Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10'-apo-beta-carotenal + NAD+ + H2O
10'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E,14E)-4,9,13-trimethyl-15-(2,6,6-trimethylcyclohex-1-en-1-yl)pentadeca-2,4,6,8,10,12,14-heptaenal
-
-
?
12'-apo-beta-carotenal + NAD+ + H2O
12'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E,12E)-2,7,11-trimethyl-13-(2,6,6-trimethylcyclohex-1-en-1-yl)trideca-2,4,6,8,10,12-hexaenal
-
-
?
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH + H+
14'-apo-beta-carotenal + NAD+ + H2O
14'-apo-beta-carotenoic acid + NADH + 2 H+
i.e. (2E,4E,6E,8E,10E)-5,9-dimethyl-11-(2,6,6trimethylcyclohex-1-en-1-yl)undeca-2,4,6,8,10-pentaenal
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + 2 H+
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + H+
3-deoxyglucosone + NAD+ + H2O
2-keto-3-deoxygluconate + NADH + H+
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH + H+
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
aldophosphoamide + NAD+ + H2O
?
-
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans retinoate + NADH + 2 H+
-
-
-
?
all-trans retinal + NAD+ + H2O
all-trans-retinoate + NADH + H+
RALDH3 oxidizes all-trans retinal with high catalytic efficiency
-
-
?
all-trans retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
all-trans retinaldehyde + NAD+ + H2O
all-trans retinoic acid + NADH + H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 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
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
-
-
?
all-trans-retinaldehyde + NAD(P)H
NAD(P)+ + H2O + all-trans-retinoate
-
-
-
-
?
all-trans-retinol + NAD(P)H
NAD(P)+ + H2O + all-trans-retinaldehyde
-
-
-
-
?
all-trans-retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
?
all-trans-retinol + NADP+ + H2O
all-trans-retinoic acid + NADPH + H+
-
-
-
?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
BODIPY-aminoacetaldehyde + NAD+ + H2O
?
-
-
-
-
?
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
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + 2 H+
decanal + NAD+ + H2O
decanoate + NADH + H+
decanal + NAD+ + H2O
decanoic acid + NADH
dihydrolipoic acid + H2O + NAD+
? + NADH + 2 H+
-
-
-
?
glutathione + H2O + NAD+
GSSG + NADH + 2 H+
-
-
-
?
hexanal + H2O + NAD+
hexanoate + NADH + 2 H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + 2 H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
octanal + NAD+ + H2O
octanoate + NADH
octanal + NAD+ + H2O
octanoate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propanoate + NADH + H+
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
propionaldehyde + NAD+
propionate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
retinal + NAD+ + H2O
retinoate + NADH
retinal + NAD+ + H2O
retinoate + NADH + 2 H+
retinal + NAD+ + H2O
retinoate + NADH + H+
retinal + NAD+ + H2O
retinoic acid + NADH
-
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
retinol + NAD+ + H2O
? + NADH + H+
retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
-
?
additional information
?
-
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH
-
type-2 isozyme
-
-
?
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+
-
-
-
?
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH + H+
isoform RALDH4 oxidizes 13-cis retinal with lower catalytic efficiency than 9-cis retinal
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + H+
-
-
-
-
?
2,4-decadienal + NAD+ + H2O
2,4-decadienoate + NADH + H+
-
-
-
-
?
3-deoxyglucosone + NAD+ + H2O
2-keto-3-deoxygluconate + NADH + H+
-
-
-
-
?
3-deoxyglucosone + NAD+ + H2O
2-keto-3-deoxygluconate + NADH + H+
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
poortly active with
-
-
?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH + H+
-
-
-
?
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
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
acetaldehyde is not a substrate
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
no substrate inhibition
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
all-trans-retinal + H2O + NAD+
all-trans-retinoate + NADH + 2 H+
-
-
-
?
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
-
-
?
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-retinoate + NADH + 2 H+
-
-
-
?
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
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH + H+
-
-
-
-
?
citral + NAD+ + H2O
(2E)-3,7-dimethylocta-2,6-dienoic acid + NADH + H+
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + 2 H+
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
-
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
-
-
-
?
decanal + NAD+ + H2O
decanoate + NADH + H+
-
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
-
-
-
?
decanal + NAD+ + H2O
decanoic acid + NADH
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
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
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH
-
-
-
?
retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
-
-
-
?
retinal + NAD+ + H2O
all-trans-retinoate + NADH + 2 H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
preferred substrate
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
enzyme also accounts for about 90% of the 9-cis-retinal dehydrogenase activity
-
-
?
retinal + NAD+ + H2O
retinoate + NADH
-
-
-
?
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 + 2 H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + 2 H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + 2 H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + 2 H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + 2 H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
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
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoate + NADH + H+
-
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
-
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
-
-
-
-
?
retinol + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
retinol + NAD+ + H2O
? + NADH + H+
-
-
-
-
?
additional information
?
-
in the first acylation step, the activated catalytic Cys, Cys300 in BcALDH, attacks the substrate aldehyde group to form a thio-hemiacetal intermediate. The oxidized NAD(P)+ cofactor takes up a hydride ion from the thio-hemiacetal intermediate, which transforms it to a thioester intermediate. This intermediate is then deacylated by a water molecule, in which the additional catalytic residue Glu, Glu266 in BcALDH, activates the hydrolytic water molecule by abstracting a proton. Finally, the reduced NAD(P)H is released. Plausible mechanism for the minor reducing activity of BcALDH with all-trans-retinal, overview. The beta-ionone ring of the superimposed retinoic acid (REA) is bound at the mouth of the channel and exposed to the solvent. The substrate binding pocket-bound REA shows a bent conformation in the carbon positions from 9 to 11. Molecular docking of retinoic acid into the enzyme structure. BcALDH has a strict substrate preference for oxidation of all-trans-retinal, with no activity detected against 9-cis-retinal and 13-cis-retinal. BcALDH also has 14 and 30fold lower Km values for all-trans-retinal compared to the small aldehydes acetaldehyde and benzaldehyde, respectively
-
-
-
additional information
?
