensable in support of the visual cycle but appears to be a key component in clearance of free all-trans-retinal, thereby preventing accumulation of N-retinylidene-N-retinylethanolamine (a toxic substance known to contribute to retinal degeneration) and photoreceptor cell death
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
the enzyme plays a role in retinoid metabolism
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
involved in retinoid homeostasis in the prostate
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
possibly involved in the first step of all-trans-retinoic acid production
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
important for the maintenance of retinoid homeostasis
-
-
r
retinol + NADP+
retinal + NADPH + H+
important for the maintenance of retinoid homeostasis, low activity of the NRDRB1 splice variant possibly contributes to a disturbed retinoid homeostasis leading to abnormal differentiation and high susceptibility to human papilloma virus in the cervical epithelium
-
-
r
retinol + NADP+
retinal + NADPH + H+
-
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
retinol + NADP+
retinal + NADPH + H+
-
-
-
?
additional information
?
-
-
although bi-directional in vitro, in living cells, RDH12 acts exclusively as a retinaldehyde reductase, shifting the retinoid homeostasis toward the increased levels of retinol and decreased levels of bioactive retinoic acid. The retinaldehyde reductase activity of RDH12 protects the cells from retinaldehyde-induced cell death
-
-
?
additional information
?
-
-
RDH10 is essential for retinoic acid biosynthesis during embryogenesis
-
-
?
additional information
?
-
it is unlikely that 11-cis retinal is metabolised by RDH12 in vivo, as according to the visual cycle, 11-cis retinal that enters the photoreceptors is likely to be sequestered by opsins. Binding of cellular-retinol-binding-protein, CRBP1, to all-trans retinol prevents its oxidation by RDH12
-
-
-
additional information
?
-
-
it is unlikely that 11-cis retinal is metabolised by RDH12 in vivo, as according to the visual cycle, 11-cis retinal that enters the photoreceptors is likely to be sequestered by opsins. Binding of cellular-retinol-binding-protein, CRBP1, to all-trans retinol prevents its oxidation by RDH12
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additional information
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the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
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additional information
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the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
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additional information
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the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
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additional information
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the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
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additional information
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the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
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additional information
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the onset of RDH12 expression during the maturation of photoreceptor cells suggests a function related to the visual process. The light-induced rapid decrease of RDH12 protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression
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evolution
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RDHs that catalyze the interconversion of retinal and retinol involved in rhodopsin turnover are members of the family of short chain dehydrogenase/reductases
evolution
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all three proteins (Rdh11/12-like 1-3) include conserved signatures of the SDR family, such as cofactor binding (TGXXXGXG), the catalytic mechanism (YXXXK), and the structural integrity (NVG or NAG) patterns. Japanese eel Rdh11/12-like 1 clusters with piscine Rdh11 and Rdh12, however the cluster is formed outside that of mammalian Rdh11 and Rdh12. In contrast, Rdh11/12-like 2 and Rdh11/12-like 3 form a clade with putative European eel Rdh11s and Rdh12s outside that of mammalian and piscine Rdh11/Rdh12
evolution
enzyme RDH10 belongs to the 16C family of the short-chain dehydrogenase/reductase (SDR) superfamily. Most members of the SDR16C family (except for DHRS3) exhibit higher binding affinities for NAD(H) as cofactor, whereas members of the SDR7C family prefer NADP(H). The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzymes function in the reductive direction
evolution
enzyme RDH10 belongs to the 16C family of the short-chain dehydrogenase/reductase (SDR) superfamily. Most members of the SDR16C family (except for DHRS3) exhibit higher binding affinities for NAD(H) as cofactor, whereas members of the SDR7C family prefer NADP(H). The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzymes function in the reductive direction
evolution
human retinol dehydrogenase 11 RDH11 belongs to the short-chain dehydrogenases/ reductases (SDR) family
evolution
retinol dehydrogenase 11 (RDH11) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. A mild reduction in retinoic acid signaling is observed in RDH11-null testis
evolution
retinol dehydrogenase-10 (RDH10) is a member of the short-chain dehydrogenase/reductase family
evolution
retinol dehydrogenases (RDHs) are members of the short chain dehydrogenases/reductases (SDR) family of enzymes. The SDRs are typically 250-350 amino acids in length and have a relatively low sequence similarity of about 15-30%. Common to all SDRs is the highly conserved Rossman fold, which is composed of a central beta-sheet flanked by 3-4 alpha-helices, forming the cofactor binding site. The SDRs have two conserved domains: the cofactor binding site (GXXXGXG) and the catalytic site (YXXXK)
evolution
the enzyme belongs to the the short-chain dehydrogenase/reductase (SDR) superfamily, NAD(P)-dependent enzymes, and short-chain dehydrogenase/reductase 16C family (SDR16C)
evolution
RDH11 is co-expressed with BCO1 in several mouse tissues, and the retinaldehyde reductase activity of RDH11 is conserved in the mouse enzyme
malfunction
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generation of Rdh13 knockout mice. No obvious difference in phenotype or function between Rdh13 knockout and wild-type mice. But in Rdh13-/- mice subjected to intense light exposure, the photoreceptor outer-plus-inner-segment and outer nuclear layer are dramatically shorter, and the amplitudes of a- and b-waves under scotopic conditions are significantly attenuated. Increased expression levels of CytC, CytC-responsive apoptosis proteinase activating factor-1 and caspases 3, and other mitochondria apoptosis-related genes, e.g. nuclear factor-kappa B P65 and B-cell lymphoma 2-associated X protein, are observed in Rdh13-/- mice
malfunction
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loss-of-function mutations of RDH12 cause retinal degeneration in some forms of Leber congenital amaurosis. Outer segments of rods deficient in Rdh12 show no altered phenotype. Following exposure to light, a leak of retinoids from outer to inner segments is detected in rods from both wild-type and knock-out mice. In cells lacking Rdh8, EC 1.1.1.105, or Rdh12, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH8-deficient mutants
malfunction
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Rdh10 null mutant mouse embryos exhibit dorsal pancreas agenesis and a hypoplastic ventral pancreas with retarded tubulogenesis and branching. Rdh10 null mutant mouse embryos exhibit dorsal pancreas agenesis and a hypoplastic ventral pancreas with retarded tubulogenesis and branching
malfunction
cyclic-light-reared Rdh8-/- knockout mice show elevated levels of all-trans retinal, contributing to RPE lipofuscin formation and accumulation. Lipofuscin accumulates in the retinal pigment epithelium (RPE) of Rdh8-/- mice
