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Information on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+]
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EC Tree
1.2.1.5 aldehyde dehydrogenase [NAD(P)+]Specify your search results
Word Map
- 1.2.1.5
-
aldhs
-
drinking
- disulfiram
-
nadp+-dependent
- benzaldehyde
-
alcohol-induced
- cyanamide
-
aldh2*2
- phosphotransacetylase
-
meta-cleavage
-
1.2.1.3
-
alcohol-related
- energy production
- medicine
- degradation
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acetaldehyde dehydrogenase, ALD4, aldehyde dehydrogenase, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 2, aldehyde: NAD(P)+ oxidoreductase, ALDH, ALDH1, ALDH13, ALDH17, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde dehydrogenase
aldehyde dehydrogenase 2
aldehyde: NAD(P)+ oxidoreductase
ALDH
Aldh1a3
ALDH2
ALDH3
ALDH3A1
Aldh3b1
ALDHIII
-
-
-
-
BCP54
-
-
-
-
Corneal 15.8 kDa protein
-
-
-
-
Corneal protein 54
-
-
-
-
dehydrogenase, aldehyde (nicotinamide adenine dinucleotide (phosphate))
-
-
-
-
HTC-ALDH
-
-
-
-
NAD(P)(+)-dependent aldehyde dehydrogenase
NAD(P)+-dependent aldehyde dehydrogenase
nicotinprotein aldehyde dehydrogenase
PEG-ALDH
PuuC
ST0064
Transparentin
-
-
-
-
Tumor-associated aldehyde dehydrogenase
-
-
-
-
ybcD
aldehyde dehydrogenase
-
ALDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H + H+
ordered bi bi mechanism with NAD+ as the leading substrate
-
an aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD(P)+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-88-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-dihydroxyacetone + NAD+ + H2O
? + NADH + H+
53.93% of the activity compared to acetaldehyde
-
-
?
1-formyl-6-methylpyrene + NADP+ + H2O
6-methylpyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
1-formyl-8-methylpyrene + NADP+ + H2O
8-methylpyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
1-formylpyrene + NADP+ + H2O
pyrene-1-carboxylic acid + NADPH + H+
-
-
-
?
2,5-dihydroxybenzaldehyde + NADP+ + H2O
2,5-dihydroxybenzoate + NADPH + H+
-
-
-
-
?
2-formylpyrene + NADP+ + H2O
pyrene-2-carboxylic acid + NADPH + H+
-
-
-
?
3,4-dihydroxymandelaldehyde + NAD+ + H2O
3,4-dihydroxyphenylmandelate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+
3,4-dihydroxyphenylacetate + NADH
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
-
-
-
?
3-hydroxybenzaldehyde + NADP+ + H2O
3-hydroxybenzoate + NADPH + H+
-
-
-
-
?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
32.98% of the activity compared to acetaldehyde
-
-
?
4-carboxybenzaldehyde + NADP+ + H2O
4-carboxybenzoate + NADPH + H+
-
-
-
-
?
4-chlorobenzaldehyde + NADP+ + H2O
4-chlorobenzoate + NADPH + H+
-
-
-
-
?
4-formylpyrene + NADP+ + H2O
pyrene-4-carboxylic acid + NADPH + H+
-
-
-
?
4-pyridinecarboxaldehyde + NAD+ + H2O
4-pyridinecarboxylate + NADH + H+
-
-
-
-
?
5-hydroxyindole-3-acetyldehyde + NAD+ + H2O
5-hydroxyindole-3-acetate + NADH + H+
-
-
-
-
?
6-methoxy-2-naphthaldehyde + NADH + H+
6-methoxy-2-naphthyl alcohol + NAD+
-
-
-
-
?
acetaldehyde + 3-pyridine aldehyde adenine dinucleotide phosphate
acetate + ?
-
-
-
-
?
aldophosphamide + NAD+
N,N-bis-(2-chloroethyl)-diaminophosphoric-(2-carboxyethylester) + ?
-
-
-
-
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
50.25% of the activity compared to acetaldehyde. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
-
-
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH
50.25% of the activity compared to acetaldehyde
-
-
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
D-glycerate 3-phosphate + NADH + H+
52.7% of the activity compared to acetaldehyde
-
-
?
