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Information on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.2.1.5
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.5 aldehyde dehydrogenase [NAD(P)+]
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.2.1.5
-
aldhs
-
retinoic
- disulfiram
-
alcohol-induced
- benzaldehyde
-
nadp+-dependent
- retinaldehyde
- cyanamide
-
meta-cleavage
-
aldh2*2
- phosphotransacetylase
-
1.2.1.3
-
hangover
-
alcohol-related
- medicine
- energy production
- synthesis
- analysis
- degradation
showSynonyms
acetaldehyde dehydrogenase, aldh3, aldh1a, myo-inositol dehydrogenase, class 3 aldehyde dehydrogenase, aldh9, tumor-associated aldehyde dehydrogenase, aldh2a, bcaldh, osaldh7, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALD4
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
NAD+-dependent Ald4
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
MetaCyc
L-tryptophan degradation V (side chain pathway)
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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
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,3-dihydroxyacetone + NAD+ + H2O
? + NADH + H+
Substrates: 53.93% of the activity compared to acetaldehyde
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1-formyl-6-methylpyrene + NADP+ + H2O
6-methylpyrene-1-carboxylic acid + NADPH + H+
Substrates: -
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1-formyl-8-methylpyrene + NADP+ + H2O
8-methylpyrene-1-carboxylic acid + NADPH + H+
Substrates: -
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1-formylpyrene + NADP+ + H2O
pyrene-1-carboxylic acid + NADPH + H+
Substrates: -
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?
2,5-dihydroxybenzaldehyde + NADP+ + H2O
2,5-dihydroxybenzoate + NADPH + H+
-
Substrates: -
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2-formylpyrene + NADP+ + H2O
pyrene-2-carboxylic acid + NADPH + H+
Substrates: -
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?
2-methylbutyraldehyde + NAD+ + H2O
2-methylbutyrate + NADH + H+
-
Substrates: -
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2-naphthaldehyde + NADH + H+
2-naphthyl alcohol + NAD+
Substrates: -
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?
3,4-dihydroxymandelaldehyde + NAD+ + H2O
3,4-dihydroxyphenylmandelate + NADH + H+
-
Substrates: -
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?
3,4-dihydroxyphenylacetaldehyde + NAD+
3,4-dihydroxyphenylacetate + NADH
-
Substrates: -
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3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
Substrates: -
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?
3,4-dihydroxyphenylglycolaldehyde + NAD+ + H2O
3,4-dihydroxyphenylglycolate + NADH + H+
Substrates: -
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?
3-chloroallylaldehyde + NAD+ + H2O
? + NADH + H+
-
Substrates: -
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?
3-chloroallylaldehyde + NADP+ + H2O
? + NADPH + H+
-
Substrates: -
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?
3-hydroxybenzaldehyde + NADP+ + H2O
3-hydroxybenzoate + NADPH + H+
-
Substrates: -
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?
3-nitrobenzaldehyde + NAD+ + H2O
3-nitrobenzoate + NADH + H+
Substrates: 32.98% of the activity compared to acetaldehyde
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?
4-bromobenzaldehyde + NAD+ + H2O
4-bromobenzoate + NADH + H+
-
Substrates: -
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?
4-carboxybenzaldehyde + NADP+ + H2O
4-carboxybenzoate + NADPH + H+
-
Substrates: -
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?
4-chlorobenzaldehyde + NADP+ + H2O
4-chlorobenzoate + NADPH + H+
-
Substrates: -
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?
4-fluorobenzaldehyde + NAD+ + H2O
4-fluorobenzoate + NADH + H+
-
Substrates: -
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?
4-formylpyrene + NADP+ + H2O
pyrene-4-carboxylic acid + NADPH + H+
Substrates: -
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?
4-hydroxy-2-nonenal + NAD(P)+ + H2O
? + NAD(P)H + H+
Substrates: -
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?
4-hydroxy-2-nonenal + NADP+ + H2O
4-hydroxy-2-nonenoic acid + NADPH + H+
-
Substrates: -
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r
4-iodobenzaldehyde + NADP+ + H2O
4-iodobenzoate + NADPH + H+
-
Substrates: -
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r
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
-
Substrates: -
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?
4-pyridinecarboxaldehyde + NAD+ + H2O
4-pyridinecarboxylate + NADH + H+
-
Substrates: -
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?
5-hydroxyindole-3-acetyldehyde + NAD+ + H2O
5-hydroxyindole-3-acetate + NADH + H+
-
Substrates: -
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?
6-methoxy-2-naphthaldehyde + NADH + H+
(6-methoxynaphthalen-2-yl)methanol + NAD+
Substrates: -
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?
acetaldehyde + 3-pyridine aldehyde adenine dinucleotide phosphate
acetate + ?
-
Substrates: -
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?
acetaldehyde + acetylpyridine adenine dinucleotide
acetate + ?
-
Substrates: -
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acetaldehyde + deamino-NAD+ + H2O
acetate + deamino-NADH + H+
-
Substrates: -
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acetaldehyde + NADP+
acetate + NADPH + H+
-
Substrates: -
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?
acetaldehyde + thio-NAD+ + H2O
acetate + thio-NADH + H+
-
Substrates: -
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?
aldophosphamide + NAD+
N,N-bis-(2-chloroethyl)-diaminophosphoric-(2-carboxyethylester) + ?
-
Substrates: -
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?
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
A0A150BLG9
Substrates: -
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?
all-trans-retinal + NADP+
all-trans-retinol + NADPH + H+
A0A150BLG9
Substrates: -
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?
all-trans-retinol + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
A0A150BLG9
Substrates: -
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all-trans-retinol + NADP+ + H2O
all-trans-retinoic acid + NADPH + H+
A0A150BLG9
Substrates: -
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?
benzaldehyde + NAD(P)+ + H2O
benzoate + NAD(P)H + H+
A0A150BLG9
Substrates: -
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?
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
Substrates: -
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?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
Substrates: 48.15% of the activity compared to acetaldehyde
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butyraldehyde + NADP+
butyrate + NADPH + H+
-
Substrates: -
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cinnamaldehyde + NAD+ + H2O
cinnamate + NADH + H+
-
Substrates: -
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cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
Substrates: -
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dihydrolipoic acid + NAD+
alpha-lipoic acid + NADH + H+
Substrates: -
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DL-glyceraldehyde + NAD(P)+ + H2O
glycerate + NAD(P)H + H+
-
Substrates: 14% of activity with benzaldehyde
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dodecanal + NADP+ + H2O
dodecanoate + NADPH + H+
-
Substrates: -
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?
glutaraldehyde + NAD+
glutarate + NADH
-
Substrates: -
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?
glyceraldehyde + NAD(P)+ + H2O
glycerate + NAD(P)H + H+
Substrates: -
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glyceraldehyde + NAD+ + H2O
glycerate + NADH + H+
-
Substrates: -
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?
glycolaldehyde + NAD+ + H2O
glycolate + NADH + H+
Substrates: 75.43% of the activity compared to acetaldehyde
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heptanal + NADP+ + H2O
heptanoate + NADPH + H+
Substrates: -
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?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
-
Substrates: -
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?
isopentanal + NAD+ + H2O
isopentanoate + NADH + H+
-
Substrates: -
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?
isovaleraldehyde + NADP+
isovalerate + NADPH + H+
-
Substrates: -
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isovaleraldehyde + NADP+ + H2O
isovalerate + NADPH + H+
Substrates: -
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malondialdehyde + NAD(P)+ + H2O
? + NAD(P)H + H+
Substrates: -
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?
n-decanal + NADP+ + H2O
n-decanoate + NADPH + H+
-
Substrates: -
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?
n-dodecanal + NADP+ + H2O
n-dodecanoate + NADPH + H+
-
Substrates: -
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?
n-hexanal + NADP+ + H2O
n-hexanoate + NADPH + H+
-
Substrates: -
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n-nonanal + NADP+ + H2O
n-nonanoate + NADPH + H+
-
Substrates: -
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n-octanal + NADP+ + H2O
n-octanoate + NADPH + H+
-
Substrates: -
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?
n-pentanal + NADP+ + H2O
n-pentanoate + NADPH + H+
-
Substrates: -
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?
n-propanal + NADP+
propionate + NADPH + H+
-
Substrates: -
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?
n-tetradecanal + NADP+ + H2O
n-tetradecanoate + NADPH + H+
-
Substrates: -
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?