malfunction
fetal mouth movement defects are correlated with cleft palate, cleft palate in retinoid deficiency results from a lack of fetal mouth movement. Mouse embryos deficient in retinoic acid (RA) have mispatterned pharyngeal nerves and skeletal elements that block spontaneous fetal mouth movement in utero. Embryos with deficient retinoid signaling are generated by stagespecific inactivation of retinol dehydrogenase 10 (Rdh10), a gene crucial for the production of RA during embryogenesis. Rdh10+ denotes the wild-type allele, Rdh10delta denotes a targeted knockout null allele with exon 2 deleted, and Rdh10flox is a floxed allele in which exon 2 is excised upon exposure to Cre recombinase thereby converting to Rdh10delta. Disruption of RA production at different embryonic stages can produce a variety of phenotypes, analysis of palate morphology in Rdh10flox/+ control and Rdh10delta/flox mutant embryos, overview
malfunction
mice lacking RDH10 either in cone photoreceptors, Müller cells, or the entire retina show normal cone photoresponses in all RDH10-deficient mouse lines. Their cone-driven dark adaptation both in vivo and in isolated retina is unaffected, indicating that RDH10 is not required for the function of the retina visual cycle. In transgenic mice overexpressing RDH10 ectopically in rod cells, rod dark adaptation is unaffected and transgenic rods are unable to use cis-retinol for pigment regeneration
malfunction
microsomes isolated from the testes and livers of Rdh11-/- mice fed a regular diet exhibit a 3 and 1.7fold lower rate of all-trans-retinaldehyde conversion to all-trans-retinol, respectively, than the microsomes of wild-type littermates. Testes and livers of Rdh11-/- mice fed a vitamin A-deficient diet have about 35% lower levels of all-trans-retinol than those of wild-type mice. Oxidative NAD+-dependent retinol dehydrogenase activity is not affected by inactivation of the rdh11 gene, while similarly to testis microsomes, liver microsomes lacking RDH11 show a lower rate (1.7fold) of retinaldehyde reduction. In lungs and intestines, the microsomal retinaldehyde reductase activities are comparable between RDH11-null mice and their wild-type littermates
malfunction
mutagenesis and targeted gene knockout studies in mice confirm that a functional RDH10 is critical for survival until embryonic day 11.5 (E11.5), as Rdh10-/- embryos can be rescued by maternal supplementation of retinaldehyde from E7.5 to E11.5. Genetic disruption of murine Rdh10 gene results in a marked reduction in retinoic acid (RA) synthesis that leads to numerous developmental abnormalities. RDH10-deficient embryos display defects in axial extension and embryonic turning, abnormal hindbrain and craniofacial patterning, agenesis of posterior pharyngeal arches, perturbed somitogenesis, hypoplastic forelimb buds, and abnormal organogenesis of multiple systems, including heart and vasculature, lungs, and gastrointestinal tract. Embryos carrying a targeted knockout of Rdh10 died by E12.5, while embryos carrying various mutant alleles survived until E13.5-E15.5, or until late gestation. Testicular cell-specific conditional knockout of Rdh10 shows that deficiency of RDH10 in both Sertoli and germ cells completely impairs testicular RA signaling in juvenile animals. Spermatogenesis progressively recovers in adult Rdh10 conditional knockout mice, suggesting that RDH10 is not essential for adult spermatogenesis. In mice, targeted knockout of Dhrs3 results in an about 30% increase in RA levels, reduction in the levels of retinol and retinyl esters, and embryonic lethality late in gestation
malfunction
mutations in RDH12 are primarily associated with Leber congenital amaurosis (LCA) type 13, an early onset retinal dystrophy, presenting in early childhood and accounting for approximately 10% of all LCA cases, clinical phenotypes of autosomal recessive RDH12 LCA, overview. One case of a heterozygous variant has also been implicated in autosomal dominant retinitis pigmentosa (RP)
malfunction
mutations in the gene encoding retinol dehydrogenase 10 (Rdh10) lead to craniofacial, limb, and organ abnormalities. This phenotype, called RDH10trex, is caused by the severely reduced ability of mutant RDH10 to oxidize retinol to retinaldehyde, resulting in insufficient RA signaling
malfunction
mutations in the retinol dehydrogenase 12 (RDH12) gene are primarily associated with Leber congenital amaurosis (LCA) type 13, a severe early onset autosomal recessive retinal dystrophy. This is a progressive disorder with significant decline from 10 years of age, which leads to complete blindness in adulthood. RDH12-LCA is characterized by macular atrophy, which extends peripherally in a variegated pattern corresponding to the retinal vasculature, and midperipheral pigmentary retinopathy. A heterozygous deletion (F254Lfs*24 ) in retinol dehydrogenase 12 (RDH12) causes familial autosomal dominant retinitis pigmentosa. Mutation E260R, a single base pair deletion resulting in a frameshift and premature termination, causes a milder late onset (average age of diagnosis is 28.5 years) retinitis pigmentosa (RP) phenotype, with intraretinal bone spicule pigmentation and attenuation of retinal arterioles. Phenotypes, overview
malfunction
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Rdh8-/- Rdh12-/- double knockout mice show that Rdh8 accounts for 70% of all-trans RDH activity. Rdh12-/- mice display normal retinal morphology at 6 weeks of age. There is no significant difference in rhodopsin levels, indicating efficient regeneration of the chromophore. No difference in all-trans RDH activity in dissected retinae or isolated rod outer segments (ROS) between wild-type and Rdh12-/- mice is observed, suggesting that other enzymes may be compensating for the loss of Rdh12 activity. Knockout mice do show a delayed dark adaptation and accumulation of all-trans retinal after bleaching, indicating an important role of RDH12 under conditions of excess illumination. Retinal homogenates show decreased all-trans retinal reduction, and increased A2E levels. Rdh8-/- Rdh12-/- double knockouts also show mild light-dependent retinal degeneration, with delayed dark adaptation and reduced all-trans RDH activity with a build-up of all-trans retinal, a subsequent accumulation of toxic A2E is observed. Double knockout mice regenerate the visual pigment in vivo and triple knockout Rdh8-/- Rdh12-/- Rdh5-/- mice also have the ability to regenerate 11-cis retinal
malfunction
shRNA-mediated RDH10 knockdown induces glioma cell cycle arrest, impairs glioma cell proliferation in vitro, and promotes glioma apoptosis. RDH10 knockdown significantly represses several key cancer pathways including TWEAK, TNFR1 and P53. RDH10 knockdown inhibits glioma cell growth by down-regulating the TWEAK-NF-kappaB axis
malfunction
the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners. Similarly, active site mutants, RDH10 Y210A-HA and DHRS3 Y188A-FLAG, retain the capacity to form complexes with wild-type protein partners. Thus, catalytically active proteins are not necessary for complex formation
malfunction
isolated retinas from Rgr+/+ and Rgr-/- mice are exposed to continuous light, and cone photoresponses are recorded. Cones in Rgr-/- retinas lose sensitivity at a faster rate than cones in Rgr+/+ retinas
malfunction
isolated retinas from Rgr+/+ and Rgr-/- mice are exposed to continuous light, and cone photoresponses are recorded. Cones in Rgr-/- retinas lose sensitivity at a faster rate than cones in Rgr+/+ retinas
malfunction
isolated retinas from Rgr+/+ and Rgr-/- mice are exposed to continuous light, and cone photoresponses are recorded. Cones in Rgr-/- retinas lose sensitivity at a significantly faster rate than cones in Rgr+/+ retinas. A similar effect is seen in Rgr+/+ retinas following treatment with alpha-aminoadipic acid. These results indicate that maintenance and recovery of cone sensitivity in isolated mouse retinas requires a light-driven visual cycle that depends on RGR opsin. Thus, ciliary photoreceptors of vertebrates, like the rhabdomeric photoreceptors of invertebrates, can use light itself to regenerate visual pigment
