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Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase and Organism(s) Pisum sativum and UniProt Accession Q8VWZ1
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1.2.1.19 aminobutyraldehyde dehydrogenaseIUBMB Comments
The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates . The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 gamma-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway and belongs in the aldehyde dehydrogenase superfamily .
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Word Map
- 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
The taxonomic range for the selected organisms is: Pisum sativum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
betaine aldehyde dehydrogenase, amadh, aminoaldehyde dehydrogenase, aldh10a8, 4-aminobutyraldehyde dehydrogenase, aldh10a9, gamma-aminobutyraldehyde dehydrogenase, slamadh1, 4-aminobutanal dehydrogenase, abaldh, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-aminobutanal dehydrogenase
-
-
-
-
4-aminobutyraldehyde dehydrogenase
ABAL dehydrogenase
-
-
-
-
dehydrogenase, aminobutyraldehyde
-
-
-
-
gamma-aminobutyraldehyde dehydroganase
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
-
-
-
-
gamma-guanidinobutyraldehyde dehydrogenase
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-
-
-
4-aminobutyraldehyde dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
4-aminobutanal:NAD+ 1-oxidoreductase
The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates [9]. The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54 gamma-guanidinobutyraldehyde dehydrogenase). As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. The enzyme forms part of the arginine-catabolism pathway [8] and belongs in the aldehyde dehydrogenase superfamily [9].
CAS REGISTRY NUMBER
COMMENTARY
9028-98-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
100% activity
-
-
?
3-butyrylaminopropanal + NAD+ + H2O
3-butyrylaminpropanoate + NADH + 2 H+
-
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
108% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
12% activity compared to 3-aminopropionaldehyde
-
-
?
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-valerylaminopropanal + NAD+ + H2O
3-valerylaminopropanoate + NADH + 2 H+
-
-
-
?
4-acetaminobutanal + NAD+ + H2O
4-acetaminobutanoate + NADH + 2 H+
-
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + H+
20% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
82% activity compared to 3-aminopropionaldehyde
-
-
?
4-butyrylaminobutanal + NAD+ + H2O
4-butyrylaminobutanoate + NADH + 2 H+
-
-
-
?
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 + H+
29% activity compared to 3-aminopropionaldehyde
-
-
?
4-propionylaminobutanal + NAD+ + H2O
4-propionylaminobutanoate + NADH + 2 H+
-
-
-
?
4-valerylaminobutanal + NAD+ + H2O
4-valerylaminobutanoate + NADH + 2 H+
-
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
54% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
45% activity compared to 3-aminopropionaldehyde
-
-
?
N,N-dimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
57% activity compared to 3-aminopropionaldehyde
-
-
?
2,2-dimethyl-3-propionylaminopropanal + NAD+ + H2O
2,2-dimethyl-3-propionylaminopropanoate + 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-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
100% activity
-
-
?
3-butyrylaminopropanal + NAD+ + H2O
3-butyrylaminpropanoate + NADH + 2 H+
-
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
99% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
17% activity compared to 3-aminopropionaldehyde
-
-
?
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-valerylaminopropanal + NAD+ + H2O
3-valerylaminopropanoate + NADH + 2 H+
-
-
-
?
4-acetaminobutanal + NAD+ + H2O
4-acetaminobutanoate + NADH + 2 H+
-
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + H+
13% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
36% activity compared to 3-aminopropionaldehyde
-
-
?
4-butyrylaminobutanal + NAD+ + H2O
4-butyrylaminobutanoate + NADH + 2 H+
-
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
22% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + H+
30% activity compared to 3-aminopropionaldehyde
-
-
?
4-propionylaminobutanal + NAD+ + H2O
4-propionylaminobutanoate + NADH + 2 H+
-
-
-
?
4-valerylaminobutanal + NAD+ + H2O
4-valerylaminobutanoate + NADH + 2 H+
-
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
35% 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-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
80% activity compared to 3-aminopropionaldehyde
-
-
?
additional information
?
-
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%
-
-
?
additional information
?
