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Information on EC 1.2.1.36 - retinal dehydrogenase and Organism(s) Mus musculus and UniProt Accession P24549
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1.2.1.36 retinal dehydrogenaseIUBMB Comments
A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.
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Word Map
- 1.2.1.36
-
retinoic
- raldhs
- mesoderm
- dendritic
-
all-trans
- aldh1a2
-
ventral
-
ra-synthesizing
-
all-trans-retinoic
-
cyp26s
- hindbrain
-
retinol-binding
- somite
-
anterior-posterior
-
gut-homing
-
otic
-
crabps
-
ra-dependent
-
ra-responsive
- molecular biology
-
somitogenesis
- all-trans-retinal
-
rhombomere
- synthesis
-
acid-synthesizing
- diagnostics
-
dorsoventral
-
epicardium
- degradation
- citral
-
anteroposterior
-
paraxial
-
ra-mediated
-
rarbeta
-
retinyl
-
retinoid-dependent
- medicine
-
foxp3+
-
raralpha
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
Synonyms
raldh2, raldh3, retinaldehyde dehydrogenase, retinal dehydrogenase, retinaldehyde dehydrogenase 2, retinaldehyde dehydrogenases, rdh13, retinal dehydrogenase 1, xctbp, retinaldehyde dehydrogenase-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aldh1a2
cytosolic retinal dehydrogenase
-
-
-
-
dehydrogenase, retinal
-
-
-
-
RalDH1
RALDH2
RALDH3
Raldh4
Retinal dehydrogenase
retinal dehydrogenase 2
retinal dehydrogenase 3
retinaldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
retinal + NAD+ + H2O = retinoate + NADH + 2 H+
sulfhydryl group involved in activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
redox reaction
-
-
-
-
oxidation
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
retinal:NAD+ oxidoreductase
A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.
CAS REGISTRY NUMBER
COMMENTARY
37250-99-0
-
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
all-trans retinaldehyde + NAD+ + H2O
all-trans retinoic acid + NADH + H+
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans-retinoate + NADH + H+
RALDH3 oxidizes all-trans retinal with high catalytic efficiency
-
-
?
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH
-
type-2 isozyme, 2fold lower activity compared to all-trans-retinal
-
-
?
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH + H+
isoform RALDH4 oxidizes 13-cis retinal with lower catalytic efficiency than 9-cis retinal
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
step in biosynthesis of vitamin A, transduction by nuclear retinoid receptors, required for ontogenesis and homeostasis of numerous tissues
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
type-2 isozyme, 5fold lower activity compared to all-trans-retinal
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH + H+
isoform RALDH4 catalyzes 9-cis retinal oxidation with 3fold higher efficiency than 13-cis retinal
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
second step in retinol clearance in adult mice, null mutants show retinol clearance reduced by 7%, and a lower LD50 concentration for all-trans-retinol compared to the wild-type mice
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
step in biosynthesis of vitamin A, transduction by nuclear retinoid receptors, required for ontogenesis and homeostasis of numerous tissues
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
type-2 isozyme
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
preferred substrate of recombinant isozyme type-1
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
preferred substrate, type-2 isozyme
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
efficiency of conversion of all-trans-retinal to retinoic acid is 2fold and 5fold higher than 13-cis and 9-cis-retinal, respectively
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
a null mutation of RALDH2 is embryonic lethal, eliminating most mesodermal synthesis of retinoic acid. Loss of RALDH1 eliminates synthesis od retinoic acid only in the embryonic dorsal retina with no obvious effect on development
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
conversion from retinal catalyzed by retinal dehydrogenase on a polyvinylidene difluoride membrane can be directly observed using laser desorption ionization time of flight mass spectrometry (LDI-TOF MS) after separation and blotting onto the membrane under non-denaturing conditions
-
-
?
additional information
?
-
-
enzyme is involved in retinoic acids biosynthesis, which are important signaling molecules in embryogenesis and tissue differentiation
-
-
?
additional information
?
-
-
physiological function, newborn lethal defect due to isozyme type-3 inactivation is prevented by maternal retinoic acid treatment, overview
-
-
?
additional information
?