malfunction
microsomes isolated from the testes and livers of Rdh11-/- mice fed a regular diet exhibited a 3 and 1.7fold lower rate of all-trans-retinaldehyde conversion to all-trans-retinol, respectively, than the microsomes of wild-type littermates. Testes and livers of Rdh11-/- mice fed a vitamin A-deficient diet have about 35% lower levels of all-trans-retinol than those of wild-type mice the conversion of beta-carotene to retinol via retinaldehyde as an intermediate appeared to be impaired in the testes of Rdh11-/-/retinol-binding protein 4-/- (Rbp4-/-) mice, which lack circulating holo RBP4 and rely on dietary supplementation with beta-carotene for maintenance of their retinoid stores. Overnight starvation results in a decrease in the amount of RDH11 in livers of fasted mice. Gene expression pattern indicates a mild reduction in retinoic acid signaling in RDH11-null testis. The oxidative NAD+-dependent retinol dehydrogenase activity is not affected by inactivation of the Rdh11 gene. The conversion of retinaldehyde to retinol in whole mouse embryonic fibroblasts (MEFs) lacking RDH11 occurs at a slower rate than in wild-type MEFs
malfunction
RDH10 is not required for the function of the retina visual cycle. Transgenic mice expressing RDH10 ectopically in rod cells show, that rod dark adaptation is unaffected by the expression of RDH10 and transgenic rods are unable to use cis-retinol for pigment regeneration. Lack of phenotype of mice lacking RDH10 in the entire retina
malfunction
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loss-of-function mutations of RDH12 cause retinal degeneration in some forms of Leber congenital amaurosis. Outer segments of rods deficient in Rdh12 show no altered phenotype. Following exposure to light, a leak of retinoids from outer to inner segments is detected in rods from both wild-type and knock-out mice. In cells lacking Rdh8, EC 1.1.1.105, or Rdh12, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH8-deficient mutants
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malfunction
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generation of Rdh13 knockout mice. No obvious difference in phenotype or function between Rdh13 knockout and wild-type mice. But in Rdh13-/- mice subjected to intense light exposure, the photoreceptor outer-plus-inner-segment and outer nuclear layer are dramatically shorter, and the amplitudes of a- and b-waves under scotopic conditions are significantly attenuated. Increased expression levels of CytC, CytC-responsive apoptosis proteinase activating factor-1 and caspases 3, and other mitochondria apoptosis-related genes, e.g. nuclear factor-kappa B P65 and B-cell lymphoma 2-associated X protein, are observed in Rdh13-/- mice
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metabolism
interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implying a role of selenoprotein F in vitamin A metabolism. Selenoprotein F has been reported to play important roles in oxidative stress, endoplasmic reticulum (ER) stress, and carcinogenesis. Both of selenoprotein F and RDH11 might reduce all-trans-retinaldehyde into all-trans-retinol, but overexpressed selenoprotein F and RDH11 inhibit the enzyme activity of each other
metabolism
the enzyme is involved in retinoic acid biosynthesis, overview. Retinoic acid (RA)-mediated transcriptional feedback loops upregulate the expression of the reductive enzyme DHRS3 and downregulate the expression of the oxidative enzyme RDHE2 in response to an increase in retinoic acid levels. Members of two families of SDRs are involved in the regulation of RA homeostasis, SDR16C and SDR7C. Regulation of the flux from retinol to retinaldehyde
metabolism
the enzyme is involved in retinoic acid biosynthesis, overview. Retinoic acid (RA)-mediated transcriptional feedback loops upregulate the expression of the reductive enzyme DHRS3 and downregulate the expression of the oxidative enzyme RDHE2 in response to an increase in retinoic acid levels. Members of two families of SDRs are involved in the regulation of RA homeostasis, SDR16C and SDR7C. Regulation of the flux from retinol to retinaldehyde
metabolism
the oxidation of all-trans-retinol to all-trans-retinal represents the first and rate-limiting step of the all-trans-retinoic acid (RA) synthesis pathway and it is the target of mechanisms that fine-tune RA levels within the cell. RDH10 is one enzyme responsible for the oxidation of all-trans-retinol to all-trans-retinaldehyde, and together with the all-trans-retinaldehyde reductase DHRS3 forms an oligomeric protein complex. The resulting retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. DHRS3 is a critical regulator of RA synthesis. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits
metabolism
the oxidation of all-trans-retinol to all-trans-retinal represents the first and rate-limiting step of the all-trans-retinoic acid (RA) synthesis pathway and it is the target of mechanisms that fine-tune RA levels within the cell. RDH10 is one enzyme responsible for the oxidation of all-trans-retinol to all-trans-retinaldehyde, and together with the all-trans-retinaldehyde reductase DHRS3 forms an oligomeric protein complex. The resulting retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits
metabolism
retinaldehyde can be produced in the cells by the oxidation of retinol or by the cleavage of beta-carotene at its central double bond (15,15') catalyzed by cytosolic BCO1. In rodents, cleavage of beta-carotene to retinaldehyde with subsequent conversion of retinaldehyde to retinol occurs mainly in the small intestine. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet
physiological function
Rdh11 is able to efficiently detoxify 4-hydroxynonenal in cells. Rdh11 protects against 4-hydroxynonenal modification of proteins and 4-hydroxynonenal-induced apoptosis in HEK-293 cells
physiological function
Rdh12 is able to efficiently detoxify 4-hydroxynonenal in cells, most probably through its ability to reduce it to a nontoxic alcohol. Cells expressing Rdh12 show significantly less formation of Michael adducts with lysine, histidine, or cysteine residues of proteins thereby inhibiting their physiological functions. Microsomes from retinas of Rdh12 knockout mice form significantly more Michael adducts with microsomal proteins in the presence of 4-hydroxynonenal than wild-type. RDH12 also protects against light-induced apoptosis of photoreceptors
physiological function
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RDH12 activity in the photoreceptor inner segments is also key enzyme function. RDH12 in inner segments can protect vital cell organelles against aldehyde toxicity caused by an intracellular leak of all-trans-retinal, as well as other aldehydes originating both inside and outside the cell
physiological function
DHRS3 activity requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. The retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other
physiological function
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Six h after re-feeding, isoform Rdh10 expression is decreased 4563% in liver, pancreas, and kidney, relative to mice fasted 16 h. All-trans-retinoic acid in the liver is decreased 44% 3 h after reduced Rdh expression. Oral gavage with glucose or injection with insulin decreases Rdh10 mRNA 50% or greater in mouse liver
physiological function
the retinol dehydrogenase activity of RDH10 is activated by retinaldehyde reductase DHRS3. In turn, DHRS3 requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other
physiological function
the retinol dehydrogenase activity of RDH10 is reciprocally activated by retinaldehyde reductase DHRS3. At E13.5, DHRS3-null embryos have 4fold lower levels of retinol and retinyl esters, but only slightly elevated levels of retinoic acid. The membrane-associated retinaldehyde reductase and retinol dehydrogenase activities are decreased by 4- and 2fold, respectively, in Dhrs3-/- embryos, and Dhrs3-/- mouse embryonic fibroblasts exhibit reduced metabolism of both retinaldehyde andretinol. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other
