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evolution
-
RDHs that catalyze the interconversion of retinal and retinol involved in rhodopsin turnover are members of the family of short chain dehydrogenase/reductases
malfunction

-
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
-
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
-
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
-
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
-
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
-
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; 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
-
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
-
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
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; 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 enzyme affects dorsal pancreas development and participates in the terminal differentiation of endocrine cells
physiological function
-
the enzyme accelerates erythroid cell proliferation by upregulating the STAT5 signaling pathway
physiological function
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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 + 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+
-
-
-
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+
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+
-
-
-
-
r
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+
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+
-
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+
-
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+
-
-
-
-
?
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+
-
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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+
Q96NR8
-
-
-
r
11-cis-retinol + NADP+
11-cis-retinal + NADPH + H+
Q96NR8, Q9HBH5
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+
Q96NR8, Q9HBH5
possibly involved in the first step of 9-cis-retinoic acid production
-
-
r
all-trans retinal + NADPH + H+
all-tans-retinol + NADP+
Q96NR8
-
-
-
r
all-trans-retinal + NADPH + H+
all-tans-retinol + NADP+
Q9GKX2
-
-
-
?
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+
Q96NR8
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+
O75911
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
-
r
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
O75911
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+
Q8NBN7
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+
-
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+
-
the enzyme plays a role in retinoid metabolism
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
Q8TC12
involved in retinoid homeostasis in the prostate
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
Q96NR8, Q9HBH5
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+
Q9BTZ2
important for the maintenance of retinoid homeostasis
-
-
r
retinol + NADP+
retinal + NADPH + H+
Q9BTZ2
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+
-
-
-
-
?
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
?
-
-
the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
-
-
-
additional information
?
-
Q8BYK4
the low and constant expression of RDH11 suggests a housekeeping function for this enzyme in retina
-
-
-
additional information
?
-
Q9QYF1
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
?
-
Q8BYK4
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
?
-
Q9QYF1
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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0.0001
11-cis-retinal
-
pH 7.4, 37°C
0.0016
11-cis-retinol
-
pH 7.4, 37°C
0.62
13-cis-retinal
-
pH 7.4, 37°C, determined with NADP+
0.00014 - 0.19
9-cis-retinal
0.0016
9-cis-retinol
-
pH 7.4, 37°C
0.0032 - 0.0044
all-trans-3-hydroxyretinal
0.00006 - 0.5
all-trans-retinal
0.0006 - 1.3
all-trans-retinol
additional information
additional information
-
0.00014
9-cis-retinal

-
pH 7.4, 37°C
0.19
9-cis-retinal
-
pH 7.4, 37°C, determined with NADP+
0.0032
all-trans-3-hydroxyretinal

Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.0041
all-trans-3-hydroxyretinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.0044
all-trans-3-hydroxyretinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.00006
all-trans-retinal

-
wild-type
0.00012
all-trans-retinal
-
purified recombinant enzyme
0.0002
all-trans-retinal
-
membrane-bound wild-type
0.00027
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.00028
all-trans-retinal
-
mutant T49M
0.0004
all-trans-retinal
-
-
0.0004
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.00041
all-trans-retinal
-
mutant I51N
0.0006
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.0007
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.00126
all-trans-retinal
-
wild-type, pH 7.3, 37°C
0.0017
all-trans-retinal
-
mutant M146G, pH 7.3, 37°C
0.0023
all-trans-retinal
-
mutant M144G, pH 7.3, 37°C
0.003
all-trans-retinal
-
mutant M147G, pH 7.3, 37°C
0.0031
all-trans-retinal
-
wild-type isoform prRDH1, pH 7.3, 37°C
0.0032
all-trans-retinal
-
0.0044
all-trans-retinal
-
wild-type isoform prRDH1, pH 7.3, 37°C
0.3
all-trans-retinal
-
37°C
0.5
all-trans-retinal
-
pH 7.4, 37°C, determined with NADP+
0.0006
all-trans-retinol

-
purified recombinant enzyme
0.0007
all-trans-retinol
-
membrane-bound wild-type
0.004
all-trans-retinol
-
pH 7.4, 37°C
0.004
all-trans-retinol
Km-value for all-trans-retinol is similar to that for retinal however, the rate of retinol oxidation by RDH13 is extremely low
0.18
all-trans-retinol
-
37°C
1.3
all-trans-retinol
-
pH 7.4, 37°C, determined with NADPH
0.0096
estrone

