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2-hexenal + NAD+ + H2O
2-hexenoate + NADH + H+
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
-
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropionate + NADH + H+
-
-
-
?
4-(dimethylamino)butyraldehyde + NAD+ + H2O
4-(dimethylamino)butyrate + NADH + 2 H+
-
-
-
?
4-(trimethylamino)butyraldehyde + NAD+ + H2O
4-(trimethylamino)butyrate + NADH + 2 H+
preferred substrate
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutyrate + NADH + H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
-
-
-
?
4-dimethylaminobutyraldehyde + NAD+
4-dimethylaminobutanoate + NADH
4-dimethylaminobutyraldehyde + NAD+ + H2O
? + NADH + H+
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+
4-N-trimethylaminobutanoate + NADH
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
4-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
4-trimethylaminobutyraldehyde + NADP+ + H2O
4-trimethylaminobutyrate + NADPH + H+
-
-
-
r
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
aminobutyraldehyde + NAD+ + H2O
aminobutyrate + NADH + H+
betaine aldehyde + NAD+
betaine + NADH
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
butyraldehyde + NAD+
butyrate + NADH
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
-
-
-
?
gamma-aminobutyraldehyde + NAD+
gamma-aminobutyrate + NADH
gamma-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
heptanal + NAD+
heptanoate + NADH
-
-
?
hexadecanal + NAD+
hexadecanoate + NADH
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
N,N,N-trimethyl-3-aminopropionate + NADH + H+
-
-
-
?
N,N-dimethyl-3-aminopropionaldehyde + NAD+ + H2O
N,N-dimethyl-3-aminopropionate + NADH + H+
-
-
-
?
octanal + NAD+ + H2O
octanoate + NADH + H+
-
-
?
pentanal + NAD+
pentanoate + NADH
-
-
?
propionaldehyde + NAD+
propionate + NADH
trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + 2 H+
enzyme is involved in L-carnitine (3-hydroxy-4-N-trimethylaminobutyrate) biosynthesis
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
-
-
-
?
additional information
?
-
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
a dopamine metabolite
-
-
?
4-dimethylaminobutyraldehyde + NAD+
4-dimethylaminobutanoate + NADH
-
-
-
-
?
4-dimethylaminobutyraldehyde + NAD+
4-dimethylaminobutanoate + NADH
-
-
-
-
?
4-dimethylaminobutyraldehyde + NAD+ + H2O
? + NADH + H+
-
-
-
?
4-dimethylaminobutyraldehyde + NAD+ + H2O
? + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+
4-N-trimethylaminobutanoate + NADH
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+
4-N-trimethylaminobutanoate + NADH
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
function in carnitine biosynthesis
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
-
?
4-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
strongly preferred substrate
-
-
?
4-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
a carnitine precursor
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
low activity
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
?
aminobutyraldehyde + NAD+ + H2O
aminobutyrate + NADH + H+
-
-
-
?
aminobutyraldehyde + NAD+ + H2O
aminobutyrate + NADH + H+
a GABA precursor
-
-
?
butyraldehyde + NAD+
butyrate + NADH
-
low activity
-
?
butyraldehyde + NAD+
butyrate + NADH
-
-
?
butyraldehyde + NAD+
butyrate + NADH
-
-
?
gamma-aminobutyraldehyde + NAD+
gamma-aminobutyrate + NADH
-
-
?
gamma-aminobutyraldehyde + NAD+
gamma-aminobutyrate + NADH
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
?
propionaldehyde + NAD+
propionate + NADH
-
low activity
-
?
propionaldehyde + NAD+
propionate + NADH
-
-
?
propionaldehyde + NAD+
propionate + NADH
-
-
?
additional information
?
-
ALDH9A1 exhibits wide substrate specificity to aminoaldehydes, aliphatic and aromatic aldehydes with a clear preference for gamma-trimethylaminobutyraldehyde (TMABAL). The enzyme is multifunctional also catalyzing the reactions of EC 1.2.1.3 and EC 1.2.1.19. Substrate specificity, overview
-
-
-
additional information
?