n-tridecanal + NADP+ + H2O
n-tridecanoate + NADPH + H+
-
Substrates: -
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?
n-undecanal + NADP+ + H2O
n-undecanoate + NADPH + H+
-
Substrates: -
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?
p-hydroxybenzaldehyde + NADP+ + H2O
p-hydroxybenzoic acid + NADPH + H+
Substrates: -
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?
p-nitrobenzaldehyde + NADP+ + H2O
p-nitrobenzoate + NADPH + H+
Substrates: -
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?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
Substrates: -
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?
phenylacetaldehyde + NADP+ + H2O
phenylacetate + NADPH + H+
-
Substrates: -
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polyethylene glycol 1000-aldehyde + NADP+
? + NADPH
-
Substrates: -
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?
polyethylene glycol 200-aldehyde + NADP+
? + NADPH
-
Substrates: -
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polyethylene glycol 400-aldehyde + NADP+
? + NADPH
-
Substrates: -
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polyethylene glycol 4000-aldehyde + NADP+
? + NADPH
-
Substrates: highest activtiy compared to other polyethylene glycolaldehydes
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polyethylene glycol 6000-aldehyde + NADP+
? + NADPH
-
Substrates: -
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?
propanal + 1,N6-ethenoadenine dinucleotide
propionate + ?
-
Substrates: isoenzyme E1 and E2
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?
propanal + 3-acetylpyridine adenine dinucleotide
propionate + ?
-
Substrates: isoenzyme E1 and E2
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?
propanal + 3-pyridine adenine dinucleotide
propionate + ?
-
Substrates: isoenzyme E1 and E2
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?
propanal + beta-NADP+ + H2O
propionate + beta-NADPH + H+
-
Substrates: isoenzyme E1 and E2
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?
propanal + N-guanine dinucleotide
propionate + ?
-
Substrates: isoenzyme E1 and E2
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propanal + oxidized nicotinamide hypoxanthine dinucleotide + H2O
propionate + reduced nicotinamide hypoxanthine dinucleotide
-
Substrates: isoenzyme E1 and E2
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propionaldehyde + 3-pyridinealdehyde adenine dinucleotide + H2O
propionate + reduced 3-pyridinealdehyde adenine dinucleotide + H+
-
Substrates: -
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propionaldehyde + N-1,N6-ethenoadenine dinucleotide + H2O
propionate + reduced N-1,N6-ethenoadenine dinucleotide + H+
-
Substrates: -
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?
retinal + NAD+ + H2O
retinoic acid + NADH + H+
Substrates: preferred substrate of isozyme ALDH1A3
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?
succinic semialdehyde + NAD+
? + NADH
-
Substrates: -
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valeraldehyde + NADP+
valerate + NADPH + H+
-
Substrates: -
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valeraldehyde + NADP+ + H2O
valerate + NADPH + H+
Substrates: -
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2-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH + H+
-
Substrates: -
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?
2-bromobenzaldehyde + NAD+ + H2O
2-bromobenzoate + NADH + H+
-
Substrates: -
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?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
Substrates: -
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?
2-chlorobenzaldehyde + NAD+ + H2O
2-chlorobenzoate + NADH + H+
-
Substrates: -
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?
2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
-
Substrates: -
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2-fluorobenzaldehyde + NAD+ + H2O
2-fluorobenzoate + NADH + H+
-
Substrates: -
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?
3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
Substrates: -
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3-hydroxypropionaldehyde + NAD+ + H2O
3-hydroxypropanoate + NADH + 2 H+
-
Substrates: -
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acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
A0A150BLG9
Substrates: -
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acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
Substrates: -
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acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
Substrates: 51% of activity with benzaldehyde
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acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
A0A150BLG9
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
A0A150BLG9
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: activity with the enzyme from stomach mucosa, no activity with the enzyme from breast adenocarcinoma cell line
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: kcat/KM for NAD+ with acetaldehyde as cosubstrate is 2.5fold higher compared to NADP+
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acetaldehyde + NADP+ + H2O
acetate + NADPH
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
Substrates: -
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all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
A0A150BLG9
Substrates: -
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all-trans-retinal + NAD+ + H2O
all-trans-retinoic acid + NADH + H+
A0A150BLG9
Substrates: -
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all-trans-retinal + NADP+ + H2O
all-trans-retinol + NADPH + H+
A0A150BLG9
Substrates: -
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all-trans-retinal + NADP+ + H2O
all-trans-retinol + NADPH + H+
A0A150BLG9
Substrates: -
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an aldehyde + NAD(P)+ + H2O
an acid + NAD(P)H + H+
-
Substrates: -
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an aldehyde + NAD(P)+ + H2O
an acid + NAD(P)H + H+
-
Substrates: -
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an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
Substrates: -
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an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
Substrates: -
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an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
-
Substrates: -
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an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
Substrates: -
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an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
A0A150BLG9
Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
A0A150BLG9
Substrates: -
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
Substrates: pro-R specific
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: pro-R specific
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benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
Substrates: ALDH2 is very active, low activity with ALDH1 and ALDH5
Products: -
Products: -
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
Substrates: 35.5% of the activity compared to acetaldehyde
Products: -
Products: -
?
benzaldehyde + NADP+
benzoate + NADPH
-
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH
Substrates: 25% of activity with NAD+
Products: -
Products: -
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH
-
Substrates: 25% of activity with NAD+
Products: -
Products: -
ir
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
Substrates: -
Products: -
Products: -
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
butyraldehyde + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
butyraldehyde + NAD(P)+ + H2O
butanoate + NAD(P)H + H+
-
Substrates: 23% of activity with benzaldehyde
Products: -
Products: -
ir
butyraldehyde + NAD+
butyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
butyraldehyde + NAD+
butyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
Substrates: 50.25% of the activity compared to acetaldehyde. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
Products: -
Products: -
?
D-glyceraldehyde + NAD+ + H2O
D-glycerate + NADH + H+
Substrates: 50.25% of the activity compared to acetaldehyde. kcat/KM for NAD+ with D-glyceraldehyde as cosubstrate is 3.8fold higher compared to NADP+
Products: -
Products: -
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH
Substrates: 50.25% of the activity compared to acetaldehyde
Products: -
Products: -
?
D-glyceraldehyde + NADP+ + H2O
D-glycerate + NADPH
Substrates: 50.25% of the activity compared to acetaldehyde
Products: -
Products: -
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
D-glycerate 3-phosphate + NADH + H+
Substrates: 52.7% of the activity compared to acetaldehyde
Products: -
Products: -
?
D-glyceraldehyde 3-phosphate + NAD+ + H2O
D-glycerate 3-phosphate + NADH + H+
Substrates: 52.7% of the activity compared to acetaldehyde
Products: -
Products: -
?
formaldehyde + NAD(P)+ + H2O
formate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
formaldehyde + NAD(P)+ + H2O
formate + NAD(P)H + H+
-
Substrates: 52% of activity with benzaldehyde
Products: -
Products: -
ir
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + NAD+ + H2O
formate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
Substrates: -
Products: -
Products: -
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
Substrates: -
Products: -
Products: -
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
Substrates: 4% of the activity with acetaldehyde
Products: -
Products: -
?
furfuryl aldehyde + NAD+ + H2O
2-furancarboxylate + NADH + H+
-
Substrates: 4% of the activity with acetaldehyde
Products: -
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?