-
-
also active with medium-chain saturated aliphatic aldehydes
-
-
?
additional information
?
-
-
no significant conversion of 17beta-, 3alpha- and 11beta-hydroxysteroids, and corresponding ketosteroids
-
-
?
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. No activity with 2,4-decadienal, citral, and hexanal
-
-
?
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. No activity with 2,4-decadienal, citral, and hexanal
-
-
?
additional information
?
-
the dissociation of NADH from the enzyme is the rate-limiting step for ALDH1A1-mediated aldehyde oxidation. ALDH1A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH, product identification by thin layer chromatography (TLC). Even though they share the same NAD+-binding sites and the same active sites, the enzymatic mechanism of the GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is distinct from its aldehyde-dehydrogenase activity
-
-
-
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
-
-
?
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
-
-
?
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
?
-
-
the enzyme xCTBP/xALDH1 binds T3 within living cells
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(6-fluoro-3-(4-(methylsulfonyl)piperazine-1-carbonyl)-quinolin-4-yl)-4-phenylpiperidine-4-carbonitrile
i.e. NCT-505
-
2,3,5,6,9-pentamethyl-7H-furo[3,2-g][1]benzopyran-7-one
21.6% inhibition at 0.01 mM
-
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
9.5% inhibition at 0.01 mM
-
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
63.7% inhibition at 0.01 mM
-
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
91.3% inhibition at 0.01 mM
-
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
25.9% inhibition at 0.01 mM
-
2-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
16.79% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
14.47% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
29.37% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
8.5% inhibition at 0.01 mM at pH 7.5, 25°C
-
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide
50.4% inhibition at 0.01 mM
-
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetamide
71.5% inhibition at 0.01 mM
-
2H-furo[2,3-h][1]benzopyran-2-one
39.0% inhibition at 0.01 mM
-
3,3',5-tri-iodothyronine
-
3,3',5-Triiodothyroacetic acid
-
0.001 mM, 60% inhibition
3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
32.6% inhibition at 0.01 mM
-
3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one
38.5% inhibition at 0.01 mM
-
3,4-dimethyl-6,7,8,9-tetrahydro-2H-[1]benzofuro[3,2-g][1]benzopyran-2-one
35.7% inhibition at 0.01 mM
-
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
51.4% inhibition at 0.01 mM
-
3-(4-(4-(trifluoromethyl)benzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
3.86 % inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-bromobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
24.42% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-chlorobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
37.43% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-cyanobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
24.52% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
68.27% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-fluorobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
31.19% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
77.15% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
60.51% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
47.31% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(4-nitrobenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
28.33% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(cyclopropanecarbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
0.05% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-(furan-2-carbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
9.44% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-benzoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
39.23% inhibition at 0.01 mM at pH 7.5, 25°C at pH 7.5, 25°C
-
3-(4-isonicotinoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
36.65% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(4-nicotinoylpiperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
30.95% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-(benzo[d][1,3]dioxole-5-carbonyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)propanamide
35.93% inhibition at 0.01 mM at pH 7.5, 25°C
-
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
75.4% inhibition at 0.01 mM
-
3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
5.5% inhibition at 0.01 mM
-
3-[(3-oxobutan-2-yl)oxy]-6H-dibenzo[b,d]pyran-6-one
41.3% inhibition at 0.01 mM
-
3-[4-(furan-2-carbonyl)piperazin-1-yl]-N-(3-methylbut-2-en-1-yl)-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)propanamide
-
-
4-(1,3-dihydro-2H-isoindol-2-yl)benzaldehyde
-
-
4-(4-(4-ethylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
27.23% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-isopropylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
33.01% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-methoxybenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
13.10% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-(4-(4-methylbenzoyl)piperazin-1-yl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-N-(3-methylbut-2-en-1-yl)acetamide
32.19% inhibition at 0.01 mM at pH 7.5, 25°C
-
4-biphenyl carboxylic acid
-
90% inhibition at 0.1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
4-diethylaminobenzaldehyde
-
partial inhibition
4-dimethylamino-4-methyl-pent-2-ynthioic acid S-methyl ester
-
-
4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one
71.0% inhibition at 0.01 mM
-
4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one
47.8% inhibition at 0.01 mM
-
4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
61.7% inhibition at 0.01 mM
-
4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
64.5% inhibition at 0.01 mM
-
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
43.0% inhibition at 0.01 mM
-
5-methyl-2-[(3-oxobutan-2-yl)oxy]-7H-furo[3,2-g][1]benzopyran-7-one
31.3% inhibition at 0.01 mM
-
6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
12.6% inhibition at 0.01 mM; 41.5% inhibition at 0.01 mM
-
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
-
6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
34.8% inhibition at 0.01 mM
-
7-(2-oxopropoxy)-2H-1-benzopyran-2-one
7.6% inhibition at 0.01 mM
-
7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one
85.7% inhibition at 0.01 mM
-
7-methoxy-4-methyl-2H-1-benzopyran-2-one
19.8% inhibition at 0.01 mM
-
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
49.2% inhibition at 0.01 mM
-
8-[[4-(3-furoyl)-1-piperazinyl]methyl]-1,3-dimethyl-7-(3-methylbutyl)-3,7-dihydro-1H-purine-2,6-dione
i.e. CM026, 75.22% inhibition at 0.01 mM at pH 7.5, 25°C at pH 7.5, 25°C
-
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
43.7% inhibition at 0.01 mM
-
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
17.6% inhibition at 0.01 mM
-
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
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
Ca2+
-
50% inhibition at 0.22 mM
D-3,3',5-triiodothyronine
-
0.001 mM, 65% inhibition
dichloro-all-trans-retinone
-
diethylaminobenzaldehyde
DEAB, an ALDH1A1 inhibitor which competitively binds to the aldehyde-binding pocket of ALDH1A1 and completely inhibits the aldehyde oxidation activity of the enzyme at 0.01 mM, but has no effect on the GSH/DHLA-dependent NAD+-reduction activity
dimethyl ampal thiolester
-
estrogen
downregulates Raldh1 expression in the uterine glandular epithelium
ethanol
-
competitive inhibition
ethyl ([4-oxo-3-[3-(pyrrolidin-1-yl)propyl]-3,4-dihydro[1]benzothieno[3,2-d]pyrimidin-2-yl]sulfanyl)acetate
i.e. CM37
-
L-thyroxine
-