-
mutant M144G, pH 7.3, 37°C
0.0233
estrone
-
mutant M147G, pH 7.3, 37°C
0.0307
estrone
-
mutant M146G, pH 7.3, 37°C
0.004
NAD+

-
at pH 7.0 and 37°C
680
NAD+
-
pH 7.4, 37°C, determined with all-trans-retinol
2.22
NADH

-
pH 7.4, 37°C
1300
NADH
-
pH 7.4, 37°C, determined with all-trans-retinal
0.0004
NADP+

-
membrane-bound wild-type
0.001
NADP+
-
purified recombinant enzyme
0.0012
NADP+
-
pH 7.4, 37°C
0.0032
NADP+
-
pH 7.4, 37°C
0.0042
NADP+
-
at pH 7.0 and 37°C
0.8
NADP+
-
pH 7.4, 37°C, determined with all-trans-retinol
0.00047
NADPH

-
purified recombinant enzyme
0.00048
NADPH
-
membrane-bound wild-type
0.00074
NADPH
-
pH 7.4, 37°C
0.0012
NADPH
-
pH 7.4, 37°C
0.033
NADPH
-
mutant T49M
0.04
NADPH
-
at pH 7.0 and 37°C
0.105
NADPH
-
mutant I51N
0.23
NADPH
-
pH 7.4, 37°C, determined with all-trans-retinal
0.007
retinal

-
with NAD+ as cosubstrate, at pH 7.0 and 37°C
0.13
retinal
-
with NADPH as cosubstrate, at pH 7.0 and 37°C
additional information
additional information

-
recombinant RRD reduces free retinal (not bound with cellular retinol binding protein) with a K0.5 value of 0.0023 mM and a Hill constant of 1.7, and reduces CRBP(I)-bound retinal (2fold molar excess of cellular retinol binding protein(I) at each retinal concentration) with a K0.5 value of 0.0086 mM and a Hill constant of 2.1
-
additional information
additional information
CG2070-expessing microsomes do not show saturation with up to 0.008 mM all-trans-3-hydroxyretinaldehyde
-
additional information
additional information
CG2070-expessing microsomes do not show saturation with up to 0.008 mM all-trans-3-hydroxyretinaldehyde
-
additional information
additional information
CG2070-expessing microsomes do not show saturation with up to 0.008 mM all-trans-3-hydroxyretinaldehyde
-
additional information
additional information
CG2070-expessing microsomes do not show saturation with up to 0.008 mM all-trans-3-hydroxyretinaldehyde
-
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C300A
-
the mutant shows no oxidation activity
C300S
-
the mutant shows reduced catalytic efficiency for the oxidation and reduction of all-trans-retinal compared to the wild-type enzyme
E194S
-
the mutant shows 15fold higher catalytic efficiency for the reduction of all-trans-retinal than the wild-type enzyme
E266A
-
the mutant shows no oxidation activity
E457V
-
the mutant shows 7.5fold higher catalytic efficiency for the reduction of all-trans-retinal than the wild-type enzyme
M146G
-
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
L99I
-
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
-
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
-
site-directed mutagenesis, no catalytic activity. Protein is stable and abundantly expressed
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
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
-
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
T49M

-
mutation found in an individual affected by autosomal recessive childhood-onset severe retinal dystrophy
T49M
-
site-directed mutagenesis, significant activity in vitro. Dramatically reduced affinity for NADPH results in loss of function within cells
T49M
-
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
additional information