glycolaldehyde + NAD+
glycolate + NADH
-
Substrates: -
Products: -
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?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
glycolaldehyde + NADP+ + H2O
glycolate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
heptylaldehyde + NAD(P)+ + H2O
heptanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
heptylaldehyde + NAD(P)+ + H2O
heptanoate + NAD(P)H + H+
-
Substrates: 12% of activity with benzaldehyde
Products: -
Products: -
ir
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
hexylaldehyde + NAD(P)+ + H2O
hexanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
hexylaldehyde + NAD(P)+ + H2O
hexanoate + NAD(P)H + H+
-
Substrates: 22% of activity with benzaldehyde
Products: -
Products: -
ir
isobutanal + NAD+ + H2O
isobutyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
isobutanal + NAD+ + H2O
isobutyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
-
Substrates: 188% of activity with benzaldehyde
Products: -
Products: -
ir
isobutyraldehyde + NAD(P)+ + H2O
isobutanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
isovaleraldehyde + NAD(P)+ + H2O
isovalerate + NAD(P)H
Substrates: -
Products: -
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ir
isovaleraldehyde + NAD(P)+ + H2O
isovalerate + NAD(P)H
-
Substrates: 83% of activity with benzaldehyde
Products: -
Products: -
ir
isovaleraldehyde + NAD+
isovalerate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
isovaleraldehyde + NAD+
isovalerate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
m-bromobenzaldehyde + NAD(P)+ + H2O
m-bromobenzoate + NAD(P)H + H+
-
Substrates: 28% of activity with benzaldehyde
Products: -
Products: -
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
m-chlorobenzaldehyde + NAD(P)+ + H2O
m-chlorobenzoate + NAD(P)H + H+
-
Substrates: 35% of activity with benzaldehyde
Products: -
Products: -
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
m-fluorobenzaldehyde + NAD(P)+ + H2O
m-fluorobenzoate + NAD(P)H + H+
-
Substrates: 41% of activity with benzaldehyde
Products: -
Products: -
ir
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
Substrates: 62% of the activity with acetaldehyde
Products: -
Products: -
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
Substrates: 62% of the activity with acetaldehyde
Products: -
Products: -
?
n-butanal + NAD+ + H2O
butanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
n-butanal + NADP+ + H2O
n-butanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
n-butanal + NADP+ + H2O
n-butanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
Substrates: 55% of the activity with acetaldehyde
Products: -
Products: -
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
n-pentanal + NAD+ + H2O
n-pentanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
n-propanal + NADP+ + H2O
n-propanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
n-propanal + NADP+ + H2O
n-propanoate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
o-fluorobenzaldehyde + NAD(P)+ + H2O
o-fluorobenzoate + NAD(P)H + H+
-
Substrates: 100% of activity with benzaldehyde
Products: -
Products: -
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
o-methoxybenzaldehyde + NAD(P)+ + H2O
o-methoxybenzoate + NAD(P)H + H+
-
Substrates: 18% of activity with benzaldehyde
Products: -
Products: -
ir
octylaldehyde + NAD(P)+ + H2O
octanoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
octylaldehyde + NAD(P)+ + H2O
octanoate + NAD(P)H + H+
-
Substrates: 10% of activity with benzaldehyde
Products: -
Products: -
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
p-bromobenzaldehyde + NAD(P)+ + H2O
p-bromobenzoate + NAD(P)H + H+
-
Substrates: 14% of activity with benzaldehyde
Products: -
Products: -
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
p-chlorobenzaldehyde + NAD(P)+ + H2O
p-chlorobenzoate + NAD(P)H + H+
-
Substrates: 35% of activity with benzaldehyde
Products: -
Products: -
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
p-fluorobenzaldehyde + NAD(P)+ + H2O
p-fluorobenzoate + NAD(P)H + H+
-
Substrates: 75% of activity with benzaldehyde
Products: -
Products: -
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
p-isopropylbenzaldehyde + NAD(P)+ + H2O
p-isopropylbenzoate + NAD(P)H + H+
-
Substrates: 15% of activity with benzaldehyde
Products: -
Products: -
ir
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
Substrates: isoenzyme E1
Products: -
Products: -
?
propanal + 3-thionicotinamide adenine dinucleotide
propionate + ?
-
Substrates: no reaction with isoenzyme E2
Products: -
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?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: 88% of the activity with acetaldehyde
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: 88% of the activity with acetaldehyde
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propanal + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
ir
propionaldehyde + NAD(P)+ + H2O
propionate + NAD(P)H
Substrates: -
Products: -
Products: -
ir
propionaldehyde + NAD(P)+ + H2O
propionate + NAD(P)H
-
Substrates: 75% of activity with benzaldehyde
Products: -
Products: -
ir
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: best substrate combination
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: best substrate combination
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
Substrates: -
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
Substrates: -
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
Substrates: -
Products: -
Products: -
r
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
Substrates: 56.22% of the activity compared to acetaldehyde
Products: -
Products: -
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
Substrates: -
Products: -
Products: -
?
propionaldehyde + NADP+ + H2O
propionate + NADPH + H+
Substrates: -
Products: -
Products: -
?
valeraldehyde + NAD(P)+ + H2O
valerate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
ir
valeraldehyde + NAD(P)+ + H2O
valerate + NAD(P)H + H+
-
Substrates: 16.3% of activity with benzaldehyde
Products: -
Products: -
ir
valeraldehyde + NAD+
valerate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
valeraldehyde + NAD+
valerate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
A0A150BLG9
Substrates: no activity with 9-cis-retinal and 13-cis-retinal
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 9-cis-retinal and 13-cis-retinal
Products: -
Products: -
?
additional information
?
-
A0A150BLG9
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
A0A150BLG9
Substrates: no activity with 9-cis-retinal and 13-cis-retinal
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with formaldehyde and benzaldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: the membrane bound enzyme may act as barrier when the aldehyde concentration in cytosol is high
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme is induced during growth on tetrahydrofurfuryl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoenzyme f1 may be the primary enzyme for oxidizing the acetaldehyde produced during ethanol oxidation in vivo
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme follows a sequential mode of reaction mechanism
Products: -
Products: -
?
additional information
?
-
Substrates: 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)
Products: -
Products: -
?
additional information
?
-
-
Substrates: iol operon is involved in myo-inositol catabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme prefers aldehyde products of lipid peroxidation as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a role in oxidation of a variety of aldehydes generated by lipid metabolism
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with methanol or ethanol
Products: -
Products: -
?
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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-chloroallylaldehyde + NAD+ + H2O
? + NADH + H+
-
Substrates: -
Products: -
Products: -
?
3-chloroallylaldehyde + NADP+ + H2O
? + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
4-hydroxy-2-nonenal + NAD(P)+ + H2O
? + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD(P)+ + H2O
acetate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
ir
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
malondialdehyde + NAD(P)+ + H2O
? + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
Products: -
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
Substrates: -
Products: -
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Substrates: -
Products: -
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?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
Substrates: -
Products: -
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an aldehyde + NAD(P)+ + H2O
an acid + NAD(P)H + H+
-
Substrates: -
Products: -
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an aldehyde + NAD(P)+ + H2O
an acid + NAD(P)H + H+
-
Substrates: -
Products: -
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an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
Substrates: -
Products: -
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an aldehyde + NAD+ + H2O
a carboxylate + NADH + H+
Substrates: -
Products: -
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an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
Substrates: -
Products: -
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an aldehyde + NADP+ + H2O
a carboxylate + NADPH + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the membrane bound enzyme may act as barrier when the aldehyde concentration in cytosol is high
Products: -
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?
additional information
?
-
-
Substrates: enzyme is induced during growth on tetrahydrofurfuryl alcohol
Products: -
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?
additional information
?
-
-
Substrates: isoenzyme f1 may be the primary enzyme for oxidizing the acetaldehyde produced during ethanol oxidation in vivo
Products: -
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?
additional information
?