0.001 mM, 64% inhibition
Mn2+
-
50% inhibition at 0.024 mM
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
WIN 18,446; WIN 18,446, strong irreversible inhibition; WIN 18,446, weak inhibition
-
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
N,N-diethylaminobenzaldehyde
-
N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3,5-dimethylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
6.25% inhibition at 0.01 mM at pH 7.5, 25°C
-
N-(3-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(3-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide
40.2% inhibition at 0.01 mM
-
N-(4-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(4-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(4-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclobutylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclohexylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclopentylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-(cyclopropylmethyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-benzyl-3-(2,3,5-trimethyl-7-oxo-7H-furo[3,2-g][1]benzopyran-6-yl)propanamide
6.4% inhibition at 0.01 mM
-
N-benzyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-butyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-ethyl-3-[4-(furan-2-carbonyl)piperazin-1-yl]-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)propanamide
-
-
N-ethyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isobutyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isopentyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-isopropyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
N-propyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
-
-
NADPH
-
0.2 mM, 79% inhibition
nitrofen
-
90% inhibition at 0.1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM in absence of DTT, 2 mM DTT protect nearly completely; strongly suppress enzyme reaction, reversed by addition of DTT
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
SB-210661
-
80% inhibition at 1 mM in cell culture in vivo, leads to posterolateral defects in the diaphragm in vivo
Zn2+
-
50% inhibition at 0.01 mM
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
64.3% inhibition at 0.01 mM
-
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
a 2,4-thiazolidinedione-3-acetic acid derivative
-
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
a 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivative; a 1-oxopyrimido[4,5-c]quinoline-2-acetic acid derivative and a non-competitive inhibitor of ALDH1A3
-
acetaldehyde
-
60% competitive inhibition of all-trans-retinal oxidation at 0.4 mM
acetaldehyde
-
0.2 mM, 0.5 mM and 1.0 mM, uncompetitive inhibition
Chloral hydrate
-
80% competitive inhibition of all-trans-retinal oxidation at 0.1 mM
Chloral hydrate
-
noncompetitive inhibition
citral
-
complete inhibition at 1 mM; strongly suppress enzyme reaction
citral
-
IC50 about 0.001 mM
dichloro-all-trans-retinone
irreversible inhibitor that effectively inhibits isoform RALDH1 in the nanomolar range. I.e. (3E,5E,7E,9E)-1,1-dichloro-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,5,7,9-tetraen-2-one; irreversible inhibitor that effectively inhibits isoforms RALDH2 in the nanomolar range. I.e. (3E,5E,7E,9E)-1,1-dichloro-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,5,7,9-tetraen-2-one; irreversible inhibitor that effectively inhibits isoforms RALDH3 in the nanomolar range. I.e. (3E,5E,7E,9E)-1,1-dichloro-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,5,7,9-tetraen-2-one
-
dichloro-all-trans-retinone
irreversible inhibitor that effectively inhibits isoform RALDH2 in the nanomolar range. I.e. (3E,5E,7E,9E)-1,1-dichloro-4,8-dimethyl-10-(2,6,6-trimethylcyclohex-1-en-1-yl)deca-3,5,7,9-tetraen-2-one
-
Disulfiram
0.01 mM
Disulfiram
-
0.2 mM, 58% inhibition
Mg2+
at 30 mM Mg2+, significant inhibition of activity is shown for isoform RALDH1; at 30 mM Mg2+, significant inhibition of activity is shown for isoform RALDH2
Mg2+
inhibits the aldehyde dehydrogenase activity of ALDH1A1 by inhibiting the dissociation of NADH from the enzyme
Mg2+
-
about 50% inhibition of all-trans- and 9-cis-retinal oxidation above 1 mM
Mg2+
4 mM Mg2+ inhibits 9-cis retinal oxidation by isoform RALDH4 by 30%
Mg2+
specific activity is reduced half in presence of Mg2+
Mg2+
-
50% inhibition at 0.035 mM
N,N-diethylaminobenzaldehyde
DEAB; DEAB; DEAB
-
N,N-diethylaminobenzaldehyde
-
-
-
NaCN
-
slight
NADH
-
inhibits noncompetitively, inhibition not reversed by direct addition of NAD+
NADH
-
0.2 mM, 62% inhibition
retinal
-
strong substrate inhibition with 0.02 mM or more
retinal
-
substrate inhibition with concentration greater than 0.006 mM
WIN 18446
-
-
additional information
transfection of transcription factor cVax/Vax2 completely abolishes the spatial expression pattern of the retinoic acid synthesizing enzyme RALDH-1
-
additional information
transfection of transcription factor cVax/Vax2 completely abolishes the spatial expression pattern of the retinoic acid synthesizing enzyme RALDH-1
-
additional information
-
if dithiothreitol is omitted from the elution buffer during RDH13-His6 purification, the purified enzyme has a very low activity, but can be reactivated by the addition of dithiothreitol. Becomes partially inactivated after 20 min of incubation at 37°C. Not inhibited at 0.05 mM by nonanal, 6-cis-nonenal and 2-trans-nonenal, glyceraldehyde and acetoacetyl-coenzyme A, taurocholic acid, 25-hydroxycholesterol and 25-nor-5-cholesten-3-ol-25b-one
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. All tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1, EC 1.2.1.36) inhibitors and comparison of inhibitory activities on different ALDH isozymes, overview. Almost all tested compounds exhibit almost no inhibition against isozyme ALDH1A2 and show excellent selectivity toward isozyme ALDH1A1; design and synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity. N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide effectively improves glucose consumption in Hep-G2 cells compared to compound 1 (CM026). Cell viability assays with compounds N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide in Hep-G2 cells. Comparison of inhibitory activities on different ALDH isozymes, overview
-
additional information
not inhibited by trans-anethole; not inhibited by trans-anethole; not inhibited by trans-anethole
-
additional information
not inhibited by trans-anethole; not inhibited by trans-anethole; not inhibited by trans-anethole
-
additional information
not inhibited by trans-anethole; not inhibited by trans-anethole; not inhibited by trans-anethole
-
additional information
-
not inhibited by trans-anethole; not inhibited by trans-anethole; not inhibited by trans-anethole
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor; no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor; no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
additional information
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid, a 2,4-thiazolidinedione-3-acetic acid derivative, is inactive as inhibitor; no inhibition of ALDH1A1 by [3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by daidzin, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one, and 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one; inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. Poor or no inhibition by methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
-
additional information
-
all-trans-retinol and chloral hydrate do not inhibit enzyme reaction
-
additional information
-
beta-ionone has no effect on isoform RALDH3 activity
-
additional information
beta-ionone has no effect on isoform RALDH3 activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Acquired Immunodeficiency Syndrome
Cutting Edge: 4-1BB Controls Regulatory Activity in Dendritic Cells through Promoting Optimal Expression of Retinal Dehydrogenase.
