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retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + 2 H+
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + H+
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH + H+
-
-
-
-
?
citral + NAD+ + H2O
3,7-dimethyl-2,6-octadienoate + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
-
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
hexanal + NAD+ + H2O
hexanoate + NADH + 2 H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
octanal + NAD+ + H2O
octanoate + NADH
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
retinal + NAD+ + H2O
retinoate + NADH + H+
retinol + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
-
?
additional information
?
-
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
poortly active with
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acetaldehyde is not a substrate
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
no substrate inhibition
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH
-
-
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH
-
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
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
enzyme also accounts for about 90% of the 9-cis-retinal dehydrogenase activity
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
acts on both the all-trans- and 13-cis-form of retinal, all-trans retinal more actively oxidized than 13-cis retinal
-
ir
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
additional information
?
-
-
does not catalyze 13-cis-retinal oxidation
-
-
?
additional information
?
-
-
13-cis-retinal is not an efficient substrate, isomerisation of 13-cis-retinal into all-trans-retinal provides substrate for all-trans retinoic acid synthesis
-
-
?
additional information
?
-
molecular basis of retinal recognition,comparison of enzyme from Rattus and human, overview. In contrast to long chain unsaturated substrates, the rate-limiting step of retinal oxidation by RALDHs is associated with acylation. Retinal recognition occurs in two steps: binding into the substrate access channel, and a slower structural reorganization with a rate constant of the same magnitude. The conformational transition of the RALDH-retinal complex significantly contributes to the rate-limiting step that controls the kinetics of retinal oxidation, as a prerequisite for the formation of a catalytically competent Michaelis complex. The conclusion is consistent with the general notion that structural flexibility within the active site of ALDH enzymes has been shown to be an integral component of catalysis
-
-
?
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0.0017 - 0.01
all-trans-retinal
additional information
additional information
-
0.0063
2,4-decadienal
pH 8.5, 25°C, recombinant enzyme
0.0063
2,4-decadienal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.0087
9-cis-retinal
-
25°C
0.0087
9-cis-retinal
-
recombinant wild-type enzyme, pH 7.2, 25°C
0.0017
all-trans-retinal
-
-
0.002
all-trans-retinal
pH 8.5, 25°C, recombinant enzyme
0.01
all-trans-retinal
-
25°C
0.01
all-trans-retinal
-
recombinant wild-type enzyme, pH 7.2, 25°C
0.0029
citral
pH 8.5, 25°C, recombinant enzyme
0.0029
citral
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.0003
decanal
-
-
0.0064
decanal
pH 8.5, 25°C, recombinant enzyme
0.0064
decanal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.0003
hexanal
-
-
0.023
hexanal
pH 8.5, 25°C, recombinant enzyme
0.023
hexanal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.022
NAD+
-
standard deviation 0.004 mM
0.166
NAD+
microsomes, high-fate diet rats, pH and temperature not specified in the publication
0.1822
NAD+
microsomes, control rats, pH and temperature not specified in the publication
0.2269
NAD+
cytosol, control rats, pH and temperature not specified in the publication
0.2424
NAD+
cytosol, high-fate diet rats, pH and temperature not specified in the publication
0.0007
retinal
cellular retinol-binding protein-bound retinal has lower Km of 0.0002 mM
0.002
retinal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.0085
retinal
-
retinal bovine serum albumin, Km is 25 times lower than the Km for acetaldehyde
0.0104
retinal
-
retinal-Tween-80
additional information
additional information
-
kinetics, recombinant wild-type and chimeric mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics and pre-steady-state kinetics
-
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Preparation and properties of retinal-oxidizing enzyme from rat intestinal mucosa
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245
439-447
1970
Rattus norvegicus, Rattus norvegicus Wistar
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Increased hepatic retinal dehydrogenase activity after phenobarbital and ethanol administration
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Changing patterns of renal retinal dehydrogenase expression parallel nephron development in the rat
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46
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1998
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brenda
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Enzymic characteristics of retinal dehydrogenase type I expressed in Escherichia coli
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1342
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brenda
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Purification and partial characterization of a rat kidney aldehyde dehydrogenase that oxidizes retinal to retinoic acid
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71
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Rattus norvegicus
brenda
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The structure of retinal dehydrogenase type II at 2.7 A resolution: implications for retinal specificity
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38
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1999
Rattus norvegicus (Q63639)
brenda
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
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Rattus norvegicus (Q63639)
brenda
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
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240
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Rattus norvegicus
brenda
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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
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19676-19682
1992
Rattus norvegicus
brenda
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
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162
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Immunolocalization of retinoic acid biosynthesis systems in selected sites in rat
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308
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329
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Characterization of retinaldehyde dehydrogenase-2 induction in NG2-positive glia after spinal cord contusion injury
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25
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2007
Rattus norvegicus
brenda
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Stromal cells confer lymph node-specific properties by shaping a unique microenvironment influencing local immune responses
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Estrogen receptor alpha regulates retinaldehyde dehydrogenase 1 expression in rat anterior pituitary cells
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56
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Rattus norvegicus (P51647)
brenda
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
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202
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brenda
Wang, C.; Kane, M.A.; Napoli, J.L.
Multiple retinol and retinal dehydrogenases catalyze all-trans-retinoic acid biosynthesis in astrocytes
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286
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2011
Rattus norvegicus
brenda
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
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202
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Homo sapiens (P00352), Homo sapiens, Rattus norvegicus (Q63639)
brenda
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
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127
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2015
Rattus norvegicus (P51647), Rattus norvegicus Sprague-Dawley (P51647)
brenda
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
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11
54
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Rattus norvegicus (P51647)
brenda