-
-
Substrates: enzyme plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
Substrates: ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme plays a role in oxidation of a variety of aldehydes generated by lipid metabolism
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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+
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+
additional information
A0A150BLG9
the nicotinamide moieties of NAD+ and NADP+ directly interact with the conserved catalytic residues Cys300 and Glu266, and binding causes concerted conformational changes. Flexible cofactor-binding pocket of BcALDH. Cofactor-enzyme binding structure analysis, overview
-
additional information
-
the nicotinamide moieties of NAD+ and NADP+ directly interact with the conserved catalytic residues Cys300 and Glu266, and binding causes concerted conformational changes. Flexible cofactor-binding pocket of BcALDH. Cofactor-enzyme binding structure analysis, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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
-
the enzyme does not require metal ions for its enzymatic reaction
Mg2+
20 mM, 107% of the activity compared to activity without metal ions
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one
13.7% inhibition at 0.01 mM
2,3-dimethyl-5-propyl-7H-furo[3,2-g][1]benzopyran-7-one
19.6% inhibition at 0.01 mM
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetamide
32.9% inhibition at 0.01 mM
2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoic acid
6.1% inhibition at 0.01 mM
3,4,10-trimethyl-2H,6H-benzo[1,2-b:5,4-b']dipyran-2,6-dione
20.8% inhibition at 0.01 mM
3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate
13.1% inhibition at 0.01 mM
3-tert-butyl-5,6-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
13.0% inhibition at 0.01 mM
3-thionicotinamide adenine dinucleotide
-
strong inhibition versus beta-NAD+, isoenzyme E2; substrate inhibition, isoenzyme E1
4-methyl-7-(2-oxo-2-phenylethoxy)-2H-1-benzopyran-2-one
32.9% inhibition at 0.01 mM
4-methyl-7-(2-oxopropoxy)-2H-1-benzopyran-2-one
35.9% inhibition at 0.01 mM
4-methyl-7-[(3-methylbut-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
76.4% inhibition at 0.01 mM
4-methyl-7-[(prop-2-en-1-yl)oxy]-2H-1-benzopyran-2-one
90.5% inhibition at 0.01 mM
5-benzyl-2,3-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
18.4% inhibition at 0.01 mM
6-benzyl-3,5-dimethyl-7H-furo[3,2-g][1]benzopyran-7-one
11.1% inhibition at 0.01 mM; 9.7% inhibition at 0.01 mM
6-bromo-3-[(1E)-N-hydroxyethanimidoyl]-2H-1-benzopyran-2-one
8.3% inhibition at 0.01 mM
6-methyl-3,4-dihydro-2H,8H-benzo[1,2-b:5,4-b']dipyran-2,8-dione
46.4% inhibition at 0.01 mM
8,9-dimethyl-2,3-dihydrocyclopenta[c]furo[3,2-g][1]benzopyran-4(1H)-one
12.9% inhibition at 0.01 mM
9,10-dimethyl-1,2,3,4-tetrahydro-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
5.9% inhibition at 0.01 mM
9,10-dimethyl-5H-6,8-dioxacyclopenta[b]phenanthren-5-one
6.6% inhibition at 0.01 mM
benomyl
potent irreversible inhibitor of ALDH. Benomyl increases superoxide production as much as nitroglycerin
benzoate
-
non-competitive with respect to either NAD+ or benzaldehyde
dimethyl ampal thiolester
complete inhibition of isozyme ALDH3 at 0.0075 mM
H2O2
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
kolaflavanone
-
the enzyme shows crucial non-canonical and non-catalytic interaction with kolaflavanone, a component of kolaviron, and a major bioflavonoid isolated from Garcinia kola (Bitter kola). The enzyme has one binding site for kolaflavanone with a binding constant (Ka) of 25700 l/mol and effective Forster resonance energy transfer (FRET) of 4.87 nm. The bonding process is enthalpically driven and the reaction not spontaneous. The flavonoid bonding slightly perturbed the secondary and tertiary structures of ALDH that is tryptophangated. The interaction is regulated by both diffusion and ionic strength. Kolaflavanone has a marked effect on the ellipticity of ALDH structure. Molecular docking shows that the binding of kolaflavanone is at the active site of ALDH and the participation of some amino acid residues in the complex formation. Protein-ligand interaction analysis, kinetics, detailed overview. The profiles of atomic fluctuations indicates the rigidity of the ligand-binding site during the simulation. With these, ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy. Temperature dependency of ligand-protein binding, Stern-Volmer dynamic quenching constants, and thermodynamic parameters. Binding is reduced by Na+
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
5.74% inhibition at 0.01 mM, pH 7.5, 25°C
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
6.05% inhibition at 0.01 mM, pH 7.5, 25°C
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
5.26% inhibition at 0.01 mM, pH 7.5, 25°C
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
9.09% inhibition at 0.01 mM, pH 7.5, 25°C
N-benzyl-3-(2,3,5-trimethyl-7-oxo-7H-furo[3,2-g][1]benzopyran-6-yl)propanamide
31.7% inhibition at 0.01 mM
trans-4-(N,N-dimethylamino)-cinnamaldehyde
-
1 mM, 58% inhibition; 58% inhibition at 1 mM
[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]acetonitrile
79.6% inhibition at 0.01 mM
Chloral hydrate
-
50% inhibition of isoenzyme F1 by 0.25 mM, 50% inhibition of isoenzyme F2 by 0.4 mM
Disulfiram
-
0.025 mM, 99% inhibition of activity with NADP+, 80% inhibition of activity with activity with NAD+
Disulfiram
-
0.025 mM or 0.05 mM, 99% inhibition of activity with NADP+, 60% inhibition of activity with NAD+
NADH
-
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
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
additional information
design, 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. Poor inhibition by 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-(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-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-(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-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-methoxybenzyl)-N-(1,3-dimethyl-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-3-(4-(4-isopropylbenzoyl)piperazin-1-yl)propanamide, and CM026
-
additional information
inhibition of the aldehyde dehydrogenase 1/2 family by psoralen and coumarin derivatives, structure-function relationships, overview. 3,5-dimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one, 2,3,5,6-tetramethyl-7H-furo[3,2-g][1]benzopyran-7-one, methyl 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]propanoate, 2,3,5,6,9-pentamethyl-7H-furo[3,2-g][1]benzopyran-7-one, 3,4-dimethyl-6,7,8,9-tetrahydro-2H-[1]benzofuro[3,2-g][1]benzopyran-2-one, 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one, 5-methyl-2-[(3-oxobutan-2-yl)oxy]-7H-furo[3,2-g][1]benzopyran-7-one, 7-(2-oxopropoxy)-2H-1-benzopyran-2-one, 3,4,8,9-tetramethyl-7H-furo[2,3-f][1]benzopyran-7-one, 2-[(4-methyl-2-oxo-2H-1-benzopyran-7-yl)oxy]-N-phenylacetamide, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, 3-[(3-oxobutan-2-yl)oxy]-6H-dibenzo[b,d]pyran-6-one, 3-(7-hydroxy-4-methyl-2-oxo-2H-1-benzopyran-3-yl)propanoic acid, and N-(4,7-dimethyl-2-oxo-2H-1-benzopyran-6-yl)-2-methylpropanamide are inactive as inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.007
all-trans-retinal
A0A150BLG9
with NAD+ as cosubstrate, at pH 7.0 and 37°C
0.137
n-dodecanal
-
50 mM potassium phosphate buffer pH8.0, 1 mM CaCl2, 36°C
0.001
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH2 from liver
0.0042
3,4-dihydroxyphenylacetaldehyde
isozyme ALDH1A1 from brain
0.091
4-Pyridinecarboxaldehyde
-
reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
0.19
4-Pyridinecarboxaldehyde
-
reaction with NAD+ or NADP+, enzyme from stomach mucosa
18.89
acetaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
393.4
acetaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.64
benzaldehyde
-
reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
2.95
Butyraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
4.93
Butyraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.013
Chloroacetaldehyde
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.039
Chloroacetaldehyde
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.052
Chloroacetaldehyde
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.3
Chloroacetaldehyde
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.46
Chloroacetaldehyde
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
9.87
Isovaleraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
10.78
Isovaleraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.0037
NAD+
A0A150BLG9
mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.004
NAD+
A0A150BLG9
wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.00625
NAD+
A0A150BLG9
mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.01
NAD+
A0A150BLG9
mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.048
NAD+
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.094
NAD+
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.19
NAD+
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.39
NAD+
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.1
NAD+
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
3.81
NADP+
pH and temperature not specified in the publication
0.067
octanal
-
reaction with NAD+ or NADP+, enzyme from breast adenocarcinoma cell line
0.46
propionaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.65
propionaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.12
Valeraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.34
Valeraldehyde
-
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
0.005
all-trans-retinal
A0A150BLG9
with NAD+ as cosubstrate, at pH 7.0 and 37°C
1.11
acetaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
4.46
acetaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
11.5
Butyraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
32.8
Butyraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.47
Chloroacetaldehyde
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.63
Chloroacetaldehyde
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.5
Chloroacetaldehyde
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4
Chloroacetaldehyde
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
7.7
Chloroacetaldehyde
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.91
Isovaleraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
3.58
Isovaleraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.0007
NAD+
A0A150BLG9
mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.0017