Adenoma
Retinoid acid receptor expression is helpful to distinguish between adenoma and well-differentiated carcinoma in the thyroid.
Alzheimer Disease
Disruption of the retinoid signalling pathway causes a deposition of amyloid beta in the adult rat brain.
Asthma
Divergent functions for airway epithelial matrix metalloproteinase 7 and retinoic acid in experimental asthma.
Barrett Esophagus
The Microenvironment in Barrett's Esophagus Tissue Is Characterized by High FOXP3 and RALDH2 Levels.
Blindness
Retinal dehydrogenase 12 (RDH12) mutations in leber congenital amaurosis.
Breast Neoplasms
Profiling of the transcriptional response to all-trans retinoic acid in breast cancer cells reveals RARE-independent mechanisms of gene expression.
Carcinoma
Retinoid acid receptor expression is helpful to distinguish between adenoma and well-differentiated carcinoma in the thyroid.
Carcinoma
Vitamin A metabolism is impaired in human ovarian cancer.
Carcinoma, Hepatocellular
Retinal dehydrogenase 5 (RHD5) attenuates metastasis via regulating HIPPO/YAP signaling pathway in Hepatocellular Carcinoma.
Cataract
Molecular Mimicry between Betaine Aldehyde Dehydrogenase of Leptospira and Retinal Dehydrogenase 1 of Human Lens: A Potential Trigger for Cataract Formation in Leptospiral Uveitis Patients.
Cataract
Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei.
Choanal Atresia
A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment.
Colitis
Antibody secreting cells are critically dependent on integrin ?4?7/MAdCAM-1 for intestinal recruitment and control of the microbiota during chronic colitis.
Crohn Disease
Human CD14+ macrophages in intestinal lamina propria exhibit potent antigen-presenting ability.
Cystic Fibrosis
Retinoic acid signaling regulates murine bronchial tubule formation.
Diabetes Mellitus, Type 2
Raldh3 expression in diabetic islets reciprocally regulates secretion of insulin and glucagon from pancreatic islets.
Endometrial Hyperplasia
From endometrial hyperplasia to endometrial cancer: insight into the biology and possible medical preventive measures.
Esotropia
PLXNC1 and RDH13 associated with bilateral convergent strabismus with exophthalmus in German Brown cattle.
Food Hypersensitivity
Dietary Fiber and Bacterial SCFA Enhance Oral Tolerance and Protect against Food Allergy through Diverse Cellular Pathways.
Glomerulonephritis, IGA
Myofibroblasts acquire retinoic acid-producing ability during fibroblast-to-myofibroblast transition following kidney injury.
Heart Defects, Congenital
ALDH1A2 (RALDH2) genetic variation in human congenital heart disease.
Heart Defects, Congenital
Embryonic retinoic acid synthesis is essential for heart morphogenesis in the mouse.
Hernias, Diaphragmatic, Congenital
Retinal dehydrogenase-2 is inhibited by compounds that induce congenital diaphragmatic hernias in rodents.
Ileitis
Granulocyte-macrophage colony stimulating factor blockade promotes ccr9(+) lymphocyte expansion in Nod2 deficient mice.
Infections
Upregulation of Retinal Dehydrogenase 2 in Alternatively Activated Macrophages during Retinoid-dependent Type-2 Immunity to Helminth Infection in Mice.
Insulin Resistance
Contribution of Hepatic Retinaldehyde Dehydrogenase Induction to Impairment of Glucose Metabolism by High-Fat-Diet Feeding in C57BL/6J Mice.
Insulin Resistance
Retinaldehyde represses adipogenesis and diet-induced obesity.
Leber Congenital Amaurosis
Retinal dehydrogenase 12 (RDH12) mutations in leber congenital amaurosis.
Liver Cirrhosis
Retinol dehydrogenase 13 deficiency diminishes carbon tetrachloride-induced liver fibrosis in mice.
Lymphatic Metastasis
Aldehyde dehydrogenase 3A1 is robustly upregulated in gastric cancer stem-like cells and associated with tumorigenesis.
Metabolic Diseases
Vitamin A signaling and homeostasis in obesity, diabetes, and metabolic disorders.
Moyamoya Disease
Deregulation of Retinaldehyde Dehydrogenase 2 Leads to Defective Angiogenic Function of Endothelial Colony-Forming Cells in Pediatric Moyamoya Disease.