-
-
ALDH9A1 exhibits wide substrate specificity to aminoaldehydes, aliphatic and aromatic aldehydes with a clear preference for gamma-trimethylaminobutyraldehyde (TMABAL). The enzyme is multifunctional also catalyzing the reactions of EC 1.2.1.3 and EC 1.2.1.19. Substrate specificity, overview
-
-
-
additional information
?
-
diethylaminobenzaldehyde (DEAB) is not a substrate for ALDH9A1
-
-
-
additional information
?
-
-
diethylaminobenzaldehyde (DEAB) is not a substrate for ALDH9A1
-
-
-
additional information
?
-
-
does not degradate 4-trimethylaminobutanol, betaine aldehyde, 4-aminobutyraldehyde, acetaldehyde, propionaldehyde, butyraldehyde, trimethylacetaldehyde, and 3-methylbutyraldehyde
-
-
?
additional information
?
-
no activity with NADP+, trimethylaminobutanol, 3-N-trimethylaminopropionaldehyde, betaine aldehyde, 4-aminobutyraldehyde, and other aliphatic aldehydes such as acetaldehyde, propionaldehyde, butyraldehyde, pivaleraldehyde, isovaleraldehyde, butyraldehyde, trimethylacetaldehyde, and 3-methylbutyraldehyde
-
-
?
additional information
?
-
-
no activity with NADP+, trimethylaminobutanol, 3-N-trimethylaminopropionaldehyde, betaine aldehyde, 4-aminobutyraldehyde, and other aliphatic aldehydes such as acetaldehyde, propionaldehyde, butyraldehyde, pivaleraldehyde, isovaleraldehyde, butyraldehyde, trimethylacetaldehyde, and 3-methylbutyraldehyde
-
-
?
additional information
?
-
-
does not degradate 4-trimethylaminobutanol, betaine aldehyde, 4-aminobutyraldehyde, acetaldehyde, propionaldehyde, butyraldehyde, trimethylacetaldehyde, and 3-methylbutyraldehyde
-
-
?
additional information
?
-
no activity with NADP+, trimethylaminobutanol, 3-N-trimethylaminopropionaldehyde, betaine aldehyde, 4-aminobutyraldehyde, and other aliphatic aldehydes such as acetaldehyde, propionaldehyde, butyraldehyde, pivaleraldehyde, isovaleraldehyde, butyraldehyde, trimethylacetaldehyde, and 3-methylbutyraldehyde
-
-
?
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3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
a dopamine metabolite
-
-
?
4-(trimethylamino)butyraldehyde + NAD+ + H2O
4-(trimethylamino)butyrate + NADH + 2 H+
preferred substrate
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
4-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
a carnitine precursor
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
aminobutyraldehyde + NAD+ + H2O
aminobutyrate + NADH + H+
a GABA precursor
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
-
-
-
?
trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + 2 H+
enzyme is involved in L-carnitine (3-hydroxy-4-N-trimethylaminobutyrate) biosynthesis
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutanoate + NADH + H+
-
-
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
function in carnitine biosynthesis
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
-
?
4-trimethylaminobutyraldehyde + NAD+
4-trimethylaminobutyrate + NADH + H+
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
-
?
4-trimethylammoniobutanal + NAD+ + H2O
4-trimethylammoniobutanoate + NADH + 2 H+
-
-
-
?