NAD+
A0A150BLG9
wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.005
NAD+
A0A150BLG9
mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.026
NAD+
A0A150BLG9
mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.47
NAD+
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.63
NAD+
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
2.5
NAD+
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4
NAD+
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
7.7
NAD+
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
13.36
propionaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
49.38
propionaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
19.41
Valeraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
30.99
Valeraldehyde
-
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
0.67
all-trans-retinal
A0A150BLG9
with NAD+ as cosubstrate, at pH 7.0 and 37°C
0.003
acetaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.24
acetaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
2.39
Butyraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
11.89
Butyraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
5.5
Chloroacetaldehyde
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
12.2
Chloroacetaldehyde
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
13.2
Chloroacetaldehyde
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
183.3
Chloroacetaldehyde
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
200
Chloroacetaldehyde
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.09
Isovaleraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.36
Isovaleraldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
0.16
NAD+
A0A150BLG9
mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.42
NAD+
A0A150BLG9
wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
0.5
NAD+
A0A150BLG9
mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
1.8
NAD+
-
mutant enzyme T244A, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
3.3
NAD+
-
mutant enzyme T244G, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
4.1
NAD+
A0A150BLG9
mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C
6.5
NAD+
-
mutant enzyme T244V, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
33.3
NAD+
-
mutant enzyme T244S, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
158.3
NAD+
-
wild type enzyme, in 25 mM Na-HEPES buffer (pH 7.4), temperature not specified in the publication
0.974
NADP+
pH and temperature not specified in the publication
20.67
propionaldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
107.5
propionaldehyde
-
with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
56.66
Valeraldehyde
-
with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C
257
Valeraldehyde
-
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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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.48
-
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
10
-
activity with NAD+, broad plateau from pH 5 to 8 followed by a sharp increase in activity to pH 10
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
pH 6.0: about 60% of maximal activity, pH 9.0: about 90% of maximal activity
6.2 - 6.7
-
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
25
36
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 90
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
-
exhibiting oxazaphosphorine-specific acquired resistance, enzyme form ALDH3
brenda
additional information
isozyme Aldh1a3 mRNA expression is highest in placenta
brenda
isozyme Aldh3a1 mRNA expression is highest in stomach
brenda
additional information
ALDH3A1 is highly expressed in lung carcinoma cell line A549 and EKVX, as well as in the large cell carcinoma cell line H460. Isozyme ALDH1A1 (EC 1.2.1.36) shows a similar expression pattern like ALDH3A1. Other members of the aldehyde dehydrogenase family are not expressed in the lung cancer cell lines examined
brenda
additional information
addition of ALDH to RASM cell homogenates significantly decreases NO consumption
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
brenda
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
aldehyde dehydrogenase 1A1 (ALDH3A1) is a member of the aldehyde dehydrogenase superfamily that oxidizes aldehydes to their corresponding acids, reactions that are coupled to the reduction of NAD(P)+ to NAD(P)H
evolution
physiological function of the regulatory mechanism for NAD+-dependent ALDHs via cysteine oxidation and vicinal disulfide formation using yeast Ald4 (EC 1.2.1.5) and Ald6. While both enzymes convert aldehyde to acetate and are important for yeast ethanol metabolism, they differ in cofactor utilization and the regulatory mechanism. Ald4 prefers NAD+ while Ald6 is NADP+-dependent. The regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction
evolution
-
physiological function of the regulatory mechanism for NAD+-dependent ALDHs via cysteine oxidation and vicinal disulfide formation using yeast Ald4 (EC 1.2.1.5) and Ald6. While both enzymes convert aldehyde to acetate and are important for yeast ethanol metabolism, they differ in cofactor utilization and the regulatory mechanism. Ald4 prefers NAD+ while Ald6 is NADP+-dependent. The regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction
-
metabolism
ALDH1A1 and ALDH3A1 have the same GSH/DHLA-dependent NAD+-reduction activity
metabolism
regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction. Isozymes Ald4, Ald5 and Ald6 play important roles in yeast survival when using ethanol as the carbon source. Both Ald4 and Ald5 preferentially use NAD+ as cofactors in cells while Ald6 only utilizes NADP+. With ethanol as the carbon source, the pentose phosphate pathway, a major pathway to generate NADPH, is shut down as the substrate is not available. Instead of cysteine, Ald6 has a serine next to the active site cysteine. As the regulatory cysteine inactivates Ald4 during oxidative stress, Ald6 remains active while Ald4 is inactivated, thus diverting all acetaldehyde to Ald6 for the production of NADPH. This way, yeast can survive oxidative stress better
metabolism
-
regulation of activity via disulfide formation between the catalytic cysteine and adjacent regulatory cysteine is only present in the NAD+-dependent Ald4, but not in the NADP+-dependent Ald6. This regulatory mechanism for Ald4 ensures the fast inactivation of Ald4 upon oxidation and the reactivation upon reduction. Isozymes Ald4, Ald5 and Ald6 play important roles in yeast survival when using ethanol as the carbon source. Both Ald4 and Ald5 preferentially use NAD+ as cofactors in cells while Ald6 only utilizes NADP+. With ethanol as the carbon source, the pentose phosphate pathway, a major pathway to generate NADPH, is shut down as the substrate is not available. Instead of cysteine, Ald6 has a serine next to the active site cysteine. As the regulatory cysteine inactivates Ald4 during oxidative stress, Ald6 remains active while Ald4 is inactivated, thus diverting all acetaldehyde to Ald6 for the production of NADPH. This way, yeast can survive oxidative stress better
-
physiological function
-
ALDH9, ALDH13, and ALDH17 genes involve the function of drought stress, acid tolerance, and pathogens infection
physiological function
isoforms ALDH3A1 plays a protective role against ultraviolet radiation-induced oxidative damage to ocular tissues, detoxifies reactive aldehydes and acts as antioxidant
physiological function
-
isotype ALDH1A1 is the key ALDH isozyme linked to tissue stem cells populations and an important contributor to cancer stem cells function in cancers
physiological function
aldehyde dehydrogenase 3A1 increases NADH levels and promotes tumor growth via glutathione/dihydrolipoic acid-dependent NAD+ reduction. ALDH3A1 can also use glutathione (GSH) and dihydrolipoic acid (DHLA) as electron donors to reduce NAD+ to NADH. The GSH/DHLA-dependent NAD+-reduction activity of ALDH1A1 is not affected by the aldehyde dehydrogenase inhibitor or by mutation of the residues in its aldehyde-binding pocket. It is thus a distinct biochemical reaction from the classic aldehyde-dehydrogenase activity catalyzed by ALDH3A1. The GSH/DHLA-dependent NAD+-reduction activity of ALDH3A1 can decrease cellular NAD+/NADH ratio and promote tumor growth
physiological function
-
enzyme ALDH is responsible for catalytic detoxification from aldehyde-induced cytotoxicity. ALDH has been reported to be involved in pseudo-ligandin properties both for nonaldehydic endobiotics and xenobiotics
physiological function
A0A150BLG9
enzyme BcALDH is an atypical aldehyde dehydrogenase having bidirectional oxidizing and reducing activities
physiological function
Ald4 converts aldehyde to acetate and are important for yeast ethanol metabolism
physiological function
-
Ald4 converts aldehyde to acetate and are important for yeast ethanol metabolism
-
Show AA Sequence and Transmembrane Helices (292 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
110000
190000
-
190000, molecular mass of the native enzyme is estimated by gel filtration, indicating that the enzyme is a homotetramer
240000
46100
52000
53000
54000
54500
46100
-
molecular weight of one subunit, determined by gel filtration on a Superdex column and by SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
tetramer
homotetramer
-
190000, molecular mass of the native enzyme is estimated by gel filtration, indicating that the enzyme is a homotetramer
homotetramer
-
190000, molecular mass of the native enzyme is estimated by gel filtration, indicating that the enzyme is a homotetramer
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.15 M DL-malic acid pH 7.0, 18% (w/v) PEG 3350
A0A150BLG9
purified recombinant BcALDH alone and in complex with NAD+ and NADP+ cofactors, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 25 mM Tris, pH 7.5, 15 mM NaCl, and 3 mM 2-mercaptoethanol, with crystallization solution containing 0.15 M DL-malic acid, pH 7.0, and 18% PEG 3350 w/v, at 14°C, 1 week, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution, molecular replacement using human ALDH2 structure (PDB ID 4FR8) as the search model, modeling. The apo-BcALDH structure contains four protomers in the asymmetric unit
A0A150BLG9
the apoenzyme is crystallized by using 100 mM ACES, pH 6.4, 100-200 mM guanidine-HCl, 1-10 mM MgCl2 and 1617% (w/v) PEG 6000, the mutant T244A in complex with NAD is crystallized by using 100 mM ACES, pH 6.4, 100 mM guanidineHCl, 10 mM MgCl2 and 18% (w/v) PEG 6000
-