DL-glyceraldehyde + NAD(P)+ + H2O
glycerate + NAD(P)H + H+
-
14% of activity with benzaldehyde
-
-
ir
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
75.43% of the activity compared to acetaldehyde
-
-
?
heptanal + NADP+ + H2O
heptanoate + NADPH + H+
-
-
-
?
isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
-
-
-
-
n-tetradecanal + NADP+ + H2O
n-tetradecanoate + NADPH + H+
-
-
-
-
?
p-hydroxybenzaldehyde + NADP+ + H2O
p-hydroxybenzoic acid + NADPH + H+
-
-
-
-
?
polyethylene glycol 4000-aldehyde + NADP+
? + NADPH
-
highest activtiy compared to other polyethylene glycolaldehydes
-
-
?
propanal + 1,N6-ethenoadenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + 3-acetylpyridine adenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + 3-pyridine adenine dinucleotide
propionate + ?
-
isoenzyme E1 and E2
-
-
?
propanal + beta-NADP+ + H2O
propionate + beta-NADPH + H+
-
isoenzyme E1 and E2
-
-
?
propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
-
isoenzyme E1 and E2
-
-
?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
preferred substrate of isozyme ALDH1A3
-
-
?
valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
-
-
-
?
2-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH + H+
-
-
-
-
?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
-
-
-
?
2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
-
-
-
?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
-
-
-
?
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
51% of activity with benzaldehyde
-
-
ir
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
activity with the enzyme from stomach mucosa, no activity with the enzyme from breast adenocarcinoma cell line
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
-
-
?
all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
-
-
-
-
?
all-trans-retinal + NADP+ + H2O
all-trans-retinol + NADPH + H+
-
-
-
-
?
an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
-
-
-
?
an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
ALDH2 is very active, low activity with ALDH1 and ALDH5
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
35.5% of the activity compared to acetaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
35.5% of the activity compared to acetaldehyde
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
25% of activity with NAD+
-
-
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
-
-
?
butyraldehyde + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
-
23% of activity with benzaldehyde
-
-
ir
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
48.15% of the activity compared to acetaldehyde
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
48.15% of the activity compared to acetaldehyde
-
-
?
formaldehyde + NAD(P)+ + H2O
formate + NAD(P)H + H+
-
52% of activity with benzaldehyde
-
-
ir
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
-
-
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
4% of the activity with acetaldehyde
-
-
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
4% of the activity with acetaldehyde
-
-
?
heptylaldehyde + NAD(P)+ + H2O
heptanoate + NAD(P)H + H+
-
12% of activity with benzaldehyde
-
-
ir
hexylaldehyde + NAD(P)+ + H2O
hexanoate + NAD(P)H + H+
-
22% of activity with benzaldehyde
-
-
ir
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
-
188% of activity with benzaldehyde
-
-
ir
isovaleraldehyde + NAD(P)+ + H2O
isovalerate + NAD(P)H
-
83% of activity with benzaldehyde
-
-
ir
isovaleraldehyde + NADP+
isovalerate + NADPH + H+
-
-
-
-
?
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
-
-
-
ir
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
-
28% of activity with benzaldehyde
-
-
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
-
-
-
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
-
35% of activity with benzaldehyde
-
-
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
-
41% of activity with benzaldehyde
-
-
ir
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
62% of the activity with acetaldehyde
-
-
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
55% of the activity with acetaldehyde
-
-
?
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
-
100% of activity with benzaldehyde
-
-
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
-
-
-
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
-
18% of activity with benzaldehyde
-
-
ir
octylaldehyde + NAD(P)+ + H2O
octanoate + NAD(P)H + H+
-
10% of activity with benzaldehyde
-
-
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
-
-
-
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
-
14% of activity with benzaldehyde
-
-
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
-
-
-
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
-
35% of activity with benzaldehyde
-
-
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
-
-
-
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
-
75% of activity with benzaldehyde
-
-
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
-
-
-
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
-
15% of activity with benzaldehyde
-
-
ir
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
isoenzyme E1
-
-
?
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
no reaction with isoenzyme E2
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
88% of the activity with acetaldehyde
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
88% of the activity with acetaldehyde
-
-
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
-
-
-
?
propionaldehyde + NAD(P)+ + H2O
propionate + NAD(P)H
-
75% of activity with benzaldehyde
-
-
ir
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
best substrate combination
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
best substrate combination
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
56.22% of the activity compared to acetaldehyde
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
56.22% of the activity compared to acetaldehyde
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
-
-
?
valeraldehyde + NAD(P)+ + H2O
valerate + NAD(P)H + H+
-
16.3% of activity with benzaldehyde
-
-
ir
additional information
?
-
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
-
additional information
?
-
-
no activity with 9-cis-retinal and 13-cis-retinal
-
-
-
additional information
?