physiological function
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the enzyme accelerates erythroid cell proliferation by upregulating the STAT5 signaling pathway
physiological function
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the enzyme affects dorsal pancreas development and participates in the terminal differentiation of endocrine cells
physiological function
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all-trans retinal in mouse photoreceptors is reduced predominantly by Rdh8 and Rdh12. Rdh8 and Rdh12 were responsible for over 98% of all-trans RDH activity, withRdh8 accounts for 70% of all-trans RDH activity. The majority of all-trans retinal is reduced by Rdh8 in the outer segments, but some all-trans retinal can leak into the inner segments, where it is reduced by Rdh12. The role of RDH12 in the visual cycle is minimal, but possibly plays a protective role in the clearance of alltrans retinal in periods of intense illumination. Another possible role of RDH12 is protection against toxic lipid peroxidation products, like nonanal and 4-HNE, produced from the oxidative attack of polyunsaturated fatty acids in lipid membranes. A buildup of either all-trans retinal or lipid peroxidation products is damaging to photoreceptors. All-trans retinal accumulation leads to the production of toxic N-retinylidene-N-retinylethanolamine (A2E), and lipid peroxidation products are inherently toxic. RDH12 appears to have two possible roles. RDHs do not appear to be necessary for the regeneration of the visual pigment in mice, but are needed for clearance of all-trans retinal in periods of excess illumination. It is possible that murine RDHs compensate for each other
physiological function
bis-retinoids are a major component of lipofuscin that accumulates in the retinal pigment epithelium (RPE) in aging and age-related macular degeneration (AMD). Bis-retinoids are known to originate from retinaldehydes required for the light response of photoreceptor cells, relative contributions of the chromophore, 11-cis retinal, and photoisomerization product, all-trans retinal, are analyzed, overview. In photoreceptor outer segments, all-trans retinal, but not 11-cis retinal, is reduced by retinol dehydrogenase 8 (RDH8). The reductase activity of RDH8 keeps in check the generation of bis-retinoids from all-trans retinal released by photoactivated rhodopsin. There is no significant increase in lipofuscin precursor fluorescence in wild-type mouse rods following light
physiological function
enzyme retinol dehydrogenase 10 (Rdh10) is crucial for the production of retinoic acid (RA) during embryogenesis, its function is necessary for spontaneous fetal mouth movement that facilitates palate shelf elevation. Proper retinoid signaling and pharyngeal patterning are crucial for the fetal mouth movement needed for palate formation. Vitamin A metabolism and RA production are essential for viability in the early organogenesis stages of development
physiological function
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Japanese eel retinol dehydrogenases 11/12-like 1-3 (Rdh11/12-like 1-3) are 17-oxosteroid reductases (EC 1.1.1.51) involved in sex steroid synthesis. Catalysis of the conversion of A4 to T and E1 to E2 is performed by recombinant Rdh11/12-like 1
physiological function
pigment regeneration is critical for the function of cone photoreceptors in bright and rapidly-changing light conditions. This process is facilitated by the recently-characterized retina visual cycle, in which Müller cells recycle spent all-trans-retinol visual chromophore back to 11-cis-retinol. This 11-cis-retinol is oxidized selectively in cones to the 11-cis-retinal used for pigment regeneration. Retinol dehydrogenase 10 (RDH10) is responsible for the oxidation of 11-cis-retinol in the cone visual cycle, but RDH10 is not the dominant retina 11-cis-RDH, overview. Cone RDH10 is not required for normal cone dark adaptation
physiological function
RDH11 is an enzyme for the reduction of all-trans-retinaldehyde to all-trans-retinol (vitamin A). It is involved in the retinal pigment epithelium (RPE) during the retinoid visual cycle. Interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) is analyzed by yeast two-hybrid system and determination of production of retinol. The production of retinol is decreased by SELENOF overexpression, resulting in more retinaldehyde
physiological function
retinol dehydrogenase 11 (RDH11) is a microsomal short-chain dehydrogenase/reductase that recognizes all-trans- and cis-retinoids as substrates and prefers NADPH as a cofactor. RDH11 contributes to the oxidation of 11-cis-retinol to 11-cis-retinaldehyde during the visual cycle in the eye's retinal pigment epithelium. The intestinal microsomes produce two products within the short 15-min incubations with retinaldehyde: retinol and retinyl esters. This suggests that, in the intestinal microsomes, the retinaldehyde reductase activity is coordinated with the retinol esterifying activity, possibly to ensure a highly efficient processing of retinaldehyde into retinyl esters for packaging into chylomicrons. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet, and RDH11 is essential for the maintenance of retinol levels in liver and testis of mice during dietary vitamin A deficiency
physiological function
retinol dehydrogenase 12 (RDH12) is an NADPH-dependent retinal reductase that functions as part of the visual cycle, involving a series of enzymatic reactions that regenerates the visual pigment, 11-cis retinal, overview of the visual cycle and the role of RDH12. A number of RDHs are involved in the visual cycle, and vary in substrate and coenzyme specificity. RDH12 functions as a retinal reductase, with highest activity towards all-trans retinal, followed by 11-cis retinal. Enzyme RDH12 has also been shown to convert dihydrotestosterone (DHT) to androstanediol, suggesting a possible involvement in steroid metabolism. RDH12 can also act on medium chain aldehydes, produced from lipid peroxidation of unsaturated fatty acids metabolising the lipid derived medium chain aldehyde nonanal, and inhibiting the reduction of all-trans retinal in RDH12 transfected HEK-293 cells, indicating that RDH12 can protect cells from nonanal induced toxity, but RDH12 does not protect cells against 4-hydroxynonenal (4-HNE), the most abundant lipid peroxidation product, although HEK-293 cells stably transfected with RDH12 do protect from 4-HNE-induced cell death
physiological function
retinol dehydrogenase-10 (RDH10) plays an important role in retinoic acid (RA) synthesis, and it promotes development and progression of human glioma via the TWEAK-NF-kappaB axis. RDH10 is highly expressed in human gliomas, and its expression correlates with tumor grade and patient survival times, RDH10 expression is associated with development and progression of human glioma. RDH10 is overexpressed in human gliomas and predicts a high grade and poor prognosis. RDH10 regulates the cell cycle progression, as its loss causes an S and G2/M phase arrest, RDH10 regulates expression of glioma genes, it affects expression of genes involved in cancer, apoptosis, growth and proliferation, motility, and cell cycle
physiological function
the enzyme is involved in retinoic acid biosynthesis, overview. The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzyme function in the reductive direction. RDH10 acts as a high-affinity retinol dehydrogenase with a preference for NAD+ as cofactor. DHRS3 acts as an NADP(H)-dependent retinaldehyde reductase
physiological function
the enzyme is involved in retinoic acid biosynthesis, overview. The NAD(H)-dependent oxidoreductases usually function in the oxidative direction in intact cells, whereas the NADP(H)-dependent enzymes function in the reductive direction. RDH10 acts as a high-affinity retinol dehydrogenase with a preference for NAD+ as cofactor
physiological function
the retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits. Catalytically active enzymes are not necessary for complex formation. As the rate-limiting step of RA synthesis, the conversion of all-trans-retinol to all-trans-retinaldehyde is a target of mechanisms that regulate RA synthesis. ROC, consisting of the retinol dehydrogenase RDH10 and the retinaldehyde reductase DHRS3, is a critical component of RA synthesis regulation
physiological function
the retinoid oxidoreductase complex (ROC) is bifunctional and has the capacity to regulate steady-state levels of the direct precursor of RA, all-trans-retinaldehyde. By coupling retinol dehydrogenase and retinaldehyde reductase activities, an elegant system is formed that can fine-tune steady-state levels of all-trans-retinaldehyde, and consequently RA, concentrations within the cell. Formation of ROC influences the catalytic properties of both RDH10 and DHRS3 subunits. DHRS3 is a critical regulator of RA synthesis. Catalytically active enzymes are not necessary for complex formation. As the rate-limiting step of RA synthesis, the conversion of all-trans-retinol to all-trans-retinaldehyde is a target of mechanisms that regulate RA synthesis. ROC, consisting of the retinol dehydrogenase RDH10 and the retinaldehyde reductase DHRS3, is a critical component of RA synthesis regulation
physiological function
cone-specific 11-cis-RDH is likely to be important in regulating access to the retina visual cycle. Retinol dehydrogenase 10, RDH10 (UniProt ID Q8VCH7), is not the dominant retina 11-cis-RDH. Cone RDH10 is not required for the normal function of dark-adapted cones and for normal cone dark adaptation, as well as for the retina visual cycle
physiological function
RDH11 contributes to the oxidation of 11-cis-retinol to 11-cis-retinaldehyde during the visual cycle in the eye's retinal pigment epithelium. In mouse testis and liver, RDH11 functions as an all-trans-retinaldehyde reductase essential for the maintenance of physiological levels of all-trans-retinol under reduced vitamin A availability. RDH11 is essential for the maintenance of retinol levels in testis of mice on beta-carotene diet
physiological function
the retinal RPE G-protein-coupled receptor, RGR opsin, and retinol dehydrogenase-10 (Rdh10) convert all-trans-retinol to 11-cis-retinol during exposure to visible light. RGR opsin is a non-visual opsin in intracellular membranes of RPE and Müller cells. The interaction between RGR and Rdh10 is specific. RGR opsin is a critical component of the Müller-cell visual cycle, and that regeneration of cone visual pigment can be driven by light, role of RGR opsin in the regeneration of cone visual pigment. Cones are responsible for vision in bright light and operate at high rates of opsin photoisomerization. Recovery of cone sensitivity is shown to be limited by chromophore supply. Only 11-cis-retinal (11cRAL) can regenerate bleached opsin. Coupled photoisomerization and oxidoreduction of vitamin A by RGR opsin and Rdh10, overview
physiological function
the retinal RPE G-protein-coupled receptor, RGR opsin, and retinol dehydrogenase-10 (Rdh10) convert all-trans-retinol to 11-cis-retinol during exposure to visible light. RGR opsin is a non-visual opsin in intracellular membranes of RPE and Müller cells. The interaction between RGR and Rdh10 is specific. RGR opsin is a critical component of the Müller-cell visual cycle, and that regeneration of cone visual pigment can be driven by light, role of RGR opsin in the regeneration of cone visual pigment. Cones are responsible for vision in bright light and operate at high rates of opsin photoisomerization. Recovery of cone sensitivity is shown to be limited by chromophore supply. Only 11-cis-retinal (11cRAL) can regenerate bleached opsin. Coupled photoisomerization and oxidoreduction of vitamin A by RGR opsin and Rdh10, overview
physiological function
the retinal RPE G-protein-coupled receptor, RGR opsin, and retinol dehydrogenase-10 (Rdh10) convert all-trans-retinol to 11-cis-retinol during exposure to visible light. RGR opsin is a non-visual opsin in intracellular membranes of RPE and Müller cells. The interaction between RGR and Rdh10 is specific. RGR opsin is a critical component of the Müller-cell visual cycle, and that regeneration of cone visual pigment can be driven by light, role of RGR opsin in the regeneration of cone visual pigment. Cones are responsible for vision in bright light and operate at high rates of opsin photoisomerization. Recovery of cone sensitivity is shown to be limited by chromophore supply. Only 11-cis-retinal (11cRAL) can regenerate bleached opsin. Coupled photoisomerization and oxidoreduction of vitamin A by RGR opsin and Rdh10, overview
physiological function
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RDH12 activity in the photoreceptor inner segments is also key enzyme function. RDH12 in inner segments can protect vital cell organelles against aldehyde toxicity caused by an intracellular leak of all-trans-retinal, as well as other aldehydes originating both inside and outside the cell
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additional information
in RDH12, the cofactor binding site is located at positions 46-52 and the catalytic site at positions 200-204
additional information
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in RDH12, the cofactor binding site is located at positions 46-52 and the catalytic site at positions 200-204
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C300A
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the mutant shows no oxidation activity
C300S
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the mutant shows reduced catalytic efficiency for the oxidation and reduction of all-trans-retinal compared to the wild-type enzyme
E194S
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the mutant shows 15fold higher catalytic efficiency for the reduction of all-trans-retinal than the wild-type enzyme
E266A
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the mutant shows no oxidation activity
E457V
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the mutant shows 7.5fold higher catalytic efficiency for the reduction of all-trans-retinal than the wild-type enzyme
M146G
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mutation in isoform prRDH1, gain-of-function mutant, enables estrone to bind and be reduced as an additional substrate
M147G
-
mutation in isoform prRDH2, gain-of-function mutant, enables estrone to bind and be reduced as an additional substrate
A269Gfs*2
naturally occuring mutation, the mutant enzyme shows highly reduced activity
C201R
naturally occuring mutation in the active site, inactive mutant
E260R
naturally occuring mutation, a single base pair deletion resulting in a frameshift and premature termination, mutants display a milder late onset (average age of diagnosis is 28.5 years) retinitis pigmentosa (RP) phenotype, with intraretinal bone spicule pigmentation and attenuation of retinal arterioles, phenotypes, overview
E260Rfs*18
naturally occuring mutation, autosomal dominant RDH12 variant, the heterozygous single base pair deletion c.776delG results in a frameshift and premature termination at codon 277, in 19 affected members of a large 6 generation family
F254Lfs*24
naturally occuring mutation c.759del, the mutation results in a frameshift and premature termination identified in two unrelated individuals with familial autosomal dominant retinitis pigmentosa (RP), phenotypes, overview
G43A/G47A/G49A
site-directed mutagenesis, the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners
G49A/G51A
site-directed mutagenesis, the cofactor binding mutants, RDH10 G43A/G47A/G49A-HA and DHRS3 G49A/G51A-FLAG, retain the capacity to form complexes with wild-type protein partners
L99I
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site-directed mutagenesis, about 30% of wild-type activity
M144G
gain-of-function mutant, enables estrone to bind and be reduced as an additional substrate
Q189X
-
mutation found in an individual affected by autosomal recessive childhood-onset severe retinal dystrophy
R25G/K26I
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The mutation allows the enzyme to flip its orientation in the membrane. The mutant is glycosylated in intact cells.
