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Information on EC 1.2.1.36 - retinal dehydrogenase and Organism(s) Rattus norvegicus and UniProt Accession Q8K4D8

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IUBMB Comments
A metalloflavoprotein (FAD). Acts on both the 11-trans- and 13-cis-forms of retinal.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q8K4D8
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
raldh2, retinaldehyde dehydrogenase, raldh3, retinal dehydrogenase, retinaldehyde dehydrogenase 2, retinaldehyde dehydrogenases, rdh13, retinal dehydrogenase 1, xctbp, retinaldehyde dehydrogenase-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
retinaldehyde dehydrogenase
-
retinaldehyde dehydrogenase 3
-
Aldh1a2
cytosolic retinal dehydrogenase
-
-
-
-
dehydrogenase, retinal
-
-
-
-
NAD-dependent retinal dehydrogenase
-
-
NAD-dependent retinal dehydrogenases
-
PB-RALDH
-
-
phenobarbital-induced aldehyde dehydrogenase
-
-
RALDH
RalDH1
RALDH2
Retinal dehydrogenase
-
-
retinal dehydrogenase 2
-
-
retinal dehydrogenase-2
-
-
retinaldehyde dehydrogenase
-
retinaldehyde dehydrogenase 1
-
retinaldehyde dehydrogenase 2
-
retinaldehyde dehydrogenase-2
-
-
retinaldehyde dehydrogenases
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
retinal + NAD+ + H2O = retinoate + NADH + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
PATHWAY SOURCE
PATHWAYS
-
-
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 hide
37250-99-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
retinal + NAD+ + H2O
retinoate + NADH + H+
show the reaction diagram
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + H+
show the reaction diagram
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
show the reaction diagram
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
show the reaction diagram
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
show the reaction diagram
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH
show the reaction diagram
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
citral + NAD+ + H2O
3,7-dimethyl-2,6-octadienoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
show the reaction diagram
-
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
show the reaction diagram
hexanal + NAD+ + H2O
hexanoate + NADH + 2 H+
show the reaction diagram
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
show the reaction diagram
octanal + NAD+ + H2O
octanoate + NADH
show the reaction diagram
propanal + NAD+ + H2O
propanoate + NADH + H+
show the reaction diagram
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
show the reaction diagram
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
show the reaction diagram
retinal + NAD+ + H2O
retinoate + NADH + H+
show the reaction diagram
retinol + NAD+ + H2O
? + NADH + H+
show the reaction diagram
-
-
-
-
?
retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
retinal + NAD+ + H2O
retinoate + NADH + H+
show the reaction diagram
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
show the reaction diagram
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH
show the reaction diagram
-
key enzyme in retinoic acid biosynthesis, essential in developing diaphragm, enzyme inhibition or disfunction causes the serious developmental anomaly congenital diaphragmatic hernia, i.e. CDH
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
show the reaction diagram
retinal + NAD+ + H2O
retinoate + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
metalloflavoprotein, reaction rate is maximal with FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
reaction rate is maximal with Fe2+
Iron
-
metalloprotein, approximately 2 mol of iron per mol of enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Iodoacetamide
-
slight
4-biphenyl carboxylic acid
-
90% inhibition at 0.1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
acetaldehyde
-
0.2 mM, 0.5 mM and 1.0 mM, uncompetitive inhibition
all-trans-retinal
-
9-cis-retinoic acid synthesis from 0.002 mM 9-cis-retinal is inhibited 50% by 0.005 mM all-trans-retinal
all-trans-retinol
-
competitive
alpha,alpha'-dipyridyl
-
slight
apo-CRBP
-
IC50 0.0014 mM
-
Atabrine
-
slight, FAD reverses inhibition
Chloral hydrate
-
noncompetitive inhibition
citral
-
IC50 about 0.001 mM
Disulfiram
-
20 mM
Mg2+
specific activity is reduced half in presence of Mg2+
N,N'-octamethylenebis (dichloroacetamide)
-
complete inhibition at very low concentration below 1 pM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
NADH
-
inhibits noncompetitively, inhibition not reversed by direct addition of NAD+
nitrofen
-
90% inhibition at 0.1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
p-chloromercuribenzoate
-
-
retinal
SB-210661
-
80% inhibition at 1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apoCRABP
-
stimulates retinoic acid synthesis by about 30-50%
-
CRBP
-
glutathione
-
reduced form, reaction rate is maximal, with reduced glutathione
additional information
-
spinal cord injury results in a significant rise in RALDH2 protein expression that is accounted for by an increase of this enzyme in meninges, blood vessels and a subpopulation of NG2-positive cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0063
2,4-decadienal
0.0087
9-cis-retinal
0.0017 - 0.01
all-trans-retinal
0.0003
benzaldehyde
-
-
0.0029
citral
0.0003 - 0.0064
decanal
0.0003 - 0.023
hexanal
0.022 - 0.2424
NAD+
0.0003
octanal
-
-
0.0066
propanal
-
-
0.0007 - 0.76
retinal
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
2,4-decadienal
0.1
all-trans-retinal
pH 8.5, 25°C, recombinant enzyme
0.1
citral
2.2
decanal
2
hexanal
0.1
retinal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
acetaldehyde
-
standard deviation 0.01 mM
0.0126
Chloral hydrate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