-
-
no activity with formaldehyde and benzaldehyde
-
-
-
additional information
?
-
-
no activity with formaldehyde and benzaldehyde
-
-
-
additional information
?
-
-
the membrane bound enzyme may act as barrier when the aldehyde concentration in cytosol is high
-
-
-
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
-
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
-
additional information
?
-
-
isoenzyme f1 may be the primary enzyme for oxidizing the acetaldehyde produced during ethanol oxidation in vivo
-
-
-
additional information
?
-
-
enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
-
-
-
additional information
?
-
-
enzyme follows a sequential mode of reaction mechanism
-
-
-
additional information
?
-
-
iol operon is involved in myo-inositol catabolism
-
-
?
additional information
?
-
-
enzyme prefers aldehyde products of lipid peroxidation as substrates
-
-
-
additional information
?
-
-
dual role for the corneal enzyme in providing the eye with protection against UV-B light: by oxidizing aldehydes generated through light-induced lipid peroxidation and by direct absorption of UV-B light by the enzyme
-
-
-
additional information
?
-
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q0DZ46
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
ALDHC is preferentially active towards linear medium-chain to long-chain aldehydes as compared to branched-chain, short-chain or aromatic aldehydes. Reorientation of an extended loop (Asn478-Pro490) is responsible for the constricted structure of the substrate tunnel, with the side chain of Asn478 imposing steric restrictions on branched-chain and aromatic aldehydes. A key glycine (Gly104) positioned at the mouth of the tunnel allows for maximum tunnel depth required to bind the linear medium to long aliphatic chain of the native substrate
-
-
-
additional information
?
-
-
the enzyme plays a role in oxidation of a variety of aldehydes generated by lipid metabolism
-
-
-
additional information
?
-
no activity with methanol or ethanol
-
-
-
additional information
?
-
no activity with methanol or ethanol
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
Q976X5
-
-
-
?
an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
Q976X5
-
-
-
?
additional information
?
-
-
the membrane bound enzyme may act as barrier when the aldehyde concentration in cytosol is high
-
-
-
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
-
additional information
?
-
-
enzyme is induced during growth on tetrahydrofurfuryl alcohol
-
-
-
additional information
?
-
-
isoenzyme f1 may be the primary enzyme for oxidizing the acetaldehyde produced during ethanol oxidation in vivo
-
-
-
additional information
?
-
-
enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
-
-
-
additional information
?
-
-
dual role for the corneal enzyme in providing the eye with protection against UV-B light: by oxidizing aldehydes generated through light-induced lipid peroxidation and by direct absorption of UV-B light by the enzyme
-
-
-
additional information
?
-
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q0DZ46
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q53NG8
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q69P84
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q6H627
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q7XR89
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q9FRX7
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q9LRE9
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
additional information
?
-
Q9LRI6
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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additional information
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the enzyme plays a role in oxidation of a variety of aldehydes generated by lipid metabolism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
NADP+
significant preference for NADP+. Cofactor selectivity is governed by a complex network of hydrogen bonds between the oxygen atoms of the 2'-phosphoryl moiety of NADP+ and a threonine/lysine pair on ALDHC
NADP+
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kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
KCl
-
120 mM: 40fold increase of activity of ALDH5 with NAD+. 16 mM: 20fold increase of activity of enzyme ALDH5 with NADP+. No stimulation of the activity of enzyme form ALDH1
Li+
-
500 mM, 107% of the activity compared to activity without metal ions
Mg2+
additional information
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the enzyme does not require metal ions for its enzymatic reaction
Mg2+
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20 mM, 107% of the activity compared to activity without metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-thionicotinamide adenine dinucleotide
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strong inhibition versus beta-NAD+, isoenzyme E2; substrate inhibition, isoenzyme E1
benomyl
potent irreversible inhibitor of ALDH. Benomyl increases superoxide production as much as nitroglycerin
Benzoate
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non-competitive with respect to either NAD+ or benzaldehyde
H2O2
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the loss of activity induced by H2O2 can be restored by reducing agents, although a decrease of the restored activity is observed upon addition of 10 mM dithiothreitol
trans-4-(N,N-dimethylamino)-cinnamaldehyde
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1 mM, 58% inhibition; 58% inhibition at 1 mM
Chloral hydrate
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50% inhibition of isoenzyme F1 by 0.25 mM, 50% inhibition of isoenzyme F2 by 0.4 mM
Disulfiram
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0.025 mM, 99% inhibition of activity with NADP+, 80% inhibition of activity with activity with NAD+
Disulfiram
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0.025 mM or 0.05 mM, 99% inhibition of activity with NADP+, 60% inhibition of activity with NAD+
NADH
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competitive with respect to NAD+ and non-competitive with respect to either benzaldehyde or glycolaldehyde
nitroglycerin
induces nitrate tolerance. Expression and activity of ALDH-2 is decreased in nitrate-tolerant rats
nitroglycerin
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more than half of the original activity is retained in the presence of 5.5 mM nitroglycerin and approximate 80% of the activity is lost by the addition of 11 mM nitroglycerin. Dithiothreitol and alpha-lipoic acid can also restore the nitroglycerin inactivated dehydrogenation to more than half of the original activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.137
n-dodecanal
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50 mM potassium phosphate buffer pH8.0, 1 mM CaCl2, 36°C
0.091
4-Pyridinecarboxaldehyde
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reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
0.19
4-Pyridinecarboxaldehyde
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reaction with NAD+ or NADP+, enzyme from stomach mucosa
18.89
acetaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
393.4
acetaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.64
benzaldehyde
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reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
2.95
Butyraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
4.93
Butyraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.013
Chloroacetaldehyde
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.039
Chloroacetaldehyde