R62X
-
mutation found in an individual affected by autosomal recessive childhood-onset severe retinal dystrophy
S175P
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site-directed mutagenesis, no catalytic activity. Protein is stable and abundantly expressed
T49M
inactive. Mutation is associated with Lebr congenital amaurosis. Mutant is not able to detoxify 4-hydroxynonenal in cells
I51N
-
site-directed mutagenesis, significant activity in vitro. Dramatically reduced affinity for NADPH results in loss of function within cells
I51N
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site-directed mutagenesis, the catalytically active I51N variant of RDH12 undergoes accelerated degradation through the ubiquitin-proteosome system, which results in reduced level of the protein in the cell. The RDH12 mutant has lost its retinaldehyde reductase activity. Inhibitors of proteosome activity, e.g. MG132, or dimethyl sulfoxide can partially restore the activity
I51N
naturally occuring mutation, when transiently transfected in HEK-293 cells, the mutant degrades at a faster rate than the wild-type protein with significantly lower half-lif, the mutant loses its ability to protect against 4-HNE induced apoptosis
T49M
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mutation found in an individual affected by autosomal recessive childhood-onset severe retinal dystrophy
T49M
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site-directed mutagenesis, significant activity in vitro. Dramatically reduced affinity for NADPH results in loss of function within cells
T49M
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site-directed mutagenesis, the catalytically active T49M variant of RDH12 undergoes accelerated degradation through the ubiquitin-proteosome system, which results in reduced level of the protein in the cell.The RDH12 mutant has lost its retinaldehyde reductase activity. Inhibitors of proteosome activity, e.g. MG132, or dimethyl sulfoxide can partially restore the activity
T49M
naturally occuring mutation, the mutant enzyme shows highly reduced activity, when transiently transfected in HEK-293 cells, the mutant degrades at a faster rate than the wild-type protein with significantly lower half-life, the mutant loses its ability to protect against 4-HNE induced apoptosis
Y226C
-
mutation present in all individuals affected by autosomal recessive childhood-onset severe retinal dystrophy from three Austrian kindreds, enzyme expressed in COS-7 cells shows diminished activity
Y226C
naturally occuring mutation, autosomal recessive biallelic mutation causing severe retinal dystrophy
additional information
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transfection with retinol dehydrogenase 12 protects cells against nonanal-induced toxicity but is ineffective against 4-hydroxynonenal
additional information
according to the human gene mutation database (HGMD, April 2019), 80 RDH12 mutations have been reported, 51 of which are missense and 12 are nonsense mutations, the mutations span the entire gene, including the conserved regions, with no specific hotspots. In COS-7 cells transiently transfected with various RDH12 missense mutants, 11 out of 14 variants show significantly reduced enzyme activity, 5-18% of wild-type levels. They also show decreased expression levels, most likely as a result of protein instability
additional information
-
according to the human gene mutation database (HGMD, April 2019), 80 RDH12 mutations have been reported, 51 of which are missense and 12 are nonsense mutations, the mutations span the entire gene, including the conserved regions, with no specific hotspots. In COS-7 cells transiently transfected with various RDH12 missense mutants, 11 out of 14 variants show significantly reduced enzyme activity, 5-18% of wild-type levels. They also show decreased expression levels, most likely as a result of protein instability
additional information
lentiviral-mediated shRNA efficiently inhibits RDH10 expression. RDH10 knockdown impairs glioma cell proliferation in vitro
additional information
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lentiviral-mediated shRNA efficiently inhibits RDH10 expression. RDH10 knockdown impairs glioma cell proliferation in vitro
additional information
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generation of Rdh13 knockout mice. No obvious difference in phenotype or function between Rdh13 knockout and wild-type mice. But in Rdh13-/- mice subjected to intense light exposure, the photoreceptor outer-plus-inner-segment and outer nuclear layer are dramatically shorter, and the amplitudes of a- and b-waves under scotopic conditions are significantly attenuated. Increased expression levels of CytC, CytC-responsive apoptosis proteinase activating factor-1 and caspases 3, and other mitochondria apoptosis-related genes, e.g. nuclear factor-kappa B P65 and B-cell lymphoma 2-associated X protein, are observed in Rdh13-/- mice
additional information
generation of embryonic stage-specific inactivation of retinol dehydrogenase 10 (Rdh10). Stage-specific inactivation of retinol metabolism in Rdh10delta/flox mutant embryos serves as a model for vitamin A/retinoid-deficient cleft palate. Conditional inactivation of Rdh10 causes cleft palate. Nuclear fluorescence imaging of Rdh10flox + control and Rdh10delta/flox mutant embryos at E16.5 reveals complete cleft of the secondary palate in 36% of mutant embryos. For insight into the tissue architecture in cleft palates of Rdh10delta/flox mutant embryos, hematoxylin and eosin staining of paraffin sections is performed. At E13.5, the palate shelf morphology of Rdh10delta/flox mutant embryos resembled that of Rdh10flox/+ control littermates, with palate shelves aligned vertically on either side of the tongue. Using the ubiquitously expressed Cre-ERT2, the genotype of embryos with a floxed allele changes following administration of tamoxifen. Embryos with a pre-tamoxifen genotype of Rdh10flox/+ become Rdh10delta/+ post-tamoxifen. Embryos with a pretamoxifen genotype of Rdh10delta/flox or Rdh10flox/flox become Rdh10delta/delta post-tamoxifen treatment. Cleft palate was not observed in any Rdh10flox/+ control embryos. Rdh10delta/flox mutants have abnormally positioned tongues that obstruct palate shelf elevation, mutant morphologies, overview. No defect in the intrinsic tongue muscles is detected in mutant embryos relative to control littermates. The morphogenesis of tongue musculature is grossly normal in retinoid-deficient embryos, suggesting the abnormal tongue shape does not result from aberrant muscle morphogenesis. Spontaneous fetal mouth movement in utero is restricted in Rdh10delta/flox mutant embryos. Rdh10delta/flox mutant embryos have defects in motor nerves of the posterior pharyngeal arches. Retinoid-deficient embryos develop defects in the pharyngeal skeleton. Retinoid-deficient embryos develop defects in the pharyngeal skeleton
additional information
generation of enzyme Rdh8-/- knockout mice. Cyclic-light-reared Rdh8-/- mice accumulates A2E and RPE lipofuscin approximately 1.5times and approximately 2times faster, respectively, than dark-reared mice. Moving Rdh8-/- mice from cyclic-light to darkness results in bis-retinoid A2E levels less than expected to have accumulated before the move. A2E levels are significantly higher in cyclic-light compared to dark-reared animals at 2, 3, and 6 months of age. In Rdh8-/- mice, the potential contribution of elevated all-trans-retinal to bis-retinoid formation can be maximized
additional information
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generation of enzyme Rdh8-/- knockout mice. Cyclic-light-reared Rdh8-/- mice accumulates A2E and RPE lipofuscin approximately 1.5times and approximately 2times faster, respectively, than dark-reared mice. Moving Rdh8-/- mice from cyclic-light to darkness results in bis-retinoid A2E levels less than expected to have accumulated before the move. A2E levels are significantly higher in cyclic-light compared to dark-reared animals at 2, 3, and 6 months of age. In Rdh8-/- mice, the potential contribution of elevated all-trans-retinal to bis-retinoid formation can be maximized
additional information
generation of RDH11 knockout (KO) mice, phenotypes, overview
additional information
-
generation of Rdh8-/- Rdh12-/- double knockout mice. The Rdh12-/- mouse model is generated by replacement of exons 1-3 of the Rdh12 gene with a neomycin cassette. Rdh12-/- mice display normal retinal morphology at 6 weeks of age. There is no significant difference in rhodopsin levels, indicating efficient regeneration of the chromophore. No difference in all-trans RDH activity in dissected retinae or isolated rod outer segments (ROS) between wild-type and Rdh12-/- mice is observed
additional information
RDH10 enzyme knockout and overexpression in retina cell. Rdh10 mRNA levels are substantially reduced in retinas obtained from Pdgfra-Cre Rdh10flox/flox mice through a knockout in Müller cells. Similarly, the expression of Rdh10 is also dramatically reduced in Six3-Cre Rdh10flox/flox retinas, demonstrating its suppression in the entire retina. In contrast, Rdh10 mRNA levels are notably increased in transgenic Rdh10+ mice. The deletion of RDH10 in cones does not affect the overall number of cone cells or their function, and cone dark adaptation in vivo is unaffected by cone-specific deletion of RDH10
additional information
generation and analysis of RGR knockout mouse microsomes
additional information
generation of enzyme knockout Rdh11-/- mice
additional information
generation of mice lacking RDH10 either in cone photoreceptors, Müller cells, or the entire retina. In vivo electroretinography and transretinal recordings reveal normal cone photoresponses in all RDH10-deficient mouse lines. Notably, their cone-driven dark adaptation both in vivo and in isolated retina is unaffected, indicating that RDH10 is not required for the function of the retina visual cycle. Generation of transgenic mice expressing RDH10 ectopically in rod cells. Rod dark adaptation is unaffected by the expression of RDH10 and transgenic rods are unable to use cis-retinol for pigment regeneration. Lack of phenotype of mice lacking RDH10 in the entire retina
additional information
-
generation of Rdh13 knockout mice. No obvious difference in phenotype or function between Rdh13 knockout and wild-type mice. But in Rdh13-/- mice subjected to intense light exposure, the photoreceptor outer-plus-inner-segment and outer nuclear layer are dramatically shorter, and the amplitudes of a- and b-waves under scotopic conditions are significantly attenuated. Increased expression levels of CytC, CytC-responsive apoptosis proteinase activating factor-1 and caspases 3, and other mitochondria apoptosis-related genes, e.g. nuclear factor-kappa B P65 and B-cell lymphoma 2-associated X protein, are observed in Rdh13-/- mice
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Haeseleer, F.; Huang, J.; Lebiodas, L.; Saari, J.C.; Palczewski, K.
Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal
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1998
Homo sapiens (O75911)
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Belyaeva, O.V.; Stetsenko, A.V.; Nelson, P.; Kedishvili, N.Y.
Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines
Biochemistry
42
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2003
Homo sapiens
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Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1)
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277
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Homo sapiens, Homo sapiens (Q8TC12)
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Haeseleer, F.; Jang, G.F.; Imanishi, Y.; Driessen, C.A.; Matsumura, M.; Nelson, P.S.; Palczewski, K.
Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina
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Homo sapiens, Homo sapiens (Q96NR8), Homo sapiens (Q9HBH5)
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Markova, N.G.; Pinkas-Sarafova, A.; Karaman-Jurukovska, N.; Jurukovski, V.; Simon, M.
Expression pattern and biochemical characteristics of a major epidermal retinol dehydrogenase
Mol. Genet. Metab.
78
119-135
2003
Homo sapiens
brenda
Janecke, A.R.; Thompson, D.A.; Utermann, G.; Becker, C.; Hubner, C.A.; Schmid, E.; McHenry, C.L.; Nair, A.R.; Ruschendorf, F.; Heckenlively, J.; Wissinger, B.; Nurnberg, P.; Gal, A.
Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy
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2004
Homo sapiens
brenda
Gallego, O.; Belyaeva, O.V.; Porte, S.; Ruiz, F.X.; Stetsenko, A.V.; Shabrova, E.V.; Kostereva, N.V.; Farres, J.; Pares, X.; Kedishvili, N.Y.
Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids
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399
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2006
Homo sapiens (Q8TC12)
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Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids
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44
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Homo sapiens, Homo sapiens (Q96NR8)
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Role of photoreceptor-specific retinol dehydrogenase in the retinoid cycle in vivo
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280
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2005
Mus musculus
brenda
Kasus-Jacobi, A.; Ou, J.; Birch, D.G.; Locke, K.G.; Shelton, J.M.; Richardson, J.A.; Murphy, A.J.; Valenzuela, D.M.; Yancopoulos, G.D.; Edwards, A.O.
Functional characterization of mouse RDH11 as a retinol dehydrogenase involved in dark adaptation in vivo
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280
20413-20420
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Understanding retinol metabolism: Structure and function of retinol dehydrogenases
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281
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Bos taurus, Mus musculus
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Retinol dehydrogenase (RDH12) protects photoreceptors from light-induced degeneration in mice
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49
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2006
Mus musculus
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Ala-Laurila, P.; Kolesnikov, A.V.; Crouch, R.K.; Tsina, E.; Shukolyukov, S.A.; Govardovskii, V.I.; Koutalos, Y.; Wiggert, B.; Estevez, M.E.; Cornwall, M.C.
Visual cycle: Dependence of retinol production and removal on photoproduct decay and cell morphology
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128
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2006
Ambystoma tigrinum
brenda
Du, K.; Liu, G.F.; Xie, J.P.; Song, X.H.; Li, R.; Liang, B.; Huang, D.Y.
A 27.368 kDa retinal reductase in New Zealand white rabbit liver cytosol encoded by the peroxisomal retinol dehydrogenase-reductase cDNA: purification and characterization of the enzyme
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85
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2007
Oryctolagus cuniculus (Q9GKX2), Oryctolagus cuniculus
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Lee, S.; Belyaeva, O.V.; Kedishvili, N.Y.
Effect of lipid peroxidation products on the activity of human retinol dehydrogenase 12 (RDH12) and retinoid metabolism
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1782
421-425
2008
Homo sapiens
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Belyaeva, O.V.; Korkina, O.V.; Stetsenko, A.V.; Kedishvili, N.Y.
Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity
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Homo sapiens (Q8NBN7), Homo sapiens
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Expression of a novel alternatively spliced variant of NADP(H)-dependent retinol dehydrogenase/reductase with deletion of exon 3 in cervical squamous carcinoma
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120
1618-1626
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Homo sapiens (Q9BTZ2), Homo sapiens
brenda
Kanan, Y.; Wicker, L.D.; Al-Ubaidi, M.R.; Mandal, N.A.; Kasus-Jacobi, A.
Retinol dehydrogenases RDH11 and RDH12 in the mouse retina: expression levels during development and regulation by oxidative stress
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49
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2008
Mus musculus, Mus musculus (Q8BYK4), Mus musculus (Q9QYF1)
brenda
Keller, B.; Adamski, J.
RDH12, a retinol dehydrogenase causing Lebers congenital amaurosis, is also involved in steroid metabolism
J. Steroid Biochem. Mol. Biol.
104
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2007
Homo sapiens, Mus musculus
brenda
Maeda, A.; Maeda, T.; Sun, W.; Zhang, H.; Baehr, W.; Palczewski, K.
Redundant and unique roles of retinol dehydrogenases in the mouse retina
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104
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Mus musculus (Q8BYK4)
brenda
Lei, Z.; Chen, W.; Zhang, M.; Napoli, J.L.
Reduction of all-trans-retinal in the mouse liver peroxisome fraction by the short-chain dehydrogenase/reductase RRD: induction by the PPAR alpha ligand clofibrate
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4190-4196
2003
Mus musculus
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Belyaeva, O.V.; Lee, S.A.; Kolupaev, O.V.; Kedishvili, N.Y.
Identification and characterization of retinoid-active short-chain dehydrogenases/reductases in Drosophila melanogaster
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1790
1266-1273
2009
Drosophila melanogaster (Q7JUS1), Drosophila melanogaster (Q7JYX2), Drosophila melanogaster (Q8MZG9), Drosophila melanogaster (Q9W404)
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Pares, X.; Farres, J.; Kedishvili, N.; Duester, G.
Medium- and short-chain dehydrogenase/reductase gene and protein families: Medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism
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65
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Homo sapiens, Mus musculus, Rattus norvegicus
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Yao, Y.; Han, W.; Zhou, Y.; Luo, Q.; Li, Z.
Catalytic reaction mechanism of human photoreceptor retinol dehydrogenase: A theoretical study
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7
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2008
Homo sapiens
-
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Marchette, L.D.; Thompson, D.A.; Kravtsova, M.; Ngansop, T.N.; Mandal, M.N.; Kasus-Jacobi, A.
Retinol dehydrogenase 12 detoxifies 4-hydroxynonenal in photoreceptor cells
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48
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Mus musculus (Q8BYK4), Mus musculus (Q9QYF1), Mus musculus
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Haller, F.; Moman, E.; Hartmann, R.W.; Adamski, J.; Mindnich, R.
Molecular framework of steroid/retinoid discrimination in 17beta-hydroxysteroid dehydrogenase type 1 and photoreceptor-associated retinol dehydrogenase
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399
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Danio rerio, Homo sapiens (Q9NYR8), Homo sapiens
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Tsigelny, I.; Baker, M.E.
