1.2.1.19: aminobutyraldehyde dehydrogenase
This is an abbreviated version!
For detailed information about aminobutyraldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.19
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1.2.1.19
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badhs
-
choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
-
glycinebetaine
-
3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
-
aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
-
4-aminobutyrate
-
synthesis
- 1.2.1.19
-
badhs
- choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
- glycinebetaine
- 3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
- aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
- 4-aminobutyrate
- synthesis
Reaction
Synonyms
4-aminobutanal dehydrogenase, 4-aminobutyraldehyde dehydrogenase, ABAL dehydrogenase, ABALDH, ALDH10A8, ALDH10A9, AMADH, AMADH1, AMADH2, aminoaldehyde dehydrogenase, BADH, betaine aldehyde dehydrogenase, dehydrogenase, aminobutyraldehyde, EC 1.5.1.35, gadbh, gamma-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydroganase, gamma-aminobutyraldehyde dehydrogenase, gamma-guanidinobutyraldehyde dehydrogenase, MdAMADH1, MdAMADH2, More, NAD+-aminoaldehyde dehydrogenase, NAD+-dependent aminoaldehyde dehydrogenase, PatD, PsAMADH 1, PsAMADH 2, SlAMADH1, SlAMADH2, YdcW, ZmAMADH1a, ZmAMADH1b, ZmAMADH2
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase
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REACTION DIAGRAM
2,2-dimethyl-3-propionylaminopropanal + NAD+ + H2O
2,2-dimethyl-3-propionylaminopropanoate + NADH + 2 H+
-
-
-
?
2,2-dimethyl-4-aminobutanal + NAD+ + H2O
2,2-dimethyl-4-aminobutanoate + NADH + 2 H+
-
-
-
?
2,2-dimethyl-4-propionylaminobutanal + NAD+ + H2O
2,2-dimethyl-4-propionylaminobutanoate + NADH + 2 H+
-
-
-
?
2-methyl-3-butyrylaminopropanal + NAD+ + H2O
2-methyl-3-butyrylaminopropanoate + NADH + 2 H+
-
-
-
?
2-methyl-3-propionylaminopropanal + NAD+ + H2O
2-methyl-3-propionylaminopropanoate + NADH + 2 H+
-
-
-
?
2-methyl-4-aminobutanal + NAD+ + H2O
2-methyl-4-aminobutanoate + NADH + 2 H+
-
-
-
?
2-methyl-4-propionylaminobutanal + NAD+ + H2O
2-methyl-4-propionylaminobutanoate + NADH + 2 H+
-
-
-
?
3-acetaminopropanal + NAD+ + H2O
3-acetaminopropanoate + NADH + 2 H+
-
-
-
?
3-adipylaminopropanal + NAD+ + H2O
3-adipylaminopropanoate + NADH + 2 H+
-
-
-
?
3-aminobutanal + NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
best substrate
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
100% activity
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + 2 H+
best substrate
-
-
?
3-butyrylaminopropanal + NAD+ + H2O
3-butyrylaminpropanoate + NADH + 2 H+
-
-
-
?
3-methyl-3-butyrylaminopropanal + NAD+ + H2O
3-methyl-3-butyrylaminopropanoate + NADH + 2 H+
-
-
-
?
3-methyl-4-aminobutanal + NAD+ + H2O
3-methyl-4-aminobutanoate + NADH + 2 H+
-
-
-
?
3-propionylaminopropanal + NAD+ + H2O
3-propionylaminopropanoate + NADH + 2 H+
-
-
-
?
3-pyridine carboxaldehyde + NAD+ + H2O
3-pyridine carboxylic acid + NADH + 2 H+
-
-
-
?
3-valerylaminopropanal + NAD+ + H2O
3-valerylaminopropanoate + NADH + 2 H+
-
-
-
?
4-acetaminobutanal + NAD+ + H2O
4-acetaminobutanoate + NADH + 2 H+
-
-
-
?