-
-
type-2 isozyme catalyzes the last step in biosynthesis of retinoic acid in embryos and adult reproductive organs, isozyme type-2 regulates the retinoic acid level during embryogenesis and tissue differentiation
-
-
?
additional information
?
-
-
substrate specificities at different substrate concentrations, no activity with 13-cis-retinal
-
-
?
additional information
?
-
-
substrate specificities of wild-type isozyme type-2 and mutant L459F/N460G
-
-
?
additional information
?
-
-
show no activity with either 9-cis or 13-cis retinal
-
-
?
additional information
?
-
show no activity with either 9-cis or 13-cis retinal
-
-
?
additional information
?
-
-
isoform RALDH3 does not show activity for either 9-cis or 13-cis retinal substrates, isoform RALDH4 is inactive for all-trans retinal substrate
-
-
?
additional information
?
-
isoform RALDH3 does not show activity for either 9-cis or 13-cis retinal substrates, isoform RALDH4 is inactive for all-trans retinal substrate
-
-
?
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
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
step in biosynthesis of vitamin A, transduction by nuclear retinoid receptors, required for ontogenesis and homeostasis of numerous tissues
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
second step in retinol clearance in adult mice, null mutants show retinol clearance reduced by 7%, and a lower LD50 concentration for all-trans-retinol compared to the wild-type mice
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
step in biosynthesis of vitamin A, transduction by nuclear retinoid receptors, required for ontogenesis and homeostasis of numerous tissues
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
type-2 isozyme
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
a null mutation of RALDH2 is embryonic lethal, eliminating most mesodermal synthesis of retinoic acid. Loss of RALDH1 eliminates synthesis od retinoic acid only in the embryonic dorsal retina with no obvious effect on development
-
-
?
additional information
?
-
-
enzyme is involved in retinoic acids biosynthesis, which are important signaling molecules in embryogenesis and tissue differentiation
-
-
?
additional information
?
-
-
physiological function, newborn lethal defect due to isozyme type-3 inactivation is prevented by maternal retinoic acid treatment, overview
-
-
?
additional information
?
-
-
type-2 isozyme catalyzes the last step in biosynthesis of retinoic acid in embryos and adult reproductive organs, isozyme type-2 regulates the retinoic acid level during embryogenesis and tissue differentiation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
activity is slightly activated by magnesium at higher concentrations
Mg2+
magnesium dramatically activated 13-cis retinal oxidation without significantly affecting 9-cis retinal oxidation
Mg2+
Mg2+ activates 13-cis retinal oxidation by isoform RALDH4 by 3fold, does not significantly influence 9-cis retinal oxidation, and slightly activates isoform RALDH3 activity, owever, magnesium at lower concentration has no effect on RALDH4 activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
estrogen
downregulates Raldh1 expression in the uterine glandular epithelium
acetaldehyde
-
60% competitive inhibition of all-trans-retinal oxidation at 0.4 mM
Chloral hydrate
-
80% competitive inhibition of all-trans-retinal oxidation at 0.1 mM
pravastatin sodium
-
cholesterol-lowering agent downregulates the expression of RALDH1,2 genes
retinol
-
40% uncompetitive inhibition of all-trans-retinal oxidation at 0.012 mM
beta-ionone
potent inhibitor of isoform RALDH4 activity, at 0.002 mM concentration 9-cis and 13-cis retinal oxidation is reduced by 53% and 63%, respectively
Mg2+
-
about 50% inhibition of all-trans- and 9-cis-retinal oxidation above 1 mM
p-hydroxymercuribenzoate
-
strongly suppress enzyme reaction, reversed by addition of DTT
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM in absence of DTT, 2 mM DTT protect nearly completely
additional information
-
all-trans-retinol and chloral hydrate do not inhibit enzyme reaction
-
additional information
beta-ionone has no effect on isoform RALDH3 activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
upregulated in response to allergic stimulation in the airway epithelium
-
additional information
-
22(R)-hydroxy cholesterol elevates significantly the RALDH2 mRNA level in H2.35 cells
