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Information on EC 1.1.1.105 - all-trans-retinol dehydrogenase (NAD+) and Organism(s) Mus musculus and UniProt Accession O55240
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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: Mus musculus
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
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-
-
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dehydrogenase, retinol
-
-
-
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MDR
-
-
-
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microsomal retinol dehydrogenase
-
-
-
-
mRDH1
multifunctional enzyme. In addition to retinol dehydrogenase activity, RDH1 has strong 3alpha-hydroxy and weak 17beta-hydroxy steroid dehydrogenase activities
P32
-
-
-
-
Rdh1
retinal reductase
-
-
-
-
retinene reductase
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-
-
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retinol dehydrogenase (vitamin A1)
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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-
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reduction
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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
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
higher activity with all-trans-retinol versus 9-cis-retinol
-
-
?
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
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-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
RDH5 has only a minor in vivo all-trans RDH activity
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 has 811fold higher activity with NAD+ versus NADP+. Higher activity with all-trans-retinol versus 9-cis-retinol. Multifunctional enzyme. In addition to retinol dehydrogenase activity, RDH1 has strong 3alpha-hydroxy and weak 17beta-hydroxy steroid dehydrogenase activities
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
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-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1, except for RDH10 that does not access holo-CRBP1 as substrate
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-
ir
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
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-
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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
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
RDH5 has only a minor in vivo all-trans RDH activity
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
N-ethylmaleimide does not affect the catalytic action of RDH1, but interferes with its approach to holo-CRBP1, interrupting retinol transfer. Modifying RDH with N-ethylmaleimide inhibited holo-CRBP1-supported generation of retinal by 90%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.086
11-cis-retinol
recombinant enzyme, pH and temperature not specified in the publication
0.0039
all-trans-retinal
recombinant enzyme, pH and temperature not specified in the publication
0.46
NAD+
recombinant enzyme, pH and temperature not specified in the publication
0.011
NADH
recombinant enzyme, pH and temperature not specified in the publication
additional information
additional information
-
possible Michaelis-Menten relationship between RDH10 and holo-CRBP1
-
0.00087
all-trans-retinol
recombinant enzyme, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the mouse embryo expresses RDH1 as early as 7.0 days post-coitus, and expression is especially intense within the neural tube, gut, and neural crest at embryo day 10.5
Rdhe2 is observed starting at E12.5, increasing in abundance through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
Rdhe2s is detected earlier in development at E10.5 and persisted through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
additional information
RDH1 has widespread and intense mRNA expression in tissues of embryonic and adult mice
additional information
-
RDH1 has widespread and intense mRNA expression in tissues of embryonic and adult mice
additional information
analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
additional information
analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
additional information
-
analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
additional information
analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
additional information
analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
additional information
-
analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
facing the cytoplasm, mutants lacking amino-terminal 18 or 30 amino acids do not localize to endoplasmic reticulum but to mitochondria instead. Deletion mutant lacking 28 C-terminal amino acids localizes both to microsomal and mitochondrial fractions. Deletion of both 18 N-terminal and 28 C-terminal amino acids leeds to overwhelming detection in mitochondria. Fusion of N-terminal 22 amino acids of enzyme with green fluorescent protein localizes in endoplasmic reticulum. Fusion of N-terminal 18 amino acids of enzyme with green fluorescent protein shows diffuse localization. Fusion of green fluorescent protein with C-terminal 29 amino acids of enzyme shows diffuse cytoplasmic and nuclear localization
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cytoplasmic or lumenal facing, RDH1. An N-terminal signaling sequence of 22 residues anchors RDH1 in the endoplasmic reticulum projecting into the cytoplasm
enzyme RDHE2S is localized primarily in the microsomal membranes
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
-
N-ethylmaleimide does not affect the catalytic action of RDH1, but interferes with its approach to holo-CRBP1, interrupting retinol transfer. The membrane context of RDH affects function
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
-