ALDHC in complex with NADPH bound in the cofactor binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel, to 1.6 A resolution. Belongs to space group P1. The ALDHC monomer comprises three distinct domains, an N-terminal cofactor (NAD/P+)-binding domain, a catalytic domain, and an oligomerization domain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E194S
A0A150BLG9
the variant shows 15fold higher catalytic efficiency (kcat/Km) for the reduction of all-trans-retinal than the wild type enzyme
E457V
A0A150BLG9
the variant shows 7.5fold higher catalytic efficiency (kcat/Km) for the reduction of all-trans-retinal than the wild type enzyme
E194S
-
the variant shows 15fold higher catalytic efficiency (kcat/Km) for the reduction of all-trans-retinal than the wild type enzyme
-
E457V
-
the variant shows 7.5fold higher catalytic efficiency (kcat/Km) for the reduction of all-trans-retinal than the wild type enzyme
-
T186S
the mutant has increased activity against aldehyde and decreased activity against smaller substrates like benzaldehyde compared to the native enzyme and cells transformed with the point mutant are better protected against the killing effect of cyclophosphamides
T244A
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244G
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244S
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
T244V
-
the mutant exhibits reduced catalytic efficiency toward substrate and coenzyme
E140D
-
Km-value for NADP+ is about half that of the native enzyme, Km-value for NAD+ is about 3.1fold that of the native enzyme, Km-value for benzaldehyde is about 1.4fold that of the native enzyme, Km-value for propanal is about 1.9fold that of the native enzyme. The coenzyme preference NADP+/NAD+ is 3.2, compared to 3.4 for the native enzyme
E140N
-
Km-value for NADP+ is about 10% of that of the native enzyme, Km-value for NAD+ is about 3.2fold that of the native enzyme, Km-value for benzaldehyde is about 1.2fold that of the native enzyme, Km-value for propanal is about 2.3fold that of the native enzyme. The coenzyme preference NADP+/NAD+ is 4.2, compared to 3.4 for the native enzyme
E140Q
-
Km-value for NADP+ is about 10% of that of the native enzyme, Km-value for NAD+ is about 7.9fold that of the native enzyme, Km-value for benzaldehyde is about 1.6fold that of the native enzyme, Km-value for propanal is about 1.1fold that of the native enzyme. The coenzyme preference NADP+/NAD+ is 2.8, compared to 3.4 for the native enzyme
E140T
-
Km-value for NADP+ is about 20% of that of the native enzyme, Km-value for NAD+ is about 15.3fold that of the native enzyme, Km-value for benzaldehyde is about 60% of that of the native enzyme, Km-value for propanal is about 1.4fold that of the native enzyme. The coenzyme preference NADP+/NAD+ is 5.8, compared to 3.4 for the native enzyme
G192A
-
Km-value for NADP+ is about half that of the native enzyme, Km-value for NAD+ is about 70% of that of the native enzyme, Km-value for benzaldehyde is about 90% of that of the native enzyme, Km-value for propanal is about 45% of that of the native enzyme
K137Q
-
Km-value for NADP+ is about 2.4fold that of the native enzyme, Km-value for NAD+ is about 16fold that of the native enzyme, Km-value for benzaldehyde is about 1.2fold that of the native enzyme, Km-value for propanal is about 95% of that of the native enzyme. The coenzyme preference NADP+/NAD+ is 1.1, compared to 3.4 for the native enzyme
C325S
additional information
C325S
site-directed mutagenesis, the mutant strain is more sensitive against H2O2 treatment than the wild-type and shows lower NADPH concentration
C325S
-
site-directed mutagenesis, the mutant strain is more sensitive against H2O2 treatment than the wild-type and shows lower NADPH concentration
-
additional information
simultaneous knockout of ALDH1A1 (EC 1.2.1.36) and its isozyme ALDH3A1 in lung cancer cell line NCI-H460 inhibits tumor growth in a xenograft model. Moreover, the ALDH1A1 mutants that retain their GSH/DHLA-dependent NAD+ reduction activity and lose their aldehyde-dehydrogenase activity are able to decrease the NAD+/NADH ratio and to rescue the impaired growth of ALDH1A1/3A1 double knockout tumor cells
additional information
construction of an Ald4 knockout (DELTAald4) strain, the mutant strain is more sensitive against H2O2 treatment than the wild-type
additional information
-
construction of an Ald4 knockout (DELTAald4) strain, the mutant strain is more sensitive against H2O2 treatment than the wild-type
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6
-
pH 6.0 attenuates more than 39% of enzymatic activity. At pH 5.0, 3% of the activity remains. The enzymatic activity is completely abolished at pH values of or below 4.0
7.4
the activity at a physiological pH value (7.4) is nearly 50% of the activity observed at the optimal pH value
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
-
the enzyme appears to be stable at 20°C, but becomes very unstable at a temperature above 37°C, most likely due to thermal denaturation
25
50
55
70 - 80
about 20% increase of activity after treatment at 70 and 80°C for 2 h, probably due to thermal activation of the enzyme
90
half-life: 4 h. Significant protection against thermal inactivation by 1 mM NAD+ or NADP+ when the preheating time is above 4 h at 90°C
additional information
coenzyme NAD+ or NADP+ can regulate the enzymatic thermostability
25
-
90 min, about 80% loss of activity without a stabilizer, about 20% loss of activity in presence of 24% v/v of ethanediol
25
-
60 min, about 60% loss of activity without stabilizer, about 10% loss of activity in presence of 5 mM NAD+
25
-
70 min, about 80% loss of activity without stabilizer, about 15% loss of activity in presence of 50 mM KCl
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing, more than once causes complete loss of activity of enzyme from breast adenocarcinoma cell line, enzyme from stomach mucosa retains 40% of its activity even after being frozen and thawed eight times
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
Ethylene glycol
isopropanol
Methanol
SDS
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM potassium phosphate, pH 7.0, several months, no loss of activity
-25°C, 50 mM potassium phosphate, pH 6.8, 2 mM 2-mercaptoethanol, 1 mM EDTA, 2 mM propionic acid, 0.6 mM PMSF, stable for at least 3 months
-
4°C, pH 7.5, 25 mM sodium phosphate supplemented with 1 mM EDTA and 0.05% dithiothreitol, 10% glycerol, enzyme from breast adenocarcinoma cell line completely loses activity after 15 days, enzyme from stomach mucosa loses 75% of its activity after 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, 5-AMP Sepharose 4B and 4-hydroxyacetophenone affinity chromatography
-
purification of the enzyme(s) responsible for the GSH/DHLA-dependent NAD+ reduction activity from large-scale cell cultures, native enzyme from EKVX lung cancer cells by ultracentrifugation of crude cell extract and anion echange chromatography, hydrophobic interaction and hydroxyapatite chromatography, followed by gel filtration and another different step of anion exchange chromatography
recombinant tagged enzyme from Escherichia coli strain ER2566 by metal chelating affinity chromatography, desalting gel filtration, and dialysis
A0A150BLG9
to homogeneity by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a hexa-histidine-tagged fusion in Escherichia coli BL21 Star (DE3)
expressed in Escherichia coli ER2566 cells
expression as His-tag fusion protein in Echerichia coli Rosetta (DE3) pLys
-
expression in Escherichia coli
gene ald4, recombinant expression of wild-type Ald4 and mutant Ald4 C325S enzymes, as well as Ald4 knockout (DELTAald4) strain under the original promoter of Ald4
into the pGEM-T easy vector for sequencing
recombinant tagged enzyme expression in Escherichia coli strain ER2566
A0A150BLG9
the pegC gene of Sphingomonas macrogoltabidus is cloned into the pGEM-T and pET23d vectors for expression of nicotinprotein aldehyde dehydrogenase in Escherichia coli Rosetta DE3 pLysS
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aldehyde dehydrogenase 1A3 is transcriptionally activated by 0.001 mM all-trans-retinoic acid in human epidermal keratinocytes whereas no upregulation is detected in dermal fibroblasts and HeLa cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
ALDH is hereby proposed as a subtle nanoparticle determinant of kolaviron bioavailability and efficacy
degradation
energy production
-
preparation of a bioanode for use in ethanol oxidation. The bioanode is obtained via immobilization of dehydrogenase enzymes (alcohol dehydrogenase or aldehyde dehydrogenase) with polyamidoamine dendrimers onto carbon paper platforms, using the layer-by-layer technique. The prepared bioanode proves to be capable of producing good power density values
medicine
synthesis
additional information
medicine
-
19 ALDH genes are identified in the human genome and mutations in these genes and subsequent inborn errors in aldehyde metabolism are the molecular basis of several diseases, including Sjögren-Larsson syndrome, type II hyperprolinemia, gamma-hydroxybutyric aciduria and pyridoxine-dependent seizures. ALDH enzymes also play important roles in embryogenesis and development, neurotransmission, oxidative stress and cancer. ALDH enzymes display multiple catalytic and non-catalytic functions including ester hydrolysis, antioxidant properties, xenobiotic bioactivation and UV light absorption
medicine
-
high ALDH1 activity and ALDH1A1 overexpression are associated with poor cancer prognosis
synthesis
-
titer and yield of 3-hydroxypropionic acid are improved to 54.7 mmol/l and 67% (mol/mol), respectively, when an ALDH gene (puuC) from Klebsiella pneumoniae is overexpressed in Pseudomonas denitrificans strain ATCC 13867
synthesis
A0A150BLG9
the enzyme can be useful in the production of retinoic acid and related high-end products
synthesis
-
titer and yield of 3-hydroxypropionic acid are improved to 54.7 mmol/l and 67% (mol/mol), respectively, when an ALDH gene (puuC) from Klebsiella pneumoniae is overexpressed in Pseudomonas denitrificans strain ATCC 13867
-
additional information
reduced ALDH-2 activity and expression leads to decreased nitroglycerin bioconversion. ALDH is an important physiological inhibitory factor of superoxide production
additional information
-
ALDH2 may have antioxidant properties. Yeast ALDH significantly and dose-dependently attenuates HX/XO-generated O2S- signal
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Izaguirre, G.; Pietruszko, R.; Cho, S.; MacKerell, A.D., Jr.