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1,10-phenanthroline
-
1 mM causes 5% inhibition at 30°C
3-methylbutyraldehyde
-
1 mM causes 57% inhibition at 30°C
4-(dimethylamino)butyraldehyde
-
-
4-(trimethylamino)butyraldehyde
-
-
4-chloromercuribenzoate
-
4-guanidinobutyraldehyde
-
4-N-trimethylaminobutyraldehyde
-
the substrate inhibits at 0.24 mM
5,5'-dithiobis-(2-nitrobenzoic acid)
acetaldehyde
-
1 mM causes 18% inhibition at 30°C
Betaine aldehyde
-
1 mM causes 41% inhibition at 30°C
diethylaminobenzaldehyde
DEAB, the broad-spectrum ALDH inhibitor reversibly inhibits ALDH9A1 in a time-dependent manner by a covalent reversible mechanism of inhibition, mechanism analysis, overview
diethylmethylamine
-
at 30°C, 5 mM causes 53% inhibition, does not inhibit at 1 mM
dimethylethylamine
-
5 mM causes 9% inhibition at 30°C
ethylmethylamine
-
1 mM causes 20% inhibition at 30°C
glyceraldehyde
-
1 mM causes 7% inhibition at 30°C
KCl
-
1 mM causes 5% inhibition at 30°C
N,N,N-trimethyl-3-aminopropionaldehyde
-
p-chloromercuribenzoate
-
0.1 mM causes 88% inhibition at 30°C
phenylacetaldehyde
-
0.1 mM causes 54% inhibition at 30°C
triethylamine
-
5 mM causes 42% inhibition at 30°C
trimethylacetaldehyde
-
1 mM causes 80% inhibition at 30°C
5,5'-dithiobis-(2-nitrobenzoic acid)
-
0.1 mM causes 100% inhibition at 30°C
5,5'-dithiobis-(2-nitrobenzoic acid)
-
Ba2+
-
1 mM causes 30% inhibition at 30°C
Co2+
-
1 mM causes 18% inhibition at 30°C
Cu2+
-
0.05 mM causes 36% inhibition at 30°C
Disulfiram
-
-
Hg2+
-
0.05 mM causes 28% inhibition at 30°C
iodoacetoamide
-
1 mM causes 42% inhibition at 30°C
Li+
-
1 mM causes 13% inhibition at 30°C
Semicarbazide
-
1 mM causes 22% inhibition at 30°C
Zn2+
-
1 mM causes 11% inhibition at 30°C
additional information
the enzyme shows substrate inhibition
-
additional information
-
the enzyme shows substrate inhibition
-
additional information
-
at 30°C, not inhibited by Rb+, Na+, Mg2+, Ca2+, potassium fluoride, 1 mM sodium azide, 2,2'-dipyridyl, EDTA, 1 mM trimethylamine and 1 mM tetramethylammonium chloride
-
additional information
potassium fluoride, sodium azide, 2,2'-dipyridyl, and EDTA have no effect on the enzyme activity
-
additional information
-
potassium fluoride, sodium azide, 2,2'-dipyridyl, and EDTA have no effect on the enzyme activity
-
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0.026
2-hexenal
pH 7.5, temperature not specified in the publication
0.011
3,4-dihydroxyphenylacetaldehyde
pH 7.5, temperature not specified in the publication
0.056
3-aminopropionaldehyde
pH 7.5, temperature not specified in the publication
0.021
4-(dimethylamino)butyraldehyde
pH 7.5, temperature not specified in the publication
-
0.006
4-(trimethylamino)butyraldehyde
pH 7.5, temperature not specified in the publication
-
0.024 - 0.067
4-Aminobutyraldehyde
0.051 - 0.62
4-dimethylaminobutyraldehyde
0.021
4-guanidinobutyraldehyde
pH 7.5, temperature not specified in the publication
0.0074 - 0.31
4-N-trimethylaminobutyraldehyde
0.0014 - 0.00417
4-trimethylaminobutyraldehyde
0.017 - 0.102
acetaldehyde
0.013 - 0.216
Butyraldehyde
0.053
N,N,N-trimethyl-3-aminopropionaldehyde
pH 7.5, temperature not specified in the publication
0.021
N,N-dimethyl-3-aminopropionaldehyde
pH 7.5, temperature not specified in the publication
-
0.035
Valeraldehyde
pH 7.5, temperature not specified in the publication
additional information
additional information
-
0.024
4-Aminobutyraldehyde
-
0.067
4-Aminobutyraldehyde
pH 7.5, temperature not specified in the publication
0.051
4-dimethylaminobutyraldehyde
-
-
0.62
4-dimethylaminobutyraldehyde
at pH 9.5 and 30°C
0.0074
4-N-trimethylaminobutyraldehyde
-
-
0.31
4-N-trimethylaminobutyraldehyde
at pH 9.5 and 30°C
0.0014
4-trimethylaminobutyraldehyde
-
0.00417
4-trimethylaminobutyraldehyde
-
-
0.017
acetaldehyde
pH 7.5, temperature not specified in the publication
0.013
Butyraldehyde
-
0.216
Butyraldehyde
pH 7.5, temperature not specified in the publication
0.009
hexanal
-
0.05
hexanal
pH 7.5, temperature not specified in the publication
0.028
