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Information on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+) and Organism(s) Homo sapiens and UniProt Accession Q92781
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1.1.1.105 all-trans-retinol dehydrogenase (NAD+)IUBMB Comments
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form . No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3alpha-hydroxysteroids .
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Word Map
- 1.1.1.105
-
retinoids
- dystrophy
- amaurosis
- photoreceptors
-
leber
- retinaldehyde
- pigmentosa
-
dehalogenase
-
all-trans-retinoic
-
retinol-binding
- all-trans-retinal
- raldhs
-
darwin
- dehalococcoides
- 11-cis-retinal
-
rpgrip1
-
retinyl
-
dechlorination
- aldh1a2
-
gucy2d
- all-trans-retinaldehyde
-
cyp26b1
-
cone-rod
-
neurosteroidogenic
-
crabp2
-
albipunctatus
-
organohalide
-
3alpha-hydroxysteroids
- srd5a1
-
hiding
- synthesis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
=
+
+
all-trans-retinol-[cellular-retinol-binding-protein]
+
=
all-trans-retinal-[cellular-retinol-binding-protein]
+
+
Synonyms
rdh, rdh12, rdh10, dhrs9, retinal reductase, rodh-4, retinol dehydrogenase 12, rdh16, retinol dehydrogenase 10, rdhe2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
all-trans retinol dehydrogenase
-
-
-
-
dehydrogenase, retinol
-
-
-
-
MDR
-
-
-
-
microsomal retinol dehydrogenase
-
-
-
-
P32
-
-
-
-
RDH10
RDH16
retinal reductase
-
-
-
-
retinene reductase
-
-
-
-
retinol dehydrogenase (vitamin A1)
-
-
-
-
retinol dehydrogenase 10
retinol dehydrogenase 4
RoDH-4
RoDH-4
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
all-trans retinol:NAD+ oxidoreductase
The enzyme recognizes all-trans-retinol and all-trans-retinal as substrates and exhibits a strong preference for NAD+/NADH as cofactors. Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein (CRBP1), but has higher affinity for the bound form [2]. No activity with 11-cis-retinol or 11-cis-retinal (cf. EC 1.1.1.315, 11-cis retinol dehydrogenase). Also active with 3alpha-hydroxysteroids [2].
CAS REGISTRY NUMBER
COMMENTARY
9033-53-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-didehydroretinol + NAD+
3,4-didehydroretinal + NADH
-
60% of the efficiency against all-trans-retinol
-
-
?
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
-
-
-
?
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
-
-
-
r
retinol bound to cellular retinol binding protein + NAD+
retinal bound to cellular retinol binding protein + NADH
-
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
wild type RDH10 catalyzes both oxidation of all-trans retinol and reduction of all-trans retinal in vitro. On cultured cells, however, oxidation is the favored reaction catalyzed by RDH10.
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1
-
-
ir
additional information
?
-
-
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid
-
-
?
additional information
?
-
-
substrate bound to cellular retinol binding protein is preferred
-
-
?
additional information
?
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
NAD+-dependent retinoid-active SDRs have higher catalytic efficiencies for the oxidation of 3alpha-hydroxysterols than of retinols
-
-
?
additional information
?
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
additional information
?
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
NATURAL SUBSTRATE
NATURAL 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
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
additional information
?
-
-
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid
-
-
?
additional information
?
-
-
NAD+-dependent retinoid-active SDRs have higher catalytic efficiencies for the oxidation of 3alpha-hydroxysterols than of retinols
-
-
?
additional information
?