Myopia
Identification of active retinaldehyde dehydrogenase isoforms in the postnatal human eye.
Myopia
Postnatal Chick Choroids Exhibit Increased Retinaldehyde Dehydrogenase Activity During Recovery From Form Deprivation Induced Myopia.
Neoplasm Metastasis
Aldehyde dehydrogenase 3A1 is robustly upregulated in gastric cancer stem-like cells and associated with tumorigenesis.
Neoplasm Metastasis
Retinal dehydrogenase 5 (RHD5) attenuates metastasis via regulating HIPPO/YAP signaling pathway in Hepatocellular Carcinoma.
Neoplasms
Aldehyde dehydrogenase 3A1 is robustly upregulated in gastric cancer stem-like cells and associated with tumorigenesis.
Neoplasms
Development of a Retinal-Based Probe for the Profiling of Retinaldehyde Dehydrogenases in Cancer Cells.
Neoplasms
Diverse actions of retinoid receptors in cancer prevention and treatment.
Neoplasms
Evaluation of spice and herb as phyto-derived selective modulators of human retinaldehyde dehydrogenases using a simple in vitro method.
Neoplasms
From endometrial hyperplasia to endometrial cancer: insight into the biology and possible medical preventive measures.
Neoplasms
Inhibition of ALDH3A1-catalyzed oxidation by chlorpropamide analogues.
Neoplasms
Intestinal bacteria condition dendritic cells to promote IgA production.
Neoplasms
Investigating the Role of Missense SNPs on ALDH 1A1 mediated pharmacokinetic resistance to cyclophosphamide.
Neoplasms
Involvement of aldehyde dehydrogenase 1A2 in the regulation of cancer stem cell properties in neuroblastoma.
Neoplasms
Isolation and Establishment of a Highly Proliferative, Cancer Stem Cell-Like, and Naturally Immortalized Triple-Negative Breast Cancer Cell Line, KAIMRC2.
Neoplasms
Mouse CD11bhigh lung dendritic cells have more potent capability to induce IgA than CD103+ lung dendritic cells in vitro.
Neoplasms
Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase 6, absent in MCF-7 cells.
Neoplasms
The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes.
Nephrosis
Retinoids regulate the repairing process of the podocytes in puromycin aminonucleoside-induced nephrotic rats.
Neuroblastoma
Involvement of aldehyde dehydrogenase 1A2 in the regulation of cancer stem cell properties in neuroblastoma.
Obesity
Contribution of Hepatic Retinaldehyde Dehydrogenase Induction to Impairment of Glucose Metabolism by High-Fat-Diet Feeding in C57BL/6J Mice.
Obesity
Effects of citral, a naturally occurring antiadipogenic molecule, on an energy-intense diet model of obesity.
Obesity
Retinaldehyde represses adipogenesis and diet-induced obesity.
Pre-Eclampsia
Analysis of the placental tissue transcriptome of normal and preeclampsia complicated pregnancies.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3.
Prolactinoma
Reduction of retinaldehyde dehydrogenase 1 expression and production in estrogen-induced prolactinoma of rat.
Retinal Degeneration
Levels of retinoic acid and retinaldehyde dehydrogenase expression in eyes of the Mitf-vit mouse model of retinal degeneration.
retinal dehydrogenase deficiency
Rdh13 deficiency weakens carbon tetrachloride-induced liver injury by regulating Spot14 and Cyp2e1 expression levels.
retinal dehydrogenase deficiency
Retinaldehyde dehydrogenase 1 deficiency inhibits PPAR?-mediated bone loss and marrow adiposity.
retinal dehydrogenase deficiency
Retinoic Acid-dependent signaling pathways and lineage events in the developing mouse spinal cord.
retinal dehydrogenase deficiency
Retinol dehydrogenase 13 deficiency diminishes carbon tetrachloride-induced liver fibrosis in mice.
Retinal Dystrophies
RDH12 retinopathy: novel mutations and phenotypic description.
Spinal Cord Injuries
Characterization of retinaldehyde dehydrogenase-2 induction in NG2-positive glia after spinal cord contusion injury.
Spinal Dysraphism
Developing with lethal RA levels: genetic ablation of Rarg can restore the viability of mice lacking Cyp26a1.
Stomach Neoplasms
Aldehyde dehydrogenase 3A1 is robustly upregulated in gastric cancer stem-like cells and associated with tumorigenesis.
Stomach Neoplasms
Filtering High-Dimensional Methylation Marks With Extremely Small Sample Size: An Application to Gastric Cancer Data.
Teratocarcinoma
Molecular identification of a major retinoic-acid-synthesizing enzyme, a retinaldehyde-specific dehydrogenase.
Uveitis
Molecular Mimicry between Betaine Aldehyde Dehydrogenase of Leptospira and Retinal Dehydrogenase 1 of Human Lens: A Potential Trigger for Cataract Formation in Leptospiral Uveitis Patients.
Vision Disorders
Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy.
Vitamin A Deficiency
Astrocytes as a regulated source of retinoic acid for the brain.
Vitamin A Deficiency
Cellular expression of retinal dehydrogenase types 1 and 2: effects of vitamin A status on testis mRNA.
Vitamin A Deficiency
Retinal dehydrogenase gene expression in stomach and small intestine of rats during postnatal development and in vitamin A deficiency.
Vitamin A Deficiency
The role of vitamin A in mammalian reproduction and embryonic development.