deleting the positive charges from the C-terminal end of the leader, and inserting two arginine residues near the N-terminus of the signaling sequence causes 95% inversion from cytoplasmic to luminal: i.e. the mutant L3R/L5R/R16Q/R19Q/R21Q faces the lumen
malfunction
-
outer segments of rods deficient in Rdh8 fail to reduce all-trans-retinal. 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 or Rdh12, EC 1.1.1.300, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH12-deficient mutants
malfunction
mice lacking both the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice
malfunction
mice with targeted knockout of the more catalytically active SDR16C6 enzyme have no obvious phenotype, possibly due to functional redundancy, because Sdr16c5 and Sdr16c6 exhibit an overlapping expression pattern during later developmental stages and in adulthood. Mice lacking both epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands
metabolism
-
the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
metabolism
two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo
metabolism
two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2
physiological function
-
in vertebrate rod cells, retinoid dehydrogenases/reductases are critical for reducing the reactive aldehyde all-trans-retinal that is released by photoactivated rhodopsin, to all-trans-retinol. Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12. RDH8 in the outer segment provides most of the activity needed to reduce all-trans-retinal generated by the light response, overview
physiological function
-
RDH1 contributes to a reconstituted pathway of all-trans-retinal biosynthesis, when expressed in intact cells with each of the three retinal dehydrogenases
physiological function
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Six hours after re-feeding, isoform Rdh1 expression decreases 80-90% in liver and brown adipose tissue, 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 Rdh1 mRNA 50% or greater in mouse liver
physiological function
the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
physiological function
the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 6 (SDR16C6 or RDHE2S) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L3R/L5R/R16Q/R19Q/R21Q
-
RDH1 mutant, deleting the positive charges from the C-terminal end of the leader, and inserting two arginine residues near the N-terminus of the signaling sequence causes 95% inversion from cytoplasmic to luminal, the mutant faces the lumen
additional information
additional information
-
mutants lacking amino-terminal 18 or 30 amino acids do not localize to endoplasmic reticulum but to mitochondria instead. Deletion mutant lacking 28 C-terminal amino acids localizes both to microsomal and mitochondrial fractions. Deletion of both 18 N-terminal and 28 C-terminal amino acids leeds to overwhelming detection in mitochondria. Fusion of N-terminal 22 amino acids of enzyme with green fluorescent protein localizes in endoplasmic reticulum. Fusion of N-terminal 18 amino acids of enzyme with green fluorescent protein shows diffuse localization. Fusion of green fluorescent protein with C-terminal 29 amino acids of enzyme shows diffuse cytoplasmic and nuclear localization.
additional information
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
-
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
-
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged RDH10 in Spodoptera frugiperda Sf9 insect cell membranes
-
recombinant expression of C-terminally His6-tagged enzyme in Spodoptera frugiperda Sf9 cell microsomes, mitochondria from RDHE2S-expressing Sf9 cells exhibit a much lower activity than RDHE2S microsomes under the same assay conditions. Transient recombinant expression of C-terminally FLAG-tagged enzyme in HEK-293 cells. Quantitative RT-PCR enzyme expression analysis
recombinant expression of C-terminally His6-tagged enzyme in Spodoptera frugiperda Sf9 cell microsomes, no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. Funtional transient recombinant expression of C-terminally FLAG-tagged enzyme in HEK-293 cells, the activity of RDHE2 resulted in a 3fold increase in RA biosynthesis relative to mock-transfected cells. Quantitative RT-PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oral gavage with glucose or injection with insulin decreases Rdh1 mRNA 50% or greater in mouse liver
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kishore, G.S.; Boutwell, R.K.
Enzymatic oxidation and reduction of retinal by mouse epidermis
Biochem. Biophys. Res. Commun.
94
1381-1386
1980
Mus musculus
Zhang, M.; Hu, P.; Napoli, J.L.
Elements in the N-terminal signaling sequence that determine cytosolic topology of short-chain dehydrogenases/reductases. Studies with retinol dehydrogenase type 1 and cis-retinol/androgen dehydrogenase type 1
J. Biol. Chem.
279
51482-51489
2004
Mus musculus
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
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 (O55240), Mus musculus
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
Zhang, M.
Chen, W.; Smith, S.M.; Napoli, J.L.: Molecular characterization of a mouse short chain dehydrogenase/reductase active with all-trans-retinol in intact cells, mRDH1
J. Biol. Chem.
276
44083-44090
2001
Mus musculus (Q8VIJ7), Mus musculus
Napoli, J.L.
Physiological insights into all-trans-retinoic acid biosynthesis
Biochim. Biophys. Acta
1821
152-167
2012
Homo sapiens, Mus musculus, Rattus norvegicus
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, Mus musculus C57BL/6 x 129/Sv
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
Wu, L.; Belyaeva, O.V.; Adams, M.K.; Klyuyeva, A.V.; Lee, S.A.; Goggans, K.R.; Kesterson, R.A.; Popov, K.M.; Kedishvili, N.Y.
Mice lacking the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands
J. Biol. Chem.
294
17060-17074
2019
Mus musculus (Q05A13), Mus musculus (Q7TQA3), Mus musculus, Mus musculus C57BL/6J (Q05A13), Mus musculus C57BL/6J (Q7TQA3)
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