-
transfection with retinol dehydrogenase 12 protects cells against nonanal-induced toxicity but is ineffective against 4-hydroxynonenal
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
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
J. Biol. Chem.
273
21790-21799
1998
Homo sapiens (O75911)
brenda
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
14838-14845
2003
Homo sapiens
brenda
Kedishvili, N.Y.; Chumakova, O.V.; Chetyrkin, S.V.; Belyaeva, O.V.; Lapshina, E.A.; Lin, D.W.; Matsumura, M.; Nelson, P.S.
Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1)
J. Biol. Chem.
277
28909-28915
2002
Homo sapiens, Homo sapiens (Q8TC12)
brenda
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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277
45537-45546
2002
Homo sapiens, Homo sapiens (Q96NR8), Homo sapiens (Q9HBH5)
brenda
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
Nat. Genet.
36
850-854
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
Biochem. J.
399
101-109
2006
Homo sapiens, Homo sapiens (Q8TC12)
brenda
Belyaeva, O.V.; Korkina, O.V.; Stetsenko, A.V.; Kim, T.; Nelson, P.S.; Kedishvili, N.Y.
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
Biochemistry
44
7035-7047
2005
Homo sapiens, Homo sapiens (Q96NR8)
brenda
Maeda, A.; Maeda, T.; Imanishi, Y.; Kuksa, V.; Alekseev, A.; Bronson, J.D.; Zhang, H.; Zhu, L.; Sun, W.; Saperstein, D.A.; Rieke, F.; Baehr, W.; Palczewski, K.
Role of photoreceptor-specific retinol dehydrogenase in the retinoid cycle in vivo
J. Biol. Chem.
280
18822-18832
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
J. Biol. Chem.
280
20413-20420
2005
Homo sapiens (O75911), Homo sapiens (Q8TC12), Homo sapiens (Q92781), Homo sapiens (Q96NR8), Homo sapiens (Q9HBH5), Homo sapiens (Q9NYR8), Mus musculus, Mus musculus (Q9QYF1)
brenda
Liden, M.; Eriksson, U.
Understanding retinol metabolism: Structure and function of retinol dehydrogenases
J. Biol. Chem.
281
13001-13004
2006
Bos taurus, Mus musculus
brenda
Maeda, A.; Maeda, T.; Imanishi, Y.; Sun, W.; Jastrzebska, B.; Hatala, D.A.; Winkens, H.J.; Hofmann, K.P.; Janssen, J.J.; Baehr, W.; Driessen, C.A.; Palczewski, K.
Retinol dehydrogenase (RDH12) protects photoreceptors from light-induced degeneration in mice
J. Biol. Chem.
49
37697-37704
2006
Mus musculus
brenda
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
J. Gen. Physiol.
128
153-169
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
Biochem. Cell Biol.
85
209-217
2007
Oryctolagus cuniculus, Oryctolagus cuniculus (Q9GKX2)
brenda
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
Biochim. Biophys. Acta
1782
421-425
2008
Homo sapiens
brenda
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
FEBS J.
275
138-147
2008
Homo sapiens, Homo sapiens (Q8NBN7)
brenda
Song, X.H.; Liang, B.; Liu, G.F.; Li, R.; Xie, J.P.; Du, K.; Huang, D.Y.
Expression of a novel alternatively spliced variant of NADP(H)-dependent retinol dehydrogenase/reductase with deletion of exon 3 in cervical squamous carcinoma
Int. J. Cancer
120
1618-1626
2007
Homo sapiens, Homo sapiens (Q9BTZ2)
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
Invest. Ophthalmol. Vis. Sci.
49
1071-1078
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
190-194
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
Proc. Natl. Acad. Sci. USA
104
19565-19570
2007
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
Biochemistry
42
4190-4196
2003
Mus musculus
brenda
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
Biochim. Biophys. Acta
1790
1266-1273
2009
Drosophila melanogaster (Q7JUS1), Drosophila melanogaster (Q7JYX2), Drosophila melanogaster (Q8MZG9), Drosophila melanogaster (Q9W404)
brenda
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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2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
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
565-578
2008
Homo sapiens
-
brenda
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, Mus musculus (Q8BYK4), Mus musculus (Q9QYF1)
brenda
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
255-267
2010
Danio rerio, Homo sapiens, Homo sapiens (Q9NYR8)
brenda
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
118-127
1996
Rattus norvegicus
brenda
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
Chem. Biol. Interact.
191
55-59
2011
Homo sapiens
brenda
Chen, C.; Thompson, D.A.; Koutalos, Y.
Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12
J. Biol. Chem.
287
24662-24670
2012
Mus musculus 129/Sv and C57BL/6, Mus musculus
brenda
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
Mol. Vis.
18
1021-1030
2012
Mus musculus 129Sv x C57BL/6 backcrossed with wild-type line 129SV, Mus musculus
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
J. Biol. Chem.
289
14868-14880
2014
Homo sapiens (O75911), Mus musculus (O88876), Mus musculus (Q8VCH7)
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