Vitamin A Deficiency
Vitamin A deficiency induces congenital spinal deformities in rats.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0018 - 0.003
12'-apo-beta-carotenal
-
0.0006 - 0.00062
13-cis-retinal
0.005 - 0.012
14'-apo-beta-carotenal
0.095
3-deoxyglucosone
-
partially purified recombinant ALDH1A1 at pH 7.1 and in the presence of 1 mM NAD
0.00225 - 0.0087
9-cis-retinal
0.0002 - 0.015
all-trans-retinal
0.0032
all-trans-retinaldehyde
-
-
0.003
all-trans-retinol
-
-
0.0003 - 0.103
benzaldehyde
additional information
additional information
-
0.0018
12'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
-
0.003
12'-apo-beta-carotenal
isoform ALDH1A3, at pH 8.0 and 37°C
-
0.0034
13-cis retinal
-
0.0034
13-cis retinal
isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C
0.0006
13-cis-retinal
-
-
0.00062
13-cis-retinal
-
recombinant isozyme type-2, pH 9.0, 25°C
0.005
14'-apo-beta-carotenal
isoform ALDH1A2, at pH 8.0 and 37°C
0.012
14'-apo-beta-carotenal
isoform ALDH1A1, at pH 8.0 and 37°C
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
0.003
9-cis retinal
-
0.003
9-cis retinal
isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C
0.00225
9-cis-retinal
-
recombinant isozyme type-2, pH 9.0, 25°C
0.0036
9-cis-retinal
-
recombinant isozyme type-1, pH 7.5, 25°C
0.0087
9-cis-retinal
-
25°C
0.0087
9-cis-retinal
-
recombinant wild-type enzyme, pH 7.2, 25°C
0.014
acetaldehyde
-
recombinant wild-type enzyme, pH 8.5, 25°C
0.019
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.01 mM Zn2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+
0.024
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.02 Mn2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+
0.027
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.03 mM Ca2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+
0.028
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.1 mM Mg2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+
0.031
acetaldehyde
-
recombinant mutant L459F/N460G, pH 8.5, 25°C
0.055
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 12 mM acetaldehyde, 0.015-0.024 mM NAD+
1.4
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.3 mM Ca2+, 1-12 mM acetaldehyde, 0.33 mM NAD+
1.8
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.1 mM Mg2+, 1-12 mM acetaldehyde, 0.33 mM NAD+
2
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.02 mM Mn2+, 1-12 mM acetaldehyde, 0.33 mM NAD+
2.1
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.01 mM Zn2+, 1-12 mM acetaldehyde, 0.33 mM NAD+
3.4
acetaldehyde
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 1-12 mM acetaldehyde, 0.33 mM NAD+
0.0039
all-trans retinal
-
0.0039
all-trans retinal
isoform RALDH3, in 10 mM Tris-HCl buffer, pH 8.5, at 37°C
0.0002
all-trans-retinal
wild-type
0.0002
all-trans-retinal
F471L mutant
0.00066
all-trans-retinal
-
recombinant isozyme type-2, pH 9.0, 25°C
0.0007
all-trans-retinal
-
-
0.0017
all-trans-retinal
-
-
0.002
all-trans-retinal
pH 8.5, 25°C, recombinant enzyme
0.0081
all-trans-retinal
pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme
0.0086
all-trans-retinal
pH 8.5, 25°C, recombinant mutant K127A
0.0089
all-trans-retinal
pH 8.5, 25°C, recombinant mutant Y296A
0.01
all-trans-retinal
-
25°C
0.01
all-trans-retinal
-
recombinant wild-type enzyme, pH 7.2, 25°C
0.011
all-trans-retinal
pH 8.5, 25°C, recombinant mutant N120A
0.0116
all-trans-retinal
-
recombinant isozyme type-1, pH 7.5, 25°C
0.015
all-trans-retinal
pH 8.5, 25°C, recombinant mutant Y296V
0.0003
benzaldehyde
-
-
0.103
benzaldehyde
wild-type
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
-
-
0.001
decanal
-
recombinant wild-type enzyme and mutant L459F/N460G, pH 8.5, 25°C
0.0064
decanal
pH 8.5, 25°C, recombinant enzyme
0.0064
decanal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.01
decanal
-
wild type enzyme ALDH1A1, at pH 8.5 and 25°C
0.01
decanal
pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme
0.0003
hexanal
-
-
0.005
hexanal
-
recombinant wild-type enzyme, pH 8.5, 25°C
0.008
hexanal
pH 8.0, 25°C, recombinant enzyme
0.008
hexanal
-
recombinant mutant L459F/N460G, pH 8.5, 25°C
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
0.067
NAD+
-
recombinant wild-type enzyme, pH 8.5, 25°C
0.085
NAD+
-
partially purified recombinant ALDH1A1 at pH 7.1 and in the presence of 0.1 mM 3-deoxyglucosone
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
0.39
NAD+
-
recombinant mutant L459F/N460G, pH 8.5, 25°C
0.0003
octanal
-
-
0.0009
octanal
F471L mutant
0.005
octanal
-
recombinant mutant L459F/N460G, pH 8.5, 25°C
0.01
octanal
-
recombinant wild-type enzyme, pH 8.5, 25°C
0.0007
retinal
cellular retinol-binding protein-bound retinal has lower Km of 0.0002 mM
0.001
retinal
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.03 mM retinal, 0.056-0.12 mM NAD+
0.002
retinal
-
wild type enzyme ALDH1A2, at pH 8.5 and 25°C
0.0044
retinal
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.5 mM Ca2+, 0.03 mM retinal, 0.056-0.12 mM NAD+
0.0046
retinal
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.04 mM Mn2+, 0.03 mM retinal, 0.056-0.12 mM NAD+
0.006
retinal
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.3 mM Mg2+, 0.03 mM retinal, 0.056-0.12 mM NAD+
0.0064
retinal
-
50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.03 mM Zn2+ 0.03 mM retinal, 0.056-0.12 mM NAD+
0.0081
retinal
-
wild type enzyme ALDH1A1, at pH 8.5 and 25°C
0.0085
retinal
-
retinal bovine serum albumin, Km is 25 times lower than the Km for acetaldehyde
0.0086
retinal
-
mutant enzyme K127A, at pH 8.5 and 25°C
0.0089
retinal
-
mutant enzyme Y296A, at pH 8.5 and 25°C
0.0104
retinal
-
retinal-Tween-80
0.011
retinal
-
mutant enzyme N120A, at pH 8.5 and 25°C
0.015
retinal
-
mutant enzyme Y296V, at pH 8.5 and 25°C
0.0807
retinal
isoform RALDH2, at pH 8.2 and 25°C
additional information
additional information
-
kinetic analysis, isozyme type-2
-
additional information
additional information
-
kinetics, recombinant wild-type and chimeric mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics and pre-steady-state kinetics
-
additional information
additional information
Michaelis-Menten kinetics and pre-steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics and pre-steady-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00027 - 0.00033
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.0003 - 0.0004
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.00013 - 0.014
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
-
0.000069