4-butyrylaminobutanal + NAD+ + H2O
4-butyrylaminobutanoate + NADH + 2 H+
-
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
4-guanidinobutyraldehyde + NADP+ + H2O
4-guanidinobutanoate + NADPH
-
-
-
-
?
4-propionylaminobutanal + NAD+ + H2O
4-propionylaminobutanoate + NADH + 2 H+
-
-
-
?
4-pyridine carboxaldehyde + NAD+ + H2O
4-pyridine carboxylic acid + NADH + 2 H+
-
-
-
?
4-valerylaminobutanal + NAD+ + H2O
4-valerylaminobutanoate + NADH + 2 H+
-
-
-
?
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH
-
12% of activity with 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
N-(3-aminopropyl)-4-aminobutyraldehyde + NAD+ + H2O
N-(3-aminopropyl)-4-aminobutanoate + NADH
-
11% of activity with 3-aminopropionaldehyde
-
-
?
N-acetyl-3-aminopropionaldehyde + NAD+ + H2O
N-acetyl-3-aminopropionate + NADH + H+
-
-
-
?
3-aminopropanoate + NADH + H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
17% the rate of 4-aminobutyraldehyde reduction
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
17% the rate of 4-aminobutyraldehyde reduction
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
high activity
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
best substrate
-
-
?
3-cyanopropanoate + NADH + H+
108% activity compared to 3-aminopropionaldehyde
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
99% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropanoate + NADH + H+
12% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
17% activity compared to 3-aminopropionaldehyde
-
-
?
4-amino-2-hydroxybutanoate + NADH + H+
13% activity compared to 3-aminopropionaldehyde
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + H+
20% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
Desulfovibrio vulgaris Marburg / DSM 2119
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
Desulfovibrio vulgaris Marburg / DSM 2119
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
specific for
-
?, ir
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
specific for
-
ir
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
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involved in amino aldehyde metabolism, connects metabolism of a diamine putrescine with that of the inhibitory neurotransmitter 4-aminobutyric acid
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
degradation of agmatine
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
gamma-aminobutyrate metabolism
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
involved in the arginine decarboxylase pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
-
51% of activity with 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
-
-
-
?
4-aminobutanoate + NADH + 2 H+
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
-
?
4-aminobutanoate + NADH + H+
36% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
82% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
-
-
-
?
4-guanidino-2-hydroxybutanoate + NADH + H+
22% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
25% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH
-
52% of activity with 3-aminopropionaldehyde
-
-
?
4-guanidinobutanoate + NADH + 2 H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + 2 H+
-
-
-
?
4-guanidinobutanoate + NADH + H+
29% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + H+
30% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyrate + NADH + H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
involved in the L-arginine catabolism
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
involved in the L-arginine catabolism
-
?
5-aminovalerate + NADH + H+
-
-
-
?
5-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
-
-
-
?
gamma-butyrobetaine + NADH + H+
35% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
54% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
-
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
best substrate
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
-
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+
best substrate
-
-
?
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
45% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
48% activity compared to 3-aminopropionaldehyde
-
-
?
N,N-dimethyl-4-aminobutanoate + NADH + H+
57% activity compared to 3-aminopropionaldehyde
-
-
?
N,N-dimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
80% activity compared to 3-aminopropionaldehyde
-
-
?
succinate semialdehyde + NAD+
succinate + NADH + H+
-
24% the rate of 4-aminobutyraldehyde reduction
-
?
?
-
maximal activity and catalytic efficiency are obtained with NAD+ and 3-aminopropanal, followed by 4-aminobutanal, negligible activity is obtained with betaine aldehyde. The betaine-aldehyde dehydrogenase ADH10A8 acts as 4-aminobutanal dehydrogenase
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-
?
additional information
?
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maximal activity and catalytic efficiency are obtained with NAD+ and 3-aminopropanal, followed by 4-aminobutanal, negligible activity is obtained with betaine aldehyde. The betaine-aldehyde dehydrogenase ADH10A8 acts as 4-aminobutanal dehydrogenase
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-
?
additional information
?