NAD+
-
0.032
NAD+
pH 7.5, temperature not specified in the publication
1.16
NAD+
at pH 9.5 and 30°C
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
steady-state Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state Michaelis-Menten kinetics
-
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evolution
aldehyde dehydrogenase 9A1 (ALDH9A1) belongs to the aldehyde dehydrogenase (ALDH) structural superfamily, which is a large group of enzymes that catalyze the NAD+-dependent oxidation of aldehydes to carboxylic acids. The superfamily comprises hundreds of distinct genes, including 19 ALDHs expressed in humans. ALDHs share a common protein fold and catalytic mechanism, but subtle differences in their active sites result in different preferences for the aldehyde substrate. Although ALDH9A1 exhibits the basic ALDH superfamily fold, the structure reveals two remarkable features. First, the final alpha-helix and beta-strand of the Rossmann dinucleotide-binding fold are disordered. Referred to as alphaE-betaE in the closely-related betaine ALDH, these secondary structural elements form extensive interactions with NAD+ in other ALDHs
malfunction
enzyme overexpression causes the Kawasaki disease (KD), an acute vasculitis that preferentially affects coronary arteries. The disease is still the leading cause of acquired heart disease in children. Patients suffering Kawasaki disease show increased TMABADH enzyme protein levels compared to controls
metabolism
the enzyme is involved in the carnitine synthesis pathway, it is abundantly expressed in tissues showing high rates of beta-oxidation such as liver and kidney
physiological function
the major in vivo function of this enzyme is to catalyze the penultimate step of carnitine biosynthesis, the oxidation of TMBAL to 4-N-trimethylaminobutyrate. Carnitine functions in the transport of long-chain fatty acids from the cytosol to the mitochondrial matrix for the synthesis of acyl-CoAs for beta-oxidation. ALDH9A1 functions indirectly in beta-oxidation
additional information
structure analysis, overview. Structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. This unique difference is not compatible with the presence of a bound substrate and a large conformational rearrangement of the linker up to 30 A has to occur to allow the access of the substrate channel. Moreover, the alphabetaE region consisting of an alpha-helix and a beta-strand of the coenzyme domain at the dimer interface are disordered, likely due to the loss of interactions with the inter-domain linker, which leads to incomplete beta-nicotinamide adenine dinucleotide (NAD+) binding pocket
additional information
-
structure analysis, overview. Structural comparison reveals a position and a unique fold of the interdomain linker of ALDH9A1. This unique difference is not compatible with the presence of a bound substrate and a large conformational rearrangement of the linker up to 30 A has to occur to allow the access of the substrate channel. Moreover, the alphabetaE region consisting of an alpha-helix and a beta-strand of the coenzyme domain at the dimer interface are disordered, likely due to the loss of interactions with the inter-domain linker, which leads to incomplete beta-nicotinamide adenine dinucleotide (NAD+) binding pocket
additional information
the active conformation of the enzyme, in which the Rossmann dinucleotide-binding domain is fully ordered and the inter-domain linker adopts the canonical beta-hairpin observed in other ALDH structures. The presence of an aldehyde substrate and NAD+ promotes isomerization of the enzyme into the active conformation
additional information
-
the active conformation of the enzyme, in which the Rossmann dinucleotide-binding domain is fully ordered and the inter-domain linker adopts the canonical beta-hairpin observed in other ALDH structures. The presence of an aldehyde substrate and NAD+ promotes isomerization of the enzyme into the active conformation
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Hulse, J.D.; Henderson, L.M.