-
additional information
-
oxysterols, cholesterol metabolites, induce the RALDH1 gene via upregulation of sterol regulatory element binding protein-1c, SREBP-1c
-
additional information
-
oxysterols, cholesterol metabolites, induce the RALDH2 gene via upregulation of sterol regulatory element binding protein-1c, SREBP-1c
-
additional information
-
an oil-in-water nanoemulsion adjuvant activates the enzyme via MyD88 dependent pathways in dendritic cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic analysis, isozyme type-2
-
0.0034
13-cis retinal
isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C
0.003
9-cis retinal
isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C
0.0039
all-trans retinal
isoform RALDH3, in 10 mM Tris-HCl buffer, pH 8.5, at 37°C
0.001
decanal
-
recombinant wild-type enzyme and mutant L459F/N460G, pH 8.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.049
acetaldehyde
-
recombinant isozyme type-1, pH 7.5, 25°C, with substrate all-trans-retinal
0.005
Chloral hydrate
-
recombinant isozyme type-1, pH 7.5, 25°C, with substrate all-trans-retinal
additional information
additional information
-
kinetics, recombinant isozyme type-1
-
0.00032
beta-ionone
isoform RALDH4, using 13-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C
0.00061
beta-ionone
isoform RALDH4, using 9-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
-
recombinant isozyme type-1 exhibits 2 pH-optima at pH 7.8 and pH 9.4 with substrates all-trans-retinal and 9-cis-retinal, respectively
8.5
9.4
-
recombinant isozyme type-1 exhibits 2 pH-optima at pH 7.8 and pH 9.4 with substrates all-trans-retinal and 9-cis-retinal, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
25
-
all retinal isomer substrates are converted to respective retinoic acids more efficiently compared to 37°C, might be due to instability of substrates at 37°C
25
-
assay at, recombinant isozyme type-2, probably higher activity than at 37°C due to higher stability of the substrates at 25°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform RALDH1 is dominantly expressed in intestinal epithelial cells
additional information
-
at 9.5 and 10.5 days of embryonic development the enzyme activity is restricted to tissues of the embryonic trunk and absent in extracts from cranial tissues
additional information
-
specific expression in embryos and adult reproductive organs
additional information
-
no activity is detectable in brain, thymus, spleen, kidneys, skeletal muscle and heart
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
ablation of retinoic acid signaling in host dencritic cells by deletion of isoform RALDH2 protects mice from acute graft-versus-host disease. Isoform RALDH1 deletion fails to reduce acute graft-versus-host disease
metabolism
-
retinaldehyde dehydrogenase 1 induction impairs glucose metabolism partly via modulating phosphoenolpyruvate carboxykinase 1 and glucokinase expressions
physiological function
additional information
physiological function
retinoic acid-producing dendritic cells play critical roles in gut immunity. Retinal dehydrogenase 2 (RALDH2) encoded by Aldh1a2 is a key enzyme for generating retinoic acid in dendritic cells
physiological function
-
isoform RALDH2 expression in dendritic cells is critical to control acute graft-versus-host disease lethality
additional information
MAPK activation is required for GM-CSF-induced Aldh1a2 expression and Sp1 nuclear translocation. Sp1 participates in the Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region
additional information
-
MAPK activation is required for GM-CSF-induced Aldh1a2 expression and Sp1 nuclear translocation. Sp1 participates in the Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region
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). AL1A1_MOUSE
501
0
54468
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme type-2 mutant L459F/N460G in complex with NAD+ and in absence of substrate, hanging drop vapour diffusion method, 7.6 mg/ml enzyme with 2 mM NAD+ and about 14 mg/ml retinol, 0.002 ml protein solution plus equal volume of well solution containing 7% PEG 6000, 2% 2-methyl-2,4-pentanediol, and 0.1 M Tris, pH 7.5, X-ray diffraction structure determination and analysis at 3.3 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C301A
-
site-directed mutagenesis, catalytic residue mutation, reduced activity compared to the wild-type enzyme
L459F/N460G