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maximal activity and catalytic efficiency are obtained with NAD+ and 3-aminopropanal, followed by 4-aminobutanal, negligible activity is obtained with betaine aldehyde. The betaine-aldehyde dehydrogenase ADH10A8 acts as 4-aminobutanal dehydrogenase
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-
?
additional information
?
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no activity with betaine aldehyde, propionaldehyde, and acetaldehyde
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-
?
additional information
?
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no activity with betaine aldehyde
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additional information
?
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no activity with betaine aldehyde
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additional information
?
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the enzyme is also active with betaine aldehyde, EC 1.2.1.8
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additional information
?
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the enzyme is also active with betaine aldehyde, EC 1.2.1.8
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additional information
?
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the enzyme is also active with betaine aldehyde, EC 1.2.1.8
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additional information
?
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apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminobutanal. Very low activity with betaine aldehyde
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-
?
additional information
?
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apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminobutanal. Very low activity with betaine aldehyde
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-
?
additional information
?
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-
apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminobutanal. Very low activity with betaine aldehyde
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-
?
additional information
?
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apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminopropanal. Very low activity with betaine aldehyde
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-
?
additional information
?
-
apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminopropanal. Very low activity with betaine aldehyde
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-
?
additional information
?
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-
apple AMADHs possess three highly conserved catalytic residues (N162, E260 and C294, MdAMADH numbering), which form the active site in PsAMADHs, and two conserved aspartate residues located at the entrance of the substrate channel (D110, D113), as well as Y163 and W288, which are considered essential for high-affinity binding of x-aminoaldehydes such as 3-aminopropanal. Very low activity with betaine aldehyde
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-
?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 52%
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?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 52%
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?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 52%
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?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 72%
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?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 72%
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?
additional information
?
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3-acetylpyridine-NAD+ is the best electron acceptor and leads to 33% activity compared to that with NAD+, while thio-NAD+ drastically and especially affects isozyme AMADH1 activity. 3-Pyridinealdehyde-NAD+ hardly functions as a coenzyme for AMADH1. Deamino-NAD+ is a better coenzyme than NAD+ and increases the reaction rate by 72%
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?
additional information
?
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isozyme AMADH1 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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isozyme AMADH1 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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isozyme AMADH1 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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isozyme AMADH2 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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isozyme AMADH2 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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isozyme AMADH2 preferentially oxidizes C3 and C4 aminoaldehydes and has no activity with butyraldehyde, acetaldehyde, propionaldehyde, betaine aldehyde, valeraldehyde, capronaldehyde, enanthaldehyde, 2-pyridine carboxaldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 1, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 1, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 1, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 2, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 2, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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design and synthesis of N-acyl derivates of 3-aminopropanal and 4-aminobutanal and confirmed as substrates of AMADH isoenzyme PsAMADH 2, molecular docking indicates the possible auxiliary role of Tyr163, Ser295 and Gln451 in binding of the substrates. Substrate specificity and molecular docking, overview. The substrate properties of N-acyl-omega-aminoaldehydes arise from their proper binding at the active site, which is facilitated by interactions with amino acid residues in the substrate channel such as Tyr163
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additional information
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1-pyrroline is used as source of substrate, delta1-pyrroline and gamma-aminobutyraldehyde exist as an equilibrium mixture in aqueous solution with the former as the predominant species
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additional information
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not: DELTA1-piperidine, glutamic semialdehyde, succinic semialdehyde, malonic semialdehyde
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additional information
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not: DELTA1-piperidine, glutamic semialdehyde, succinic semialdehyde, malonic semialdehyde
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additional information
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N-acetyl-4-aminobutyraldehyde and 3-aminopropionaldehyde are poor substrates of the enzyme
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additional information
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very low activity with: succinate semialdehyde
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additional information
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very low activity with: succinate semialdehyde
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additional information
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very low activity with benzaldehyde, propionaldehyde
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additional information
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very low activity with: succinate semialdehyde
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additional information
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very low activity with benzaldehyde, propionaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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additional information
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identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde
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