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Enzyme Nomenclature
Information on EC 1.1.1.300 - NADP-retinol dehydrogenase
Word Map on EC 1.1.1.300
- 1.1.1.300
-
retinoids
- photoreceptors
- all-trans-retinal
- 11-cis-retinal
- epithelium
-
chromophore
-
nadph-dependent
-
cone
-
vision
- retinaldehyde
-
bleaching
-
electroretinogram
- amaurosis
-
leber
- erg
- medicine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.1.1.300
-
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RECOMMENDED NAME
GeneOntology No.
NADP-retinol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
retinol + NADP+ = retinal + NADPH + H+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
retinol:NADP+ oxidoreductase
Greater catalytic efficiency in the reductive direction. This observation, and the enzyme's localization at the entrance to the mitochondrial matrix, suggest that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinal produced from dietary beta-carotene by EC 1.13.11.63 (beta-carotene 15,15'-dioxygenase) [2]. Km-values for NADP+ and NADPH are at least 800-fold lower than those for NAD+ and NADH [1,4]. This enzyme differs from EC 1.1.1.105, retinol dehydrogenase, which prefers NAD+ and NADH.
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CAS REGISTRY NUMBER
COMMENTARY
90033-53-8
cf. EC 1.1.1.105
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene harbours two initiation sites, one of which encodes a 279 and the other a 260 amino acids protein
SwissProt
; isoform 4, from full length cDNA, isoform of NRDR without residues 85-118; alternatively spliced variant NRDRB1 with a complete deletion of exon 3, activity of NRDRB1 much lower than activity of NRDR in forward and reverse reaction; isoform 5, from full length cDNA, isoform of NRDR without residues 85-118 and 160-204; alternatively spliced variant NRDRB2 with a complete deletion of exons 3 and 6; isoform 6, from full length cDNA, isoform of NRDR without residues 1-203; alternatively spliced variant NRDRA1 with a complete deletion of exons 3-6
UniProt
Austrian kindreds with individuals affected by autosomal recessive childhood-onset severe retinal dystrophy
-
-
mouse monoclonal anti-GRK1 (G-proteinassociated rhodopsin kinase-1)
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
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 45–63% 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
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
11-cis-retinal + NADH + H+
11-cis-retinol + NAD+
NADH much less efficient than NADPH
-
-
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
13-cis-retinal + NADPH + H+
13-cis-retinol + NADP+
-
4fold lower activity than with all-trans-retinal
-
-
?
9-cis-retinal + NADPH + H+
9-cis-retinol + NADP+
-
60fold lower activity than with all-trans-retinal
-
-
?
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-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-retinol + NAD+
all-trans-retinal + NADH + H+
low activity with NAD+ as cofactor
-
-
r
cis-6-nonenal + NADPH + H+
?
-
good substrate of RDH11 and RDH12, while RHD10 has very low activity towards this substrate
-
-
?
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
-
-
?
(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+
-
-
-
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+
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)+
-
-
r
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-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+
-
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+
-
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+
-
-
-
-
?
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
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
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
n-nonanal + NADPH + H+
n-nonanol + NADP+
Q96NR8
might play a role in detoxification of lipid peroxidation products
-
-
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+
-
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+
-
-
-
-
?