Human aldehyde dehydrogenase catalytic activity and structural interactions with coenzyme analogs
J. Biomol. Struct. Dyn.
19
429-447
2001
Homo sapiens
brenda
Downes, J.E.; Holmes, R.S.
Purification and properties of murine corneal aldehyde dehydrogenase
Biochem. Mol. Biol. Int.
30
525-535
1993
Mus musculus
brenda
Choi, S.D.; Joo, C.N.
Purification and characterization of the bovine cerebral mitochondrial aldehyde dehydrogenase
Korean Biochem. J.
24
224-230
1991
Bos taurus
-
brenda
King, G.; Holmes, R.S.
Human corneal aldehyde dehydrogenase: purification, kinetic characterisation and phenotypic variation
Biochem. Mol. Biol. Int.
31
49-63
1993
Homo sapiens
brenda
Wang, X.; Mann, C.J.; Bai, Y.; Ni, L.; Weiner, H.
Molecular cloning, characterization, and potential roles of cytosolic and mitochondrial aldehyde dehydrogenases in ethanol metabolism in Saccharomyces cerevisiae
J. Bacteriol.
180
822-830
1998
Saccharomyces cerevisiae
brenda
Sreerama, L.; Sladek, N.E.
Identification and characterization of a novel class 3 aldehyde dehydrogenase overexpressed in a human breast adenocarcinoma cell line exhibiting oxazaphosphorine-specific acquired resistance
Biochem. Pharmacol.
45
2487-2505
1993
Homo sapiens
brenda
Senior, d.J.; Tasi, C.S.
Purification and characterization of aldehyde dehydrogenase from rat liver mitochondria
Arch. Biochem. Biophys.
262
211-220
1988
Rattus norvegicus
brenda
Evces, S.; Lindahl, R.
Characterization of rat cornea aldehyde dehydrogenase
Arch. Biochem. Biophys.
274
518-524
1989
Rattus norvegicus
brenda
Jeng, J.; Weiner, H.
Purification and characterization of catalytically active precursor of rat liver mitochondrial aldehyde dehydrogenase expressed in Escherichia coli
Arch. Biochem. Biophys.
289
214-222
1991
Rattus norvegicus
brenda
Rietveld, E.C.; de Zwart, M.; Cox, P.G.F.; Seutter-Berlage, F.
Substituent effects during the rat liver aldehyde dehydrogenase catalyzed oxidation of aromatic aldehydes
Biochim. Biophys. Acta
914
162-169
1987
Rattus norvegicus, Saccharomyces cerevisiae
brenda
Lindahl, R.; Baggett, D.W.; Winters, A.L.
Characterization of aldehyde dehydrogenase from HTC rat hepatoma cells
Biochim. Biophys. Acta
843
180-185
1985
Rattus norvegicus
brenda
Eckfeldt, J.H.; Yonetani, T.
Isozymes of aldehyde dehydrogenase from horse liver
Methods Enzymol.
89
474-479
1982
Equus caballus
brenda
Tamaki, N.; Hama, T.
Aldehyde dehydrogenase from bakers yeast
Methods Enzymol.
89
469-473
1982
Saccharomyces cerevisiae
brenda
Tamaki, N.; Nakamura, M.; Kimura, K.; Hama, T.
Purification and properties of aldehyde dehydrogenase from Saccharomyces cerevisiae
J. Biochem.
82
73-79
1977
Saccharomyces cerevisiae
brenda
Bostian, K.A.; Betts, G.F.
Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae
Biochem. J.
173
787-798
1978
Saccharomyces cerevisiae
brenda
Eckfeldt, J.; Mope, L.; Takio, K.; Yonetani, T.
Horse liver aldehyde dehydrogenase. Purification and characterization of two isozymes
J. Biol. Chem.
251
236-240
1976
Equus caballus
brenda
Perozich, J.; Kuo, I.; Wang, B.C.; Boesch, J.S.; Hempel, J.
Shifting the NAD/NADP preference in class 3 aldehyde dehydrogenase
Eur. J. Biochem.
267
6197-6203
2000
Rattus norvegicus
brenda
Schraeder, T.; Zernt, G.; Andreesen, J.R.
NAD(P)-dependent aldehyde dehydrogenase induced during growth of Ralstonia eutropha strain Bo on tetrahydrofurfuryl alcohol
J. Bacteriol.
183
7408-7411
2001
Cupriavidus necator, Cupriavidus necator Bo
brenda
Yamanaka, Y.; Kazuoka, T.; Yoshida, M.; Yamanaka, K.; Oikawa, T.; Soda, K.
Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties
Biochem. Biophys. Res. Commun.
298
632-637
2002
Cytophaga sp. (Q8KZT4)
brenda
Boubekeur, S.; Camougrand, N.; Bunoust, O.; Rigoulet, M.; Guerin, B.
Participation of acetaldehyde dehydrogenases in ethanol and pyruvate metabolism of the yeast Saccharomyces cerevisiae
Eur. J. Biochem.
268
5057-5065
2001
Saccharomyces cerevisiae
brenda
Oikawa, T.; Kazuoka, T.; Soda, K.
Paradoxical thermostable enzymes from psychrophile: molecular characterization and potentiality for biotechnological application
J. Mol. Catal. B
23
65-70
2003
Cytophaga sp.
-
brenda
Ohta, T.; Tani, A.; Kimbara, K.; Kawai, F.
A novel nicotinoprotein aldehyde dehydrogenase involved in polyethylene glycol degradation
Appl. Microbiol. Biotechnol.
68
639-646
2005
Sphingopyxis macrogoltabida, Sphingopyxis macrogoltabida 103
brenda
Maestre, O.; Garcia-Martinez, T.; Peinado, R.A.; Mauricio, J.C.
Effects of ADH2 overexpression in Saccharomyces bayanus during alcoholic fermentation
Appl. Environ. Microbiol.
74
702-707
2008
Lacticaseibacillus casei BL23
brenda
Glatt, H.; Rost, K.; Frank, H.; Seidel, A.; Kollock, R.
Detoxification of promutagenic aldehydes derived from methylpyrenes by human aldehyde dehydrogenases ALDH2 and ALDH3A1
Arch. Biochem. Biophys.
477
196-205
2008
Homo sapiens (P30838)
brenda
Ho, K.K.; Mukhopadhyay, A.; Li, Y.F.; Mukhopadhyay, S.; Weiner, H.