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00076 - 0.0011
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
-
0.01 - 0.011
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
-
0.00013 - 0.00017
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
-
0.00121
8-[[4-(3-furoyl)-1-piperazinyl]methyl]-1,3-dimethyl-7-(3-methylbutyl)-3,7-dihydro-1H-purine-2,6-dione
Homo sapiens
pH 7.5, 25°C
-
0.000065 - 0.00013
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
-
0.0014
apo-CRBP
Rattus norvegicus
-
IC50 0.0014 mM
-
0.001
citral
Rattus norvegicus
-
IC50 about 0.001 mM
0.0045
daidzin
Homo sapiens
pH 7.5, 25°C
0.000055 - 0.0004347
dichloro-all-trans-retinone
-
0.00007 - 0.056
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
-
0.00018 - 0.047
N,N-diethylaminobenzaldehyde
-
0.000059
N-(2-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000126
N-(2-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000429
N-(2-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000872
N-(2-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000149
N-(2-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000379
N-(3-(trifluoromethyl)benzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000385
N-(3-chlorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.001075
N-(3-fluorobenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000966
N-(3-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.000715
N-(3-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.001144
N-(4-methylbenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.001135
N-benzyl-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide
Homo sapiens
pH 7.5, 25°C
-
0.0054 - 0.023
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
-
0.0012 - 0.0035
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
-
0.00027
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00033
2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0003
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0004
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00013
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0016
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.014
2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.00076
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.0011
3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
Homo sapiens
pH 7.5, 25°C
-
0.01
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
Homo sapiens
pH 7.5, 25°C
-
0.011
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
Homo sapiens
pH 7.5, 25°C
-
0.00013
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
Homo sapiens
pH 7.5, 25°C
-
0.00017
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
Homo sapiens
pH 7.5, 25°C
-
0.000065
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
Homo sapiens
pH 7.5, 25°C
-
0.00013
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
Homo sapiens
pH 7.5, 25°C
-
0.000055
dichloro-all-trans-retinone
Gallus gallus
isoform RALDH2, at pH 8.2 and 25°C
-
0.00016127
dichloro-all-trans-retinone
Gallus gallus
isoform RALDH3, at pH 8.2 and 25°C
-
0.00019132
dichloro-all-trans-retinone
Homo sapiens
isoform RALDH2, at pH 8.2 and 25°C
-
0.0004347
dichloro-all-trans-retinone
Gallus gallus
isoform RALDH1, at pH 8.2 and 25°C
-
0.00007
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.031
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.056
N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide)
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.00018
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0095
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.047
N,N-diethylaminobenzaldehyde
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0054
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.023
[(5E)-2,4-dioxo-5-([4-[(4-oxo-3-phenyl-3,4-dihydroquinazolin-2-yl)methoxy]phenyl]methylidene)-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0012
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
0.0035
[3-benzyl-5-(4-chlorophenyl)-1-oxopyrimido[4,5-c]quinolin-2(1H)-yl]acetic acid
Homo sapiens
pH 8.0, 25°C, recombinant enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Graham, C.; Hodin, J.; Wistow, G.
A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of beta-crystallin
J. Biol. Chem.
271
15623-15628
1996
Galegeeska rufescens
brenda
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)
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
16288-16293
1996
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
Eur. J. Biochem.
240
15-22
1996
Rattus norvegicus
brenda
Moore, S.A.; Baker, H.M.; Blythe, T.; Kitson, K.E.; Kitson, T.M.; Baker, E.N.
Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases
Structure
6
1541-1551
1998
Ovis aries aries
brenda
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
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
Am. J. Pathol.
162
673-679
2003
Rattus norvegicus
brenda
Gagnon, I.; Duester, G.; Bhat, P.V.
Enzymatic characterization of recombinant mouse retinal dehydrogenase type 1
Biochem. Pharmacol.
65
1685-1690
2003
Mus musculus
brenda
Bateman, O.A.; Purkiss, A.G.; van Montfort, R.; Slingsby, C.; Graham, C.; Wistow, G.
Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens
Biochemistry
42
4349-4356
2003
Elephantulus edwardii (Q28399)
brenda
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
brenda
Yamauchi, K.; Nakajima, J.
Effect of coenzymes and thyroid hormones on the dual activities of Xenopus cytosolic thyroid-hormone-binding protein (xCTBP) with aldehyde dehydrogenase activity
Eur. J. Biochem.
269
2257-2264
2002
Xenopus laevis
brenda
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
brenda
Sladek, N.E.
Human aldehyde dehydrogenases: Potential pathological, pharmacological, and toxicological impact
J. Biochem. Mol. Toxicol.
17
7-23
2003
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
Moreb, J.S.; Gabr, A.; Vartikar, G.R.; Gowda, S.; Zucali, J.R.; Mohuczy, D.
Retinoic acid down-regulates aldehyde dehydrogenase and increases cytotoxicity of 4-hydroperoxycyclophosphamide and acetaldehyde
J. Pharmacol. Exp. Ther.
312
339-345
2005
Homo sapiens
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Kim, Y.H.; Arnold, A.P.
Distribution and onset of retinaldehyde dehydrogenase (zRalDH) expression in zebra finch brain: lack of sex difference in HVC and RA at early posthatch ages
J. Neurobiol.
65
260-268
2005
Taeniopygia guttata
brenda
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
brenda
Rahman, F.B.; Yamauchi, K.