Carnitine biosynthesis. Purification of 4-N-trimethylaminobutyraldehyde dehydrogenase from beef liver
J. Biol. Chem.
255
1146-1151
1980
Bos taurus
brenda
Vaz, F.M.; Fouchier, S.W.; Ofman, R.; Sommer, M.; Wanders, R.J.A.
Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis
J. Biol. Chem.
275
7390-7394
2000
Rattus norvegicus (Q9JLJ3), Rattus norvegicus Wistar (Q9JLJ3)
brenda
van Vlies, N.; Wanders, R.J.; Vaz, F.M.
Measurement of carnitine biosynthesis enzyme activities by tandem mass spectrometry: differences between the mouse and the rat
Anal. Biochem.
354
132-139
2006
Mus musculus, Rattus norvegicus
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 (P49189)
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 (Q9JLJ2)
brenda
Hassan, M.; Okada, M.; Ichiyanagi, T.; Mori, N.
4-N-trimethylaminobutyraldehyde dehydrogenase: purification and characterization of an enzyme from Pseudomonas sp. 13CM
Biosci. Biotechnol. Biochem.
72
155-162
2008
Pseudomonas sp., Pseudomonas sp. 13CM
brenda
Garcia-Delgado, M.; Peral, M.J.; Duran, J.M.; Garcia-Miranda, P.; Calonge, M.L.; Ilundain, A.A.
Ontogeny of Na(+)/L-carnitine transporter and of gamma-trimethylaminobutyraldehyde dehydrogenase and gamma-butyrobetaine hydroxylase genes expression in rat kidney
Mech. Ageing Dev.
130
227-233
2009
Rattus norvegicus (Q9JLJ3)
brenda
Wen, G.; Ringseis, R.; Rauer, C.; Eder, K.
The mouse gene encoding the carnitine biosynthetic enzyme 4-N-trimethylaminobutyraldehyde dehydrogenase is regulated by peroxisome proliferator-activated receptor alpha
Biochim. Biophys. Acta
1819
357-365
2012
Mus musculus (Q9JLJ2), Mus musculus
brenda
Bari, M.R.; Hassan, M.; Akai, N.; Arima, J.; Mori, N.
Gene cloning and biochemical characterization of 4-N-trimethylaminobutyraldehyde dehydrogenase II from Pseudomonas sp. 13CM
World J. Microbiol. Biotechnol.
29
683-692
2013
Pseudomonas sp. (N0DT23), Pseudomonas sp., Pseudomonas sp. 13CM (N0DT23)
brenda
Matsunaga, A.; Harita, Y.; Shibagaki, Y.; Shimizu, N.; Shibuya, K.; Ono, H.; Kato, H.; Sekine, T.; Sakamoto, N.; Igarashi, T.; Hattori, S.
Identification of 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) as a candidate serum autoantibody target for Kawasaki disease
PLoS ONE
10
e0128189
2015
Homo sapiens (P49189), Homo sapiens, Rattus norvegicus (Q9JLJ3)
brenda
Wyatt, J.W.; Korasick, D.A.; Qureshi, I.A.; Campbell, A.C.; Gates, K.S.; Tanner, J.J.
Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1
Arch. Biochem. Biophys.
691
108477
2020
Homo sapiens (P49189), Homo sapiens
brenda
Koncitikova, R.; Vigouroux, A.; Kopecna, M.; Sebela, M.; Morera, S.; Kopecny, D.
Kinetic and structural analysis of human ALDH9A1
Biosci. Rep.
39
BSR20190558
2019
Homo sapiens (P49189), Homo sapiens
brenda
Almannai, M.; Alfadhel, M.; El-Hattab, A.W.
Carnitine inborn errors of metabolism
Molecules
24
3251
2019
Homo sapiens
brenda