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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
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-
?
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
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-
?
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
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-
?
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+
-
-
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?
additional information
?
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13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH
-
type-2 isozyme
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-
?
13-cis-retinal + NAD+ + H2O
13-cis-retinoate + NADH
-
type-2 isozyme, 2fold lower activity compared to all-trans-retinal
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?
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
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-
?
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
-
-
-
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?
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
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-
?
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
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?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
-
-
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?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH
-
poortly active with
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?
9-cis-retinal + NAD+ + H2O
9-cis-retinoate + NADH + H+
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?
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
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?
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
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?
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+
-
-
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?
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
-
-
-
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?
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
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-
?
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
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-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoate + NADH
-
preferred substrate, type-2 isozyme
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-
?
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
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-
?
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
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-
-
additional information
?
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-
also active with medium-chain saturated aliphatic aldehydes
-
-
?
additional information
?
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-
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
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-
?
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
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-
-
additional information
?
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-
enzyme is involved in retinoic acids biosynthesis, which are important signaling molecules in embryogenesis and tissue differentiation
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-
?
additional information
?
-
-
physiological function, newborn lethal defect due to isozyme type-3 inactivation is prevented by maternal retinoic acid treatment, overview
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-
?
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
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-
?
additional information
?
-
-
substrate specificities of wild-type isozyme type-2 and mutant L459F/N460G
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-
?
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
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-
?
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
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-
?
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
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the enzyme xCTBP/xALDH1 binds T3 within living cells
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