Uncompetitive inhibition of Xenopus laevis aldehyde dehydrogenase 1A1 by divalent cations
Zool. Sci.
23
239-244
2006
Xenopus laevis
brenda
Belyaeva, O.V.; Korkina, O.V.; Stetsenko, A.V.; Kedishvili, N.Y.
Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity
FEBS J.
275
138-147
2008
Homo sapiens
brenda
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens (O94788)
brenda
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)
brenda
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
brenda
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)
brenda
Liang, D.; Zhang, M.; Bao, J.; Zhang, L.; Xu, X.; Gao, X.; Zhao, Q.
Expressions of Raldh3 and Raldh4 during zebrafish early development
Gene Expr. Patterns
8
248-253
2008
Danio rerio (A9YD19), Danio rerio (Q0H2G3), Danio rerio
brenda
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
brenda
Golz, S.; Muehleisen, T.; Schulte, D.; Mey, J.
Regulation of RALDH-1, RALDH-3 and CYP26A1 by transcription factors cVax/Vax2 and Tbx5 in the embryonic chick retina
Int. J. Dev. Neurosci.
26
435-445
2008
Gallus gallus (P27463), Gallus gallus (Q9DD46)
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
Kot-Leibovich, H.; Fainsod, A.
Ethanol induces embryonic malformations by competing for retinaldehyde dehydrogenase activity during vertebrate gastrulation
Dis. Model. Mech.
2
295-305
2009
Xenopus laevis
brenda
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)
brenda
Kirschner, R.D.; Rother, K.; Mueller, G.A.; Engeland, K.
The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes
Cell Cycle
9
2177-2188
2010
Homo sapiens
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
Chem. Biol. Interact.
202
78-84
2013
Homo sapiens, Rattus norvegicus
brenda
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
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
Chem. Biol. Interact.
202
78-84
2013
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
J. Pharmacol. Sci.
127
430-438
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
Nutr. Metab.
11
54
2014
Rattus norvegicus (P51647)
brenda
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)
brenda
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
brenda
Ma, Z.; Jiang, L.; Li, G.; Liang, D.; Li, L.; Liu, L.; Jiang, C.
Design, synthesis of 1,3-dimethylpyrimidine-2,4-diones as potent and selective aldehyde dehydrogenase 1A1 (ALDH1A1) inhibitors with glucose consumption improving activity
Bioorg. Chem.
101
103971
2020
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
brenda
Harper, A.R.; Le, A.T.; Mather, T.; Burgett, A.; Berry, W.; Summers, J.A.
Design, synthesis, and ex vivo evaluation of a selective inhibitor for retinaldehyde dehydrogenase enzymes
Bioorg. Med. Chem.
26
5766-5779
2018
Gallus gallus, Gallus gallus (O93344), Gallus gallus (P27463), Homo sapiens (O94788)
brenda
Bui, T.B.C.; Nosaki, S.; Kokawa, M.; Xu, Y.; Kitamura, Y.; Tanokura, M.; Hachimura, S.; Miyakawa, T.
Evaluation of spice and herb as phyto-derived selective modulators of human retinaldehyde dehydrogenases using a simple in vitro method
Biosci. Rep.
41
BSR20210491
2021
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895), Homo sapiens
brenda
Jimenez, R.; Pequerul, R.; Amor, A.; Lorenzo, J.; Metwally, K.; Aviles, F.X.; Pares, X.; Farres, J.
Inhibitors of aldehyde dehydrogenases of the 1A subfamily as putative anticancer agents kinetic characterization and effect on human cancer cells
Chem. Biol. Interact.
306
123-130
2019
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
brenda
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
brenda
Jung, K.; Hong, S.H.; Ngo, H.P.; Ho, T.H.; Ahn, Y.J.; Oh, D.K.; Kang, L.W.
Crystal structures of an atypical aldehyde dehydrogenase having bidirectional oxidizing and reducing activities
Int. J. Biol. Macromol.
105
816-824
2017
Bacillus cereus (A0A150BLG9)
brenda
Hu, H.; Xu, L.; Luo, S.J.; Xiang, T.; Chen, Y.; Cao, Z.R.; Zhang, Y.J.; Mo, Z.; Wang, Y.; Meng, D.F.; Yu, L.; Lin, L.Z.; Zhang, S.J.
Retinal dehydrogenase 5 (RHD5) attenuates metastasis via regulating HIPPO/YAP signaling pathway in hepatocellular carcinoma
Int. J. Med. Sci.
17
1897-1908
2020
Homo sapiens
brenda
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
brenda
Buchman, C.D.; Hurley, T.D.
Inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives
J. Med. Chem.
60
2439-2455
2017
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
brenda
Wang, B.; Chen, X.; Wang, Z.; Xiong, W.; Xu, T.; Zhao, X.; Cao, Y.; Guo, Y.; Li, L.; Chen, S.; Huang, S.; Wang, X.; Fang, M.; Shen, Z.
Aldehyde dehydrogenase 1A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction
Oncotarget
8
67043-67055
2017
Homo sapiens (P00352)
brenda
Park, J.W.; Jung, K.H.; Lee, J.H.; Moon, S.H.; Cho, Y.S.; Lee, K.H.
Inhibition of aldehyde dehydrogenase 1 enhances the cytotoxic effect of retinaldehyde on A549 cancer cells
Oncotarget
8
99382-99393
2017
Homo sapiens
brenda
Dominguez, M.; Pequerul, R.; Alvarez, R.; Gimenez-Dejoz, J.; Birta, E.; Porte, S.; Ruehl, R.; Pares, X.; Farres, J.; de Lera, A.
Synthesis of apocarotenoids by acyclic cross metathesis and characterization as substrates for human retinaldehyde dehydrogenases
Tetrahedron
74
2567-2574
2018
Homo sapiens (O94788), Homo sapiens (P00352), Homo sapiens (P47895)
-
brenda