-
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%
-
-
?
additional information
?
-
-
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%
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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%
-
-
?
additional information
?
-
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%
-
-
?
additional information
?
-
-
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%
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
NADP+ is a poor electron acceptor compared to NAD+ reducing the activity of isozyme AMDH1 by 86%
NADP+
NADP+ is a poor electron acceptor compared to NAD+ reducing the activity of isozyme AMDH2 by 85%
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2-dimethyl-4-propionylaminobutanal
causes substrate inhibition at high concentration
3-methyl-3-butyrylaminopropanal
causes substrate inhibition at high concentration
3-methyl-4-butyrylaminobutanal
causes substrate inhibition at high concentration
3-propionylaminopropanal
causes substrate inhibition at high concentration
4-acetamidobutanal
causes substrate inhibition at high concentration
4-propionylaminobutanal
causes substrate inhibition at high concentration
additional information
isozyme PsAMADH 1 shows no substrate inhibition
-
additional information
isozyme PsAMADH 1 shows no substrate inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
injury elicites increase in AMADH in both etiolated and green seedlings. Activity is localized in cortical parenchyma and epidermal cells adjacent to the wound site in spatial correlation with an intensive lignification
-
additional information
-
injury elicites increase in AMADH in both etiolated and green seedlings. Activity is localized in cortical parenchyma and epidermal cells adjacent to the wound site in spatial correlation with an intensive lignification
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.266
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.183
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.525
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.075
3-aminopropionaldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.49 - 2
3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.17
4-Aminobutyraldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.011
4-guanidinobutyraldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.01
N,N,N-trimethyl-4-aminobutyraldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.04
NAD+
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.477
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.506
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.0935
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.189
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.01
3-aminopropionaldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.029
4-Aminobutyraldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.007
4-guanidinobutyraldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.021
N,N,N-trimethyl-4-aminobutyraldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.055
NAD+
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.366
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.638
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.137
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.361
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
0.397
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.469
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.13
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
0.531
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.41
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
2.03
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
2.32
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
14.4
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
5.8
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
6.49
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
4.08
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
1.2
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
2.87
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
1.22
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
1.24
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
1.56
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
12.1
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
6.84
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
9.54
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in etiolated seedlings, AMADH activity in extracts from root tips is higher than those determined for stem segments
in etiolated seedlings, AMADH activity in extracts from shoot apices is higher than those determined for stem segments
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
metabolism
AMADH participates in carnitine biosynthesis in plants
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
metabolism
AMADH participates in carnitine biosynthesis in plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AADH1_PEA
503
0
54809
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme AMADH1 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 13% (w/v) PEG 6000 and 5% (v/v) 2-methyl-2,4-pentanediol, at 20°C
isozyme AMADH2 in complex with NAD+, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.5), 18% (w/v) PEG 4000, 10% (v/v) isopropanol and 0.5% (w/v) n-octyl beta-D-glucopyranoside, at 20°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cobalt- or nickel-charged IDA-Sepharose column chromatography and Resource Q column chromatography
cobalt- or nickel-charged IDA-Sepharose column chromatography and Resource Q column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
AMADH may participate in processes of adaptation to stress events caused by mechanical injury, which involve polyamine catabolism, GABA production and lignification
additional information
-
AMADH may participate in processes of adaptation to stress events caused by mechanical injury, which involve polyamine catabolism, GABA production and lignification
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petrivalsky, M.; Brauner, F.; Luhova, L.; Gagneul, D.; Sebela, M.
Aminoaldehyde dehydrogenase activity during wound healing of mechanically injured pea seedlings
J. Plant Physiol.
164
1410-1418
2007
Pisum sativum (Q8VWZ1), Pisum sativum
Tylichova, M.; Kopecny, D.; Morera, S.; Briozzo, P.; Lenobel, R.; Snegaroff, J.; Sebela, M.
Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes
J. Mol. Biol.
396
870-882
2010
Pisum sativum (Q8VWZ1), Pisum sativum (Q93YB2), Pisum sativum
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