-
site-directed mutagenesis, inactive mutant, still able to bind the cofactor NAD+
additional information
additional information
-
construction of isozyme type-3 knock-out mice with suppressed retinoic acid biosynthesis, showing malformations restricted to ocular and nasal regions and choanal atresia, i.e. CA, leading to respiratory distress and death of mutant mice after birth, overview
additional information
-
Raldh1-/- null mutant mice show retinol clearance reduced by 7%, mutant mice are viable and fertile, and show no obvious defects, overview
additional information
-
3-deoxyglucosone dehydrogenase activity is undetectable in tissues from ALDH1A1-/- mice
additional information
-
Rdh12-/- mice are viable, develop normally, and can not be distinguished from heterozygous or wild-type littermates by mere observation. Rdh12 knockout mice exhibit grossly normal retinal histology at 10 months of age. Lipid peroxidation products and other measures of oxidative stress are not elevated in Rdh12-/- animals. Rdh12-/- and wild-type mice show approximately equivalent expression of the visual cycle genes Rdh5, Rpe65, Lrat, Cralbp, Crbp, Irbp, Rho, and Abcr. There is also no change in the expression of other Rdh isoforms expressed in photoreceptors, including Rdh8 (prRdh), Rdh11, Rdh13, Rdh14, and retSDR1
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozyme type-1 as fusion protein from Escherichia coli by GST-affinity chromatography, cleavage by thrombin to eliminate the fusion tag
-
recombinant isozyme type-2 as fusion protein from Escherichia coli by GST-affinity chromatography, cleavage by thrombin to eliminate the fusion tag
-
recombinant wild-type and mutant isozyme type-2 from Escherichia coli strain Bl21(DE3), no usage of His-tag since it may influence the enzyme activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of isozyme type-1 in Escherichia coli strain BL21(DE3) as N-terminally fusion protein to glutathione-S-transferase
-
expression of isozyme type-2 in Escherichia coli strain BL21(DE3) as N-terminally fusion protein to glutathione-S-transferase
-
gene Aldh1a2, comprises 14 exons that are divided by 13 introns spanning more than 50 kb of genomic DNA, and it is localized on chromosome 9. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation
into the cloning vector pGEM-T Easy and subcloned into the expression vector pET14b
overexpression of wild-type and mutant isozyme type-2 in Escherichia coli strain Bl21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ERK and p38 MAPK inhibitors PD98059 and SB203580 suppress GM-CSF-induced nuclear translocation of Sp1 and Aldh1a2 expression. CpG methylation in the Aldh1a2 promoter region inhibits Sp1-dependent Aldh1a2 promoter activation. Aldh1a2 transcription silencing by CpG methylation of the promoter region is not due to direct interference with Sp1 binding to the promoter region
granulocyte-macrophage colony-stimulating factor (GMCSF) potently induces RALDH2 expression in dendritic cells in an retinoic acid-dependent manner, and retinoic acid alone weakly induces the expression. Retinoic acid and GM-CSF coordinately induce retinal dehydrogenase 2 (RALDH2) expression through cooperation between the RAR/RXR complex and Sp1 in dendritic cells
high retinoic acid levels inhibit Raldh1 gene expression by sequestering CCAAT/enhancer binding protein beta through its interaction to GADD153. A decrease in Raldh1 mRNA levels in the aryl hydrocarbon receptor-null liver relative to wild type mouse liver is observed
-
obesity and insulin resistance are associated with overexpression of retinaldehyde dehydrogenase 1. High-fat-diet-feeding significantly induces the activity and expression of RALDH1 protein
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
ALDH1A1 appears to be the major if not the only enzyme responsible for the oxidation of 3-deoxyglucosone to 2-keto-3-deoxygluconate
medicine
-
activity of any one isoform is not rate limiting in the visual response
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gagnon, I.; Duester, G.; Bhat, P.V.
Kinetic analysis of mouse retinal dehydrogenase type-2 (RALDH2) for retinal substrates
Biochim. Biophys. Acta
1596
156-162
2002
Mus musculus
Gagnon, I.; Duester, G.; Bhat, P.V.
Enzymatic characterization of recombinant mouse retinal dehydrogenase type 1
Biochem. Pharmacol.
65
1685-1690
2003
Mus musculus
Duester, G.; Mic, F.A.; Molotkov, A.