apo-CRBP
Rattus norvegicus
-
IC50 0.0014 mM
-
0.001
citral
Rattus norvegicus
-
IC50 about 0.001 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
about, assay at
7.7
-
in 0.1 M sodium phosphate buffer, rather broad pH curve with pH-otimum at approximately pH 7.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9
-
exhibits a broad pH optimum
8.4 - 8.6
-
on chromatofocusing column, major activity peak is eluted at pH range 8.4-8.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression of RALDH3 is located in Rathke's pouch at embryonic day 12.5 and subsequently in the developing anterior pituitary gland. Pituitary RALDH3 mRNA levels are high at E17.5 and decrease markedly after birth
Manually annotated by BRENDA team
-
endocrine islets of Langerhans
Manually annotated by BRENDA team
-
epididymis capa, epididymis cauda
Manually annotated by BRENDA team
-
pancreas exocrine acini
Manually annotated by BRENDA team
ALDH1A1 protein exhibits diffuse staining in hepatocytes, with greater intensity in the periportal region including surrounding bile ducts
Manually annotated by BRENDA team
-
cell culture
Manually annotated by BRENDA team
-
submaxillary gland
Manually annotated by BRENDA team
-
in the uninjured spinal cord low levels of RALDH2 are present in oligodendrocytes as well as in the meninges and in blood vessels
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoform Raldh1
Manually annotated by BRENDA team
-
isoform Raldh2
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme is a member of the ALDH1 protein family
malfunction
acute inflammation rapidly downregulates ALDH1A1 expression in whole liver while increasing its expression in periportal macrophages
metabolism
-
both isoforms Raldh1 and -2 contribute to atRA biosynthesis in hippocampus astrocytes
physiological function
changes in ALDH1A1 expression appear to be part of the early acute-phase inflammatory response, which alters the expression of other retinoid homeostatic genes
additional information
high-fat diet significantly decreases basal retinal levels in liver to 44% of control rats. Enhanced activity and expression of RALDHs in liver of high-fat diet rats
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AL1A3_RAT
512
0
56171
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
standard deviation 3500, gel filtration
214000
-
gel filtration
53000
-
3 * 53000, SDS-PAGE
55000
80000
-
thin layer chromatography, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
trimer
-
3 * 53000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no glycoprotein
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of recombinant chimeric enzymes exchanging parts of the enzyme by sequences of the phenobarbital-induced aldehyde dehydrogenase from rat, and vice versa, the chimeric enzymes show altered substrate specificity towards 9-cis- or all-trans-retinal, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against distilled water, several hours, about 29% loss of activity
-
quite unstable during extensive freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 20 mM Hepes, 2 mM DTT, 150 mM KCl, 15% glycerol, pH 8
-
-70°C, at concentration of 0.078 mg/ml, 15% glycerol, stable for three months
-
dilution (1:5) with 100 mM phosphate buffer often results in loss of 80-90% of specific activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
after recombinant production in Escherichia coli BL-21DE3
-
nickel-Sepharose column chromatography and Q-Sepharose column chromatography
-
partially by isoelectric focusing
-
recombinant N-terminally His-tagged enzyme from Escherichia coli strain C41(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the pGEM-T easy vector, 396-1002
expressed in Escherichia coli C41(DE3) cells
-
expression in Escherichia coli
-
functional expression of wild-type and chimeric mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene Aldh1a1, quantitative reverse transcription PCR enzyme expression analysis
gene ALDH1A2, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain C41(DE3)
into the pGEM-T easy vector, bp 1488-2079
into the pGEM-T easy vector, bp 935-1485
recombinant in Escherichia coli BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
acute inflammation rapidly increases the enzyme expression in periportal macrophages
enhanced activity and expression of RALDHs in liver of high-fat diet rats. High-fat diet feeding significantly up-regulates cytosolic RALDHs activity, 1.7fold and 2fold in the presence of NAD+ and NADP+, respectively
inflammation reduces ALDH1A1 mRNA in whole liver regardless of the level of vitamin A in the diet, while treatment with retinal reduces ALDH1A1 expression only in chow-fed rats. Acute inflammation rapidly downregulates ALDH1A1 expression in whole liver
levels of RALDH1 gene expression and protein production markedly decrease after 1-week treatment with 17beta-estradiol in male rats. Treatment of isolated anterior pituitary cells with 17beta-estradiol (0.00001-10 nM) decreases expression of RALDH1 mRNA in a dose-dependent manner (about 55% RALDH1 mRNA level remaining 6 h after treatment with 10 nM 17beta-estradiol). 17beta-Estradiol-induced suppression of RALDH1 expression is completely blocked by the estrogen receptor antagonist ICI 182, 780. The ERalpha-selective agonist propylpyrazole triol (10 nM) mimicks the effect of 17beta-estradiol on RALDH1 expression, but the ERbeta-selective agonist diarylpropionitrile (10 nM) does not
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
ALDH1A1 is rapidly gaining importance as a stem cell marker
molecular biology
ALDH1A1 is rapidly gaining importance as a stem cell marker
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Moffa, D.J.; Lotspeich, F.J.; Krause, R.F.