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
NAD+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
imidazole
increasing the amount of imidazole in the reaction mixture with purified RDH-E2 from 25 to 225mM significantly decreases RDH-E2 activity
additional information
all-trans-retinol and 13-cis-retinol inhibit RoDH-4 catalyzed oxidation of androsterone
-
additional information
-
all-trans-retinol and 13-cis-retinol inhibit RoDH-4 catalyzed oxidation of androsterone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00006
11-cis-retinol
pH and temperature not specified in the publication
0.00046
all-trans retinal
pH not specified in the publication, temperature not specified in the publication
0.57
all-trans-retinal
wild type enzyme, in 100 mM sodium phosphate, pH 7.4
0.00046
all-trans-retinaldehyde
pH and temperature not specified in the publication
0.000039
all-trans-retinol
pH and temperature not specified in the publication
0.000039
all-trans-retinol
pH not specified in the publication, temperature not specified in the publication
0.0041
all-trans-retinol
wild type enzyme, in 100 mM sodium phosphate, pH 7.4
0.011
NADH
pH not specified in the publication, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the highest level of RDH12 expression is in the retina where it is localised to the inner segments and cell bodies of rod and cone photoreceptors
-
epidermal keratinocytes, gene is expressed predominantly in the differentiating spinous layers
retinal dehydrogenase 2 is significantly elevated in psoriatic skin
mRNA for RoDH-4 is abundant in adult liver, where it is translated into RoDH-4 protein. Significant amounts of RoDH-4 message is detected in fetal liver
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
RDH-E2 protein exhibits a punctuate localization pattern, surrounding the nucleus suggesting that RDH-E2 is associated with endoplasmic reticulum
behaves as an integral membrane protein, RoDH-4 contains four potential membrane-spanning domains
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
physiological function
physiological function
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Removing serum from the medium of the human hepatoma cell line HepG2 increases isoforms Rdh10 and Rdh16 mRNA expression 2-3-fold by 4 h, by increasing transcription and stabilizing mRNA. Insulin decreases Rdh10 and Rdh16 mRNA in HepG2 cells incubated in serum-free medium by inhibiting transcription and destabilizing mRNA. Insulin action requires PI3K and Akt, which suppress FoxO1
physiological function
RDHE2 does not partner with dehydrogenase/reductase DHRS3/SDR16C1 or cellular retinol binding protein type CRBP1
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C201R
the loss of function mutant is associated with severe loss of retinal functionand early onset severe retinal dystrophy
DELTAM1-Y13
truncated RoDH-4 that lacks the first thirteen amino acids of the N-terminal segment is partially active and exhibits the apparent Km value for androsterone similar to that of the wild-type enzyme, truncated mutant behaves as an integral membrane protein
DELTAS295-L317
removal of 23 N-terminal hydrophobic amino acids results in significant loss of activity and a 14fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
DELTAY291-L317
removal of the C-terminal 27 amino acid segment results in about 600fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
G43A/G47A/G49A
the triple mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214R
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169D
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197A
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197C
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197G
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197T
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197V
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210F
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
additional information
additional information
protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction
additional information
-
protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction
additional information
-
RDH8 genotping and phenotyping in Han Chinese population, identification of single nucleotide polymorphisms in RDH8 gene: RDH855b (-1715G/A; rs3760753), RDH851 (-472C/T; rs2233789), and RDH8E5a (7826T/C; rs1644731), overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
gel-filtration of RDH-E2 preparation to remove imidazole results in significant loss of activity (about 90%) despite nearly complete recovery of the protein suggesting that RDH-E2 is sensitive to desalting
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, reconstitution of enzyme into proteoliposomes, stable for at least 4 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
preparation of RoDH-4 contains a minor contaminating protein band. Therefore, the exact concentration of RoDH-4 is determined based on the calibration curve constructed from several concentrations of BSA loaded on to the same SDS/PAGE gel
solubilized enzyme is extremely unstable and loses almost 80% of the initial activity even at partially purified stage, purification uses resistance of enzyme to proteolysis at 4°C in the presence of 1% Triton
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
human RDHE2 exhibits a relatively low but reproducible activity when expressed in either HepG2 or HEK293 cells
human RDHE2S is unstable when expressed in HEK293 cells. RDHE2S protein produced in Sf9 cells is stable but has no detectable catalytic activity towards retinol
RDH-E2 is expressed in Sf9 insect cells as a fusion to the C-terminal His6-tag
RDH8 gene is located on 19p13, DNA and amino acid sequence determination and analysis, RDH8 genotping and phenotyping in Han Chinese population
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the native RDHE2 is downregulated in the presence of elevated levels of all-trans-retinoic acid
insulin decreases Rdh10 and Rdh16 mRNA in HepG2 cells incubated in serum-free medium by inhibiting transcription and destabilizing mRNA
removing serum from the medium of the human hepatoma cell line HepG2 increases isoforms Rdh10 and Rdh16 mRNA expression 2-3-fold by 4 h, by increasing transcription and stabilizing mRNA
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
mutations in RDH12 are associated with Leber congenital amaurosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gough, W.H.; VanOoteghem, S.; Sint, T.; Kedishvili, N.Y.
cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids
J. Biol. Chem.
273
19778-19785
1998
Homo sapiens (O75452), Homo sapiens
Jurukovski, V.; Markova, N.G.; Karaman-Jurukovska, N.; Randolph, R.K.; Su, J.; Napoli, J.L.; Simon, M.
Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes
Mol. Genet. Metab.
67
62-73
1999
Homo sapiens
Karlsson, T.; Vahlquist, A.; Kedishvili, N.; Torma, H.
13-cis-retinoic acid competitively inhibits 3alpha-hydroxysteroid oxidation by retinol dehydrogenase RoDH-4: a mechanism for its anti-androgenic effects in sebaceous glands?
Biochem. Biophys. Res. Commun.
303
273-278
2003
Homo sapiens
Lapshina, E.A.; Belyaeva, O.V.; Chumakova, O.V.; Kedishvili, N.Y.
Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4
Biochemistry
42
776-784
2003
Homo sapiens
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 (O75452), Homo sapiens
Liden, M.; Eriksson, U.
Understanding retinol metabolism: Structure and function of retinol dehydrogenases
J. Biol. Chem.
281
13001-13004
2006
Bos taurus, Homo sapiens, Mus musculus
Takahashi, Y.; Moiseyev, G.; Farjo, K.; Ma, J.X.
Characterization of key residues and membrane association domains in retinol dehydrogenase 10
Biochem. J.
419
113-122
2009
Homo sapiens (Q8IZV5)
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
Cell. Mol. Life Sci.
65
3936-3949
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Belyaeva, O.V.; Chetyrkin, S.V.; Kedishvili, N.Y.
Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4
Chem. Biol. Interact.
143-144
279-287
2003
Homo sapiens (O75462), Homo sapiens
Lee, S.A.; Belyaeva, O.V.; Kedishvili, N.Y.
Biochemical characterization of human epidermal retinol dehydrogenase 2
Chem. Biol. Interact.
178
182-187
2009
Homo sapiens (Q8N3Y7), Homo sapiens
Moradi, P.; Mackay, D.; Hunt, D.; Moore, A.
Focus on molecules: Retinol dehydrogenase 12 (RDH12)
Exp. Eye Res.
87
160-161
2008
Homo sapiens (Q96NR8)
Napoli, J.L.
Physiological insights into all-trans-retinoic acid biosynthesis
Biochim. Biophys. Acta
1821
152-167
2012
Homo sapiens, Mus musculus, Rattus norvegicus
Yu, Y.S.; Wang, L.L.; Shen, Y.; Yap, M.K.; Yip, S.P.; Han, W.
Investigation of the association between all-trans-retinol dehydrogenase (RDH8) polymorphisms and high myopia in Chinese
J. Zhejiang Univ. Sci. B
11
836-841
2010
Homo sapiens
Adams, M.K.; Lee, S.A.; Belyaeva, O.V.; Wu, L.; Kedishvili, N.Y.
Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10
Chem. Biol. Interact.
276
88-94
2017
Homo sapiens, Homo sapiens (Q8N3Y7)
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, Homo sapiens (Q8IZV5)
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
Homo sapiens (O75452), Homo sapiens (Q8IZV5), Homo sapiens, Mus musculus (Q8VIJ7), Mus musculus
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