Cytosolic retinoid dehydrogenases govern ubiquitous metabolism of retinol to retinaldehyde followed by tissue-specific metabolism to retinoic acid
Chem. Biol. Interact.
143-144
201-210
2003
Mus musculus
Maly, I.P.; Crotet, V.; Toranelli, M.
The so-called "testis-specific aldehyde dehydrogenase" corresponds to type 2 retinaldehyde dehydrogenase in the mouse
Histochem. Cell Biol.
119
169-174
2003
Mus musculus
Molotkov, A.; Duester, G.
Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1) functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol to retinoic acid
J. Biol. Chem.
278
36085-36090
2003
Mus musculus
Bordelon, T.; Montegudo, S.K.; Pakhomova, S.; Oldham, M.L.; Newcomer, M.E.
A disorder to order transition accompanies catalysis in retinaldehyde dehydrogenase type II
J. Biol. Chem.
279
43085-43091
2004
Mus musculus
Dupe, V.; Matt, N.; Garnier, J.M.; Chambon, P.; Mark, M.; Ghyselinck, N.B.
A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment
Proc. Natl. Acad. Sci. USA
100
14036-14041
2003
Mus musculus
Graham, C.E.; Brocklehurst, K.; Pickersgill, R.W.; Warren, M.J.
Characterization of retinaldehyde dehydrogenase 3
Biochem. J.
394
67-75
2006
Mus musculus (Q9JHW9)
Molotkov, A.; Molotkova, N.; Duester, G.
Retinoic acid generated by Raldh2 in mesoderm is required for mouse dorsal endodermal pancreas development
Dev. Dyn.
232
950-957
2005
Mus musculus (Q62148), Mus musculus
Vermot, J.; Schuhbaur, B.; Le Mouellic, H.; McCaffery, P.; Garnier, J.M.; Hentsch, D.; Brulet, P.; Niederreither, K.; Chambon, P.; Dolle, P.; Le Roux, I.
Retinaldehyde dehydrogenase 2 and Hoxc8 are required in the murine brachial spinal cord for the specification of Lim1+ motoneurons and the correct distribution of Islet1+ motoneurons
Development
132
1611-1621
2005
Mus musculus (Q62148), Mus musculus
Ribes, V.; Wang, Z.; Dolle, P.; Niederreither, K.
Retinaldehyde dehydrogenase 2 (RALDH2)-mediated retinoic acid synthesis regulates early mouse embryonic forebrain development by controlling FGF and sonic hedgehog signaling
Development
133
351-361
2006
Mus musculus (Q62148), Mus musculus
Vermot, J.; Messaddeq, N.; Niederreither, K.; Dierich, A.; Dolle, P.
Rescue of morphogenetic defects and of retinoic acid signaling in retinaldehyde dehydrogenase 2 (Raldh2) mouse mutants by chimerism with wild-type cells
Differentiation
74
661-668
2006
Mus musculus (P24549), Mus musculus
Huq, M.D.; Tsai, N.P.; Gupta, P.; Wei, L.N.
Regulation of retinal dehydrogenases and retinoic acid synthesis by cholesterol metabolites
EMBO J.
25
3203-3213
2006
Mus musculus
Ruehl, R.; Fritzsche, B.; Vermot, J.; Niederreither, K.; Neumann, U.; Schmidt, A.; Schweigert, F.J.; Dolle, P.
Regulation of expression of the retinoic acid-synthesising enzymes retinaldehyde dehydrogenases in the uteri of ovariectomised mice after treatment with oestrogen, gestagen and their combination
Reprod. Fertil. Dev.
18
339-345
2006
Mus musculus (P24549), Mus musculus (Q62148), Mus musculus
Alnouti, Y.; Klaassen, C.D.
Tissue distribution, ontogeny, and regulation of aldehyde dehydrogenase (Aldh) enzymes mRNA by prototypical microsomal enzyme inducers in mice
Toxicol. Sci.
101
51-64
2008
Mus musculus (Q62148)
Collard, F.; Vertommen, D.; Fortpied, J.; Duester, G.; Van Schaftingen, E.
Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase 1A1 (retinaldehyde dehydrogenase 1)
Biochimie
89
369-373
2007
Homo sapiens, Mus musculus
Shimazaki, Y.; Kuroda, T.
Direct analysis of retinal dehydrogenase activity on an electroblotting membrane following separation by non-denaturing two-dimensional electrophoresis
J. Chromatogr. B
860
180-184
2007
Mus musculus
Kurth, I.; Thompson, D.A.; Ruether, K.; Feathers, K.L.; Chrispell, J.D.; Schroth, J.; McHenry, C.L.; Schweizer, M.; Skosyrski, S.; Gal, A.; Huebner, C.A.
Targeted disruption of the murine retinal dehydrogenase gene Rdh12 does not limit visual cycle function
Mol. Cell. Biol.
27
1370-1379
2007
Homo sapiens, Mus musculus
Sima, A.; Parisotto, M.; Mader, S.; Bhat, P.V.
Kinetic characterization of recombinant mouse retinal dehydrogenase types 3 and 4 for retinal substrates
Biochim. Biophys. Acta
1790
1660-1664
2009
Mus musculus, Mus musculus (Q9JHW9)
Huang, J.; Bi, Y.; Zhu, G.H.; He, Y.; Su, Y.; He, B.C.; Wang, Y.; Kang, Q.; Chen, L.; Zuo, G.W.; Luo, Q.; Shi, Q.; Zhang, B.Q.; Huang, A.; Zhou, L.; Feng, T.; Luu, H.H.; Haydon, R.C.; He, T.C.; Tang, N.
Retinoic acid signalling induces the differentiation of mouse fetal liver-derived hepatic progenitor cells
Liver Int.
29
1569-1581
2009
Mus musculus
Goswami, S.; Angkasekwinai, P.; Shan, M.; Greenlee, K.J.; Barranco, W.T.; Polikepahad, S.; Seryshev, A.; Song, L.Z.; Redding, D.; Singh, B.; Sur, S.; Woodruff, P.; Dong, C.; Corry, D.B.; Kheradmand, F.
Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma
Nat. Immunol.
10
496-503
2009
Mus musculus (P24549)
Elizondo, G.; Medina-Diaz, I.M.; Cruz, R.; Gonzalez, F.J.; Vega, L.
Retinoic acid modulates retinaldehyde dehydrogenase 1 gene expression through the induction of GADD153-C/EBPbeta interaction
Biochem. Pharmacol.
77
248-257
2009
Mus musculus
Ohoka, Y.; Yokota-Nakatsuma, A.; Maeda, N.; Takeuchi, H.; Iwata, M.
Retinoic acid and GM-CSF coordinately induce retinal dehydrogenase 2 (RALDH2) expression through cooperation between the RAR/RXR complex and Sp1 in dendritic cells
PLoS ONE
9
e96512
2014
Mus musculus (Q62148), Mus musculus, Mus musculus B10.D2 mice and C57BL/6 mice (Q62148)
Xu, J.; Zhang, M.; Zhang, X.; Yang, H.; Sun, B.; Wang, Z.; Zhou, Y.; Wang, S.; Liu, X.; Liu, L.
Contribution of hepatic retinaldehyde dehydrogenase induction to impairment of glucose metabolism by high-fat-diet feeding in C57BL/6J mice
Basic Clin. Pharmacol. Toxicol.
123
539-548
2018
Mus musculus
Farazuddin, M.; Goel, R.R.; Kline, N.J.; Landers, J.J.; O'Konek, J.J.; Baker, J.R.
Nanoemulsion adjuvant augments retinaldehyde dehydrogenase activity in dendritic cells via MyD88 pathway
Front. Immunol.
10
916
2019
Mus musculus
Thangavelu, G.; Lee, Y.C.; Loschi, M.; Schaechter, K.M.; Feser, C.J.; Koehn, B.H.; Nowak, E.C.; Zeiser, R.; Serody, J.S.; Murphy, W.J.; Munn, D.H.; Chambon, P.; Noelle, R.J.; Blazar, B.R.
Dendritic cell expression of retinal aldehyde dehydrogenase-2 controls graft-versus-host disease lethality
J. Immunol.
202
2795-2805
2019
Mus musculus
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