Preparation and properties of retinal-oxidizing enzyme from rat intestinal mucosa
J. Biol. Chem.
245
439-447
1970
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Leo, M.A.; Kim, C.I.; Lowe, N.; Lieber, C.S.
Increased hepatic retinal dehydrogenase activity after phenobarbital and ethanol administration
Biochem. Pharmacol.
38
97-103
1989
Peromyscus maniculatus, Rattus norvegicus, Rattus norvegicus BR
Manually annotated by BRENDA team
el Akawi, Z.; Napoli, J.L.
Rat liver cytosolic retinal dehydrogenase: comparison of 13-cis-, 9-cis-, and all-trans-retinal as substrates and effects of cellular retinoid-binding proteins and retinoic acid on activity
Biochemistry
33
1938-1943
1994
Rattus norvegicus, Rattus norvegicus BR
Manually annotated by BRENDA team
Bhat, P.V.; Samaha, H.
Kinetic properties of the human liver cytosolic aldehyde dehydrogenase for retinal isomers
Biochem. Pharmacol.
57
195-197
1999
Rattus norvegicus
Manually annotated by BRENDA team
Lamb, A.L.; Wang, X.; Napoli, J.L.; Newcomer, M.E.
Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II
Acta Crystallogr. Sect. D
54
639-642
1998
Rattus norvegicus
Manually annotated by BRENDA team
Bhat, P.V.; Marcinkiewicz, M.; Li, Y.; Mader, S.
Changing patterns of renal retinal dehydrogenase expression parallel nephron development in the rat
J. Histochem. Cytochem.
46
1025-1032
1998
Rattus norvegicus, Rattus norvegicus BR
Manually annotated by BRENDA team
Penzes, P.; Wang, X.; Napoli, J.L.
Enzymic characteristics of retinal dehydrogenase type I expressed in Escherichia coli
Biochim. Biophys. Acta
1342
175-181
1997
Rattus norvegicus
Manually annotated by BRENDA team
Labrecque, J.; Bhat, P.V.; Lacroix, A.
Purification and partial characterization of a rat kidney aldehyde dehydrogenase that oxidizes retinal to retinoic acid
Biochem. Cell Biol.
71
85-89
1993
Rattus norvegicus
Manually annotated by BRENDA team
Lamb, A.L.; Newcomer, M.E.
The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity
Biochemistry
38
6003-6011
1999
Rattus norvegicus (Q63639)
Manually annotated by BRENDA team
Wang, X.; Penzes, P.; Napoli, J.L.
Cloning of a cDNA encoding an aldehyde dehydrogenase and its expression in Escherichia coli. Recognition of retinal as substrate
J. Biol. Chem.
271
16288-16293
1996
Rattus norvegicus (Q63639)
Manually annotated by BRENDA team
Zhao, D.; McCaffery, P.; Ivins, K.J.; Neve, R.L.; Hogan, P.; Chin, W.W.; Drager, U.C.
Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase
Eur. J. Biochem.
240
15-22
1996
Rattus norvegicus
Manually annotated by BRENDA team
Posch, K.C.; Burns, R.D; Napoli, J.L.