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
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors
NADH
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
NADH
prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors
NADP+
prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors
NADP+
-
lysine64 is important in the specificity of 11-cis retinol dehydrogenase for NADP+
NADPH
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
NADPH
prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors; prefers NADP+ and NADPH as cofactors
NADPH
-
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3beta)-3-[(3-carboxypropanoyl)oxy]-11-oxoolean-12-en-30-oic acid
-
0.5 mM, 60% of inhibition
-
1,2-diheptanoyl-sn-glycero-3-phosphocholine
substitution of the detergent 1,2-diheptanoyl-sn-glycero-3-phosphocholine for Tween-20 results in complete inactivation of the enzyme
additional information
-
not inhibitory: methylpyrazole, phenylmethylsulfonylfluoride
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00027
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
0.0004
all-trans-retinal
Km-value is determined for microsomal preparations expressing recombinant Drosophila proteins
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
0.004
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.012
-
mutant enzyme C300S, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.0386
-
mutant enzyme C300S, with retinal and NAD+ as substrates, at pH 7.0 and 37°C
0.068
-
mutant enzyme C300A, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.08
-
mutant enzyme E266A, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.136
-
wild type enzyme, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.26
-
mutant enzyme E457V, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.408
-
mutant enzyme E194S, with retinal and NADPH as substrates, at pH 7.0 and 37°C
0.461
-
wild type enzyme, with retinal and NAD+ as substrates, at pH 7.0 and 37°C
0.493
-
mutant enzyme E194S, with retinal and NAD+ as substrates, at pH 7.0 and 37°C
0.63
-
eluate after purification, the specific activity of the purified enzyme with all-trans-retinal as substrate is 13fold higher than that of the microsomal preparation of wild-type
2.536
-
mutant enzyme E457V, with retinal and NAD+ as substrates, at pH 7.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
detected in 54% of cervical tumor tissue samples but not in normal cervical tissue; detected in cervical tumor tissue samples where NRDRB1 could not be detected; normal and neoplastic cervical tissue samples
level of isoform Rdh11 is low and remarkably constant during development and oxidative stress. Rdh12 expression starts at postnatal day 7 and increases until postnatal day 30 to approximately sevenfold higher than Rdh11. Oxidative stress induced by exposure to constant bright light leads to a rapid and significant decrease of Rdh12 protein; RDH12 expression starts at postnatal day and increases until postnatal day 30. Oxidative stress induced by exposure to constant bright light leads to a rapid and significant decrease of RDH12 protein; the RDH11 level is low and remarkably constant during development and oxidative stress
; expression in inner segments, cell bodies and synaptic termini of photoreceptors
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
associated with microsomal membranes; associated with microsomal membranes; associated with microsomal membranes; associated with microsomal membranes
RDH13 is localized on the outer side of the inner mitochondrial membrane
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27430
2 * 27430, calculated from the deduced amino acid sequence, native mass by gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 23917, calculated from the deduced amino acid sequence; x * 27572, calculated from the deduced amino acid sequence
dimer
2 * 27000, SDS-PAGE, native mass by gel filtration; 2 * 27368, MALDI-TOF MS, native mass by gel filtration; 2 * 27430, calculated from the deduced amino acid sequence, native mass by gel filtration
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alignment of Streptomyces hydrogenans 20beta-hydroxysteroid dehydrogenase with rat retinol dehydrogenase and cow 11-cis retinol dehydrogenase. Lysine64 of the rat enzyme is important in stabilizing binding of 2'-phosphate on NADP+ in two ways: lysine's positively charged side chain has a coulombic attraction to the 2'-phosphate and partially compensates for the negative charge of aspartic acid-38. Cow 11-cis retinol dehydrogenase has threonine61 at the position homologous to lysine64. Threonine61 does not have a stabilizing coulombic interaction with NADP+, nor can threonine61 counteract the repulsive interaction between NADP+ and aspartic acid37 in 11-cis retinol dehydrogenase
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, buffer containing 1 mM 1,2-diheptanoyl-sn-glycero-3-phosphocholine, stable for several months
-
8°C, in a refrigerator, the enzyme is nearly fully active for at least one month
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned as a gene regulated by the transcription factor sterol regulatory element binding proteins and previously named SCALD for short chain aldehyde reductase
expressed in native, soluble form in Escherichia coli BL21-AI and as GFP-fusion protein in HeLa-cells; GFP-fusion protein in HeLa-cells
expression in HEK-293 cell
expression in HeLa cell and 293T cell
expression in Sf9 cells; expression in Sf9 cells; expression in Sf9 cells; expression in Sf9 cells
full-length short-chain dehydrogenase/reductase cDNA expressed in Escherichia coli, truncated cDNA expressed in SF9 insect cells, enzyme belongs to the short-chain dehydrogenase/reductase superfamily
-
stable transfection of HEK-293 cells; stable transfection of HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oral gavage with glucose or injection with insulin decreases Rdh10 mRNA 50% or greater in mouse liver
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
I51N
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
T49M
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
additional information
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
enzyme is associated with retinal dystrophy and encodes an enzyme with unique, nonredundant role in the photoreceptor cells
medicine
-
transfection with retinol dehydrogenase 12 protects cells against nonanal-induced toxicity but is ineffective against 4-hydroxynonenal. 4-Hydroxynonenal strongly inhibits the activities of lecithin:retinol acyl transferase and aldehyde dehydrogenase, resulting in decreased levels of retinyl esters and retinoic acid and accumulation of unesterified retinol
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.300)
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