A point mutation produced a class 3 aldehyde dehydrogenase with increased protective ability against the killing effect of cyclophosphamide
Biochem. Pharmacol.
76
690-696
2008
Homo sapiens (P30838), Homo sapiens
brenda
Quash, G.; Fournet, G.; Courvoisier, C.; Martinez, R.M.; Chantepie, J.; Paret, M.J.; Pharaboz, J.; Joly-Pharaboz, M.O.; Gore, J.; Andre, J.; Reichert, U.
Aldehyde dehydrogenase inhibitors: alpha,beta-acetylenic N-substituted aminothiolesters are reversible growth inhibitors of normal epithelial but irreversible apoptogens for cancer epithelial cells from human prostate in culture
Eur. J. Med. Chem.
43
906-916
2008
Homo sapiens (P30838), Homo sapiens
brenda
Bajns J., Boulanger MJ.
Structural and biochemical characterization of a novel aldehyde dehydrogenase encoded by the benzoate oxidation pathway in Burkholderia xenovorans LB400
J. Mol. Biol.
379
597-608
2008
Paraburkholderia xenovorans LB400 (Q13WK4), Paraburkholderia xenovorans (Q13WK4)
brenda
Szoecs, K.; Lassegue, B.; Wenzel, P.; Wendt, M.; Daiber, A.; Oelze, M.; Meinertz, T.; Muenzel, T.; Baldus, S.
Increased superoxide production in nitrate tolerance is associated with NAD(P)H oxidase and aldehyde dehydrogenase 2 downregulation
J. Mol. Cell. Cardiol.
42
1111-1118
2007
Rattus norvegicus (P11884), Saccharomyces cerevisiae
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 (P30838), Homo sapiens (P47895), Homo sapiens (P43353)
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 (Q9JHW9), Mus musculus (P47739), Mus musculus (Q80VQ0)
brenda
Marchitti, S.A.; Brocker, C.; Stagos, D.; Vasiliou, V.
Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily
Expert. Opin. Drug Metab. Toxicol.
4
697-720
2008
Homo sapiens
brenda
Gao, C.; Han, B.
Evolutionary and expression study of the aldehyde dehydrogenase (ALDH) gene superfamily in rice (Oryza sativa)
Gene
431
86-94
2009
Oryza sativa, Oryza sativa (Q9FRX7), Oryza sativa (Q6H627), Oryza sativa (Q0DZ46), Oryza sativa (Q7XR89), Oryza sativa (Q53NG8), Oryza sativa (Q69P84), Oryza sativa (Q9LRE9), Oryza sativa (Q9LRI6)
brenda
Koenig, U.; Amatschek, S.; Mildner, M.; Eckhart, L.; Tschachler, E.
Aldehyde dehydrogenase 1A3 is transcriptionally activated by all-trans-retinoic acid in human epidermal keratinocytes
Biochem. Biophys. Res. Commun.
400
207-211
2010
Homo sapiens (P47895)
brenda
Stagos, D.; Chen, Y.; Cantore, M.; Jester, J.V.; Vasiliou, V.
Corneal aldehyde dehydrogenases: multiple functions and novel nuclear localization
Brain Res. Bull.
81
211-218
2010
Mus musculus (Q9JHW9)
brenda
Liu, T.; Hao, L.; Wang, R.; Liu, B.
Molecular characterization of a thermostable aldehyde dehydrogenase (ALDH) from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7
Extremophiles
17
181-190
2013
Sulfurisphaera tokodaii (Q976X5), Sulfurisphaera tokodaii 7 (Q976X5)
brenda
Ngo, H.P.; Hong, S.H.; Oh, D.K.; Kang, L.W.
Expression, crystallization and preliminary X-ray crystallographic analysis of aldehyde dehydrogenase (ALDH) from Bacillus cereus
Acta Crystallogr. Sect. F
69
528-531
2013
Bacillus cereus (A0A150BLG9), Bacillus cereus ATCC 10876 (A0A150BLG9)
brenda
Zhou, S.; Catherine, C.; Rathnasingh, C.; Somasundar, A.; Park, S.
Production of 3-hydroxypropionic acid from glycerol by recombinant Pseudomonas denitrificans
Biotechnol. Bioeng.
110
3177-3187
2013
Klebsiella pneumoniae, Klebsiella pneumoniae DSM 2026
brenda
Gonzalez-Segura, L.; Ho, K.K.; Perez-Miller, S.; Weiner, H.; Hurley, T.D.
Catalytic contribution of threonine 244 in human ALDH2
Chem. Biol. Interact.
202
32-40
2013
Homo sapiens
brenda
Zhou, M.L.; Zhang, Q.; Zhou, M.; Qi, L.P.; Yang, X.B.; Zhang, K.X.; Pang, J.F.; Zhu, X.M.; Shao, J.R.; Tang, Y.X.; Wu, Y.M.
Aldehyde dehydrogenase protein superfamily in maize
Funct. Integr. Genomics
12
683-691
2012
Zea mays
brenda
Lo, H.F.; Chen, Y.J.
Gene cloning and biochemical characterization of a NAD(P)+ -dependent aldehyde dehydrogenase from Bacillus licheniformis
Mol. Biotechnol.
46
157-167
2010
Bacillus licheniformis, Bacillus licheniformis ATCC 14580
brenda
Alam, M.F.; Laskar, A.A.; Choudhary, H.H.; Younus, H.
Human salivary aldehyde dehydrogenase: purification, kinetic characterization and effect of ethanol, hydrogen peroxide and sodium dodecyl sulfate on the activity of the enzyme
Cell Biochem. Biophys.
74
307-315
2016
Homo sapiens (P30838)
brenda
Hong, S.H.; Ngo, H.P.; Nam, H.K.; Kim, K.R.; Kang, L.W.; Oh, D.K.
Alternative biotransformation of retinal to retinoic acid or retinol by an aldehyde dehydrogenase from Bacillus cereus
Appl. Environ. Microbiol.
82
3940-3946
2016
Bacillus cereus (A0A150BLG9), Bacillus cereus, Bacillus cereus ATCC 10876 (A0A150BLG9)
brenda
Mali, V.R.; Deshpande, M.; Pan, G.; Thandavarayan, R.A.; Palaniyandi, S.S.
Impaired ALDH2 activity decreases the mitochondrial respiration in H9C2 cardiomyocytes
Cell. Signal.
28
1-6
2016
Rattus norvegicus
brenda
Gonzalez-Segura, L.; Riveros-Rosas, H.; Julian-Sanchez, A.; Munoz-Clares, R.A.
Residues that influence coenzyme preference in the aldehyde dehydrogenases
Chem. Biol. Interact.
234
59-74
2015
Sulfurisphaera tokodaii (Q976X5), Sulfurisphaera tokodaii DSM 16993 (Q976X5)
brenda
Tomita, H.; Tanaka, K.; Tanaka, T.; Hara, A.
Aldehyde dehydrogenase 1A1 in stem cells and cancer
Oncotarget
7
11018-11032
2016
Homo sapiens
brenda
Jimenez-Lopez, J.
Narrow-leafed lupin (Lupinus angustifolius L.) functional identification and characterization of the aldehyde dehydrogenase (ALDH) gene superfamily
Plant Gene
6
67-76
2016
Lupinus angustifolius
-
brenda
Aquino Neto, S.; Forti, J.; Zucolotto, V.; Ciancaglini, P.; de Andrade, A.
Development of nanostructured bioanodes containing dendrimers and dehydrogenases enzymes for application in ethanol biofuel cells
Biosens. Bioelectron.
26
2922-2926
2011
Saccharomyces cerevisiae
brenda
Zhang, Y.; Wang, M.; Lin, H.
A regulatory cysteine residue mediates reversible inactivation of NAD+-dependent aldehyde dehydrogenases to promote oxidative stress response
ACS Chem. Biol.
15
28-32
2020
Saccharomyces cerevisiae (P46367), Saccharomyces cerevisiae ATCC 204508 (P46367)
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 (P30838)
brenda
Kolawole, A.N.; Akinladejo, V.T.; Elekofehinti, O.O.; Akinmoladun, A.C.; Kolawole, A.O.
Experimental and computational modeling of interaction of kolaviron-kolaflavanone with aldehyde dehydrogenase
Bioorg. Chem.
78
68-79
2018
Saccharomyces cerevisiae
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), Bacillus cereus
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 (P30838)
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 (P30838)
brenda
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