Biosynthesis of all-trans-retinoic acid from retinal. Recognition of retinal bound to cellular retinol binding protein (type I) as substrate by a purified cytosolic dehydrogenase
J. Biol. Chem.
267
19676-19682
1992
Rattus norvegicus
Manually annotated by BRENDA team
Mey, J.; Babiuk, R.P.; Clugston, R.; Zhang, W.; Greer, J.J.
Retinal dehydrogenase-2 is inhibited by compounds that induce congenital diaphragmatic hernias in rodents
Am. J. Pathol.
162
673-679
2003
Rattus norvegicus
Manually annotated by BRENDA team
Montplaisir, V.; Lan, N.C.; Guimond, J.; Savineau, C.; Bhat, P.V.; Mader, S.
Recombinant class I aldehyde dehydrogenases specific for all-trans- or 9-cis-retinal
J. Biol. Chem.
277
17486-17492
2002
Rattus norvegicus
Manually annotated by BRENDA team
Everts, H.B.; Sundberg, J.P.; Ong, D.E.
Immunolocalization of retinoic acid biosynthesis systems in selected sites in rat
Exp. Cell Res.
308
309-319
2005
Rattus norvegicus
Manually annotated by BRENDA team
Fujiwara, K.; Maekawa, F.; Kikuchi, M.; Takigami, S.; Yada, T.; Yashiro, T.
Expression of retinaldehyde dehydrogenase (RALDH)2 and RALDH3 but not RALDH1 in the developing anterior pituitary glands of rats
Cell Tissue Res.
328
129-135
2006
Rattus norvegicus (P51647), Rattus norvegicus (Q63639), Rattus norvegicus (Q8K4D8)
Manually annotated by BRENDA team
Fujiwara, K.; Kikuchi, M.; Takigami, S.; Kouki, T.; Yashiro, T.
Expression of retinaldehyde dehydrogenase 1 in the anterior pituitary glands of adult rats
Cell Tissue Res.
329
321-327
2007
Rattus norvegicus (P51647)
Manually annotated by BRENDA team
Kern, J.; Schrage, K.; Koopmans, G.C.; Joosten, E.A.; McCaffery, P.; Mey, J.
Characterization of retinaldehyde dehydrogenase-2 induction in NG2-positive glia after spinal cord contusion injury
Int. J. Dev. Neurosci.
25
7-16
2007
Rattus norvegicus
Manually annotated by BRENDA team
Ahrendt, M.; Hammerschmidt, S.I.; Pabst, O.; Pabst, R.; Bode, U.
Stromal cells confer lymph node-specific properties by shaping a unique microenvironment influencing local immune responses
J. Immunol.
181
1898-1907
2008
Rattus norvegicus
Manually annotated by BRENDA team
Fujiwara, K.; Kikuchi, M.; Horiguchi, K.; Kusumoto, K.; Kouki, T.; Kawanishi, K.; Yashiro, T.
Estrogen receptor alpha regulates retinaldehyde dehydrogenase 1 expression in rat anterior pituitary cells
Endocr. J.
56
963-973
2009
Rattus norvegicus (P51647)
Manually annotated by BRENDA team
Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.
Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition
Chem. Biol. Interact.
202
78-84
2013
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Wang, C.; Kane, M.A.; Napoli, J.L.
Multiple retinol and retinal dehydrogenases catalyze all-trans-retinoic acid biosynthesis in astrocytes
J. Biol. Chem.
286
6542-6553
2011
Rattus norvegicus
Manually annotated by BRENDA team
Bchini, R.; Vasiliou, V.; Branlant, G.; Talfournier, F.; Rahuel-Clermont, S.
Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition
Chem. Biol. Interact.
202
78-84
2013
Homo sapiens (P00352), Homo sapiens, Rattus norvegicus (Q63639)
Manually annotated by BRENDA team
Zhang, M.; Liu, C.; Hu, M.Y.; Zhang, J.; Xu, P.; Li, F.; Zhong, Z.Y.; Liu, L.; Liu, X.D.
High-fat diet enhanced retinal dehydrogenase activity, but suppressed retinol dehydrogenase activity in liver of rats
J. Pharmacol. Sci.
127
430-438
2015
Rattus norvegicus (P51647), Rattus norvegicus Sprague-Dawley (P51647)
Manually annotated by BRENDA team
Ito, K.; Zolfaghari, R.; Hao, L.; Ross, A.C.
Inflammation rapidly modulates the expression of ALDH1A1 (RALDH1) and vimentin in the liver and hepatic macrophages of rats in vivo
Nutr. Metab.
11
54
2014
Rattus norvegicus (P51647)
Manually annotated by BRENDA team