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.052
Chloroacetaldehyde
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.3
Chloroacetaldehyde
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.46
Chloroacetaldehyde
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
9.87
Isovaleraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
10.78
Isovaleraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.0037
NAD+
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mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.004
NAD+
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wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.00625
NAD+
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mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.01
NAD+
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mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.048
NAD+
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.094
NAD+
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.19
NAD+
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.39
NAD+
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.1
NAD+
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.067
octanal
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reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
0.46
propionaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.65
propionaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.12
Valeraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.34
Valeraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.11
acetaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
4.46
acetaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
11.5
Butyraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
32.8
Butyraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.47
Chloroacetaldehyde
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.63
Chloroacetaldehyde
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.5
Chloroacetaldehyde
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4
Chloroacetaldehyde
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
7.7
Chloroacetaldehyde
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.91
Isovaleraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
3.58
Isovaleraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.0007
NAD+
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mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.0017
NAD+
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wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.005
NAD+
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mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.026
NAD+
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mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.47
NAD+
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.63
NAD+
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.5
NAD+
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4
NAD+
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
7.7
NAD+
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
13.36
propionaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
49.38
propionaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
19.41
Valeraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
30.99
Valeraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
acetaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.24
acetaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
2.39
Butyraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
11.89
Butyraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
5.5
Chloroacetaldehyde
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
12.2
Chloroacetaldehyde
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
13.2
Chloroacetaldehyde
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
183.3
Chloroacetaldehyde
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
200
Chloroacetaldehyde
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.09
Isovaleraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.36
Isovaleraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.16
NAD+
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mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.42
NAD+
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wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.5
NAD+
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mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
1.8
NAD+
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mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
3.3
NAD+
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mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4.1
NAD+
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mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
6.5
NAD+
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mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
33.3
NAD+
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mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
158.3
NAD+
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wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
20.67
propionaldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
107.5
propionaldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
56.66
Valeraldehyde
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with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
257
Valeraldehyde
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with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.48
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recombinant enzyme, using 3-hydroxypropionaldehyde and NAD+ as substrates, at pH 8.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
10
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activity with NAD+, broad plateau from pH 5 to 8 followed by a sharp increase in activity to pH 10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
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pH 6.0: about 60% of maximal activity, pH 9.0: about 90% of maximal activity
6.2 - 6.7
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pH 6.2: about 80% of maximal activity, pH 6.7: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 90
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70°C: about 50% of maximal activity, 90°C: about 90% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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exhibiting oxazaphosphorine-specific acquired resistance, enzyme form ALDH3
brenda
isozyme Aldh1a3 mRNA expression is highest in placenta
brenda
additional information
addition of ALDH to RASM cell homogenates significantly decreases NO consumption
brenda
isozyme Aldh3a1 mRNA expression is highest in stomach
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
;
brenda
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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isoforms ALDH3A1 plays a protective role against ultraviolet radiation-induced oxidative damage to ocular tissues, detoxifies reactive aldehydes and acts as antioxidant
physiological function
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ALDH9, ALDH13, and ALDH17 genes involve the function of drought stress, acid tolerance, and pathogens infection
physiological function
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isotype ALDH1A1 is the key ALDH isozyme linked to tissue stem cells populations and an important contributor to cancer stem cells function in cancers
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