Structures important in NAD(P)(H) specificity for mammalian retinol and 11-cis-retinol dehydrogenases
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226
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1996
Rattus norvegicus
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Lee, S.A.; Belyaeva, O.V.; Kedishvili, N.Y.
Evidence that proteosome inhibitors and chemical chaperones can rescue the activity of retinol dehydrogenase 12 mutant T49M
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191
55-59
2011
Homo sapiens
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Chen, C.; Thompson, D.A.; Koutalos, Y.
Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12
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287
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Mus musculus, Mus musculus C57BL/6 x 129/Sv
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Wang, H.; Cui, X.; Gu, Q.; Chen, Y.; Zhou, J.; Kuang, Y.; Wang, Z.; Xu, X.
Retinol dehydrogenase 13 protects the mouse retina from acute light damage
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18
1021-1030
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Mus musculus, Mus musculus C57BL/6 x 129/Sv
brenda
Adams, M.K.; Belyaeva, O.V.; Wu, L.; Kedishvili, N.Y.
The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis
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289
14868-14880
2014
Homo sapiens (O75911), Mus musculus (O88876), Mus musculus (Q8VCH7), Mus musculus
brenda
Obrochta, K.M.; Krois, C.R.; Campos, B.; Napoli, J.L.
Insulin regulates retinol dehydrogenase expression and all-trans-retinoic acid biosynthesis through FoxO1
J. Biol. Chem.
290
7259-7268
2015
Mus musculus (Q8VCH7)
brenda
Hong, S.H.; Ngo, H.P.; Nam, H.K.; Kim, K.R.; Kang, L.W.; Oh, D.K.
Alternative biotransformation of retinal to retinoic acid or retinol by an aldehyde dehydrogenase from Bacillus cereus
Appl. Environ. Microbiol.
82
3940-3946
2016
Bacillus cereus
brenda
Lhor, M.; Methot, M.; Horchani, H.; Salesse, C.
Structure of the N-terminal segment of human retinol dehydrogenase 11 and its preferential lipid binding using model membranes
Biochim. Biophys. Acta
1848
878-885
2015
Homo sapiens
brenda
Arregi, I.; Climent, M.; Iliev, D.; Strasser, J.; Gouignard, N.; Johansson, J.K.; Singh, T.; Mazur, M.; Semb, H.; Artner, I.; Minichiello, L.; Pera, E.M.
Retinol dehydrogenase-10 regulates pancreas organogenesis and endocrine cell differentiation via paracrine retinoic acid signaling
Endocrinology
157
4615-4631
2016
Mus musculus
brenda
Kummalue, T.; Inoue, T.; Miura, Y.; Narusawa, M.; Inoue, H.; Komatsu, N.; Wanachiwanawin, W.; Sugiyama, D.; Tani, K.
Ribosomal protein L11- and retinol dehydrogenase 11-induced erythroid proliferation without erythropoietin in UT-7/Epo erythroleukemic cells
Exp. Hematol.
43
414-423.e1
2015
Homo sapiens
brenda
Jiang, W.; Napoli, J.
The retinol dehydrogenase Rdh10 localizes to lipid droplets during acyl ester biosynthesis
J. Biol. Chem.
288
589-597
2013
Mus musculus
brenda
Kolesnikov, A.V.; Maeda, A.; Tang, P.H.; Imanishi, Y.; Palczewski, K.; Kefalov, V.J.
Retinol dehydrogenase 8 and ATP-binding cassette transporter 4 modulate dark adaptation of M-cones in mammalian retina
J. Physiol.
593
4923-4941
2015
Mus musculus
brenda
Belyaeva, O.V.; Adams, M.K.; Popov, K.M.; Kedishvili, N.Y.
Generation of retinaldehyde for retinoic acid biosynthesis
Biomolecules
10
5
2019
Homo sapiens (Q8IZV5), Mus musculus (Q8VCH7)
brenda
Friedl, R.M.; Raja, S.; Metzler, M.A.; Patel, N.D.; Brittian, K.R.; Jones, S.P.; Sandell, L.L.
RDH10 function is necessary for spontaneous fetal mouth movement that facilitates palate shelf elevation
Dis. Model. Mech.
12
dmm039073
2019
Mus musculus (Q8VCH7)
brenda
Sarkar, H.; Moosajee, M.
Retinol dehydrogenase 12 (RDH12) Role in vision, retinal disease and future perspectives
Exp. Eye Res.
188
107793
2019
Mus musculus, Homo sapiens (Q96NR8), Homo sapiens
brenda
Sarkar, H.; Dubis, A.M.; Downes, S.; Moosajee, M.
Novel heterozygous deletion in retinol dehydrogenase 12 (RDH12) causes familial autosomal dominant retinitis pigmentosa
Front. Genet.
11
335
2020
Homo sapiens (Q96NR8)
brenda
Suzuki, H.; Ozaki, Y.; Gen, K.; Kazeto, Y.
Japanese eel retinol dehydrogenases 11/12-like are 17-ketosteroid reductases involved in sex steroid synthesis
Gen. Comp. Endocrinol.
305
113685
2021
Anguilla japonica
brenda
Boyer, N.P.; Thompson, D.A.; Koutalos, Y.
Relative contributions of all-trans and 11-cis retinal to formation of lipofuscin and A2E accumulating in mouse retinal pigment epithelium
Invest. Ophthalmol. Vis. Sci.
62
1
2021
Mus musculus (D3Z6W3), Mus musculus
brenda
Belyaeva, O.V.; Wu, L.; Shmarakov, I.; Nelson, P.S.; Kedishvili, N.Y.
Retinol dehydrogenase 11 is essential for the maintenance of retinol homeostasis in liver and testis in mice
J. Biol. Chem.
293
6996-7007
2018
Mus musculus (Q9QYF1)
brenda
Adams, M.K.; Belyaeva, O.V.; Kedishvili, N.Y.
Generation and isolation of recombinant retinoid oxidoreductase complex
Methods Enzymol.
637
77-93
2020
Homo sapiens (O75911), Homo sapiens (Q8IZV5)
brenda
Tian, J.; Liu, J.; Li, J.; Zheng, J.; Chen, L.; Wang, Y.; Liu, Q.; Ni, J.
The interaction of selenoprotein F (SELENOF) with retinol dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A metabolism
Nutr. Metab.
15
7
2018
Homo sapiens (Q8TC12), Homo sapiens
brenda
Guan, F.; Wang, L.; Hao, S.; Wu, Z.; Bai, J.; Kang, Z.; Zhou, Q.; Chang, H.; Yin, H.; Li, D.; Tian, K.; Ma, J.; Zhang, G.; Zhang, J.
Retinol dehydrogenase-10 promotes development and progression of human glioma via the TWEAK-NF-kappaB axis
Oncotarget
8
105262-105275
2017
Homo sapiens (Q8IZV5), Homo sapiens
brenda
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 (Q8VCH7)
brenda
Morshedian, A.; Kaylor, J.J.; Ng, S.Y.; Tsan, A.; Frederiksen, R.; Xu, T.; Yuan, L.; Sampath, A.P.; Radu, R.A.; Fain, G.L.; Travis, G.H.
Light-driven regeneration of cone visual pigments through a mechanism involving RGR opsin in Mueller glial cells
Neuron
102
1172-1183.e5
2019
Gallus gallus (A0A3Q3ATC8), Homo sapiens (Q8IZV5), Mus musculus (Q8VCH7)
brenda