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Enzyme Nomenclature
Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase
for references in articles please use BRENDA:EC1.2.1.19
Word Map on EC 1.2.1.19
- 1.2.1.19
-
polyamine
- putrescine
- betaine
- 3-aminopropionaldehyde
- 4-aminobutyrate
-
badhs
-
gamma-aminobutyric
-
osmoprotectant
- aroma
-
2-acetyl-1-pyrroline
-
diamine
- 3-aminopropanal
-
non-aromatic
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.19
-
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RECOMMENDED NAME
GeneOntology No.
aminobutyraldehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
A-stereospecific with respect to NAD+
-
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9028-98-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 general aldehyde oxidases: A and B, both oxidize a range of aldehyde substrates, enzyme B is probably more specifically involved in putrescine degradation
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
AMADH participates in carnitine biosynthesis in plants; AMADH participates in carnitine biosynthesis in plants
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
100% activity
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
4-guanidinobutyraldehyde + NADP+ + H2O
4-guanidinobutanoate + NADPH
-
-
-
-
?
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 + 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-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-cyanopropionaldehyde + NAD+ + H2O
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-guanidinopropionaldehyde + NAD+ + H2O
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-hydroxybutyraldehyde + NAD+ + H2O
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-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+
-
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+
-
-
-
?
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+
-
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+
-
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-aminobutyraldehyde + NAD+ + H2O
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-hydroxybutyraldehyde + NAD+ + H2O
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-guanidinobutyraldehyde + NAD+ + H2O
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-guanidinobutyraldehyde + NAD+ + H2O
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-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
-
-
-
?
5-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
-
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
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-aminobutyraldehyde + NAD+ + H2O
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-aminobutyraldehyde + NAD+ + H2O
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
-
?
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 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 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 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
?
-
-
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
-
-
-
additional information
?
-
-
not: DELTA1-piperidine, glutamic semialdehyde, succinic semialdehyde, malonic semialdehyde
-
-
-
additional information
?
-
-
not: DELTA1-piperidine, glutamic semialdehyde, succinic semialdehyde, malonic semialdehyde
-
-
-
additional information
?
-
-
N-acetyl-4-aminobutyraldehyde and 3-aminopropionaldehyde are poor substrates of the enzyme
-
-
-
additional information
?
-
-
very low activity with: succinate semialdehyde
-
-
-
additional information
?
-
-
very low activity with: succinate semialdehyde
-
-
-
additional information
?
-
-
very low activity with benzaldehyde, propionaldehyde
-
-
-
additional information
?
-
-
very low activity with: succinate semialdehyde
-
-
-
additional information
?
-
-
very low activity with benzaldehyde, propionaldehyde
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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+
-
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+
-
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+
-
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+
-
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+
-
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+
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
involved in the L-arginine catabolism
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
-
involved in the L-arginine catabolism
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
preferred cofactor over NADP+; preferred cofactor over NADP+
NADP+
NADP+ is a poor electron acceptor compared to NAD+ reducing the activity of isozyme AMDH1 by 86%; NADP+ is a poor electron acceptor compared to NAD+ reducing the activity of isozyme AMDH2 by 85%
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
10% activation by 2 mM observed with 0.1 mM capronaldehyde as substrate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
inactivation ocurrs due to interaction with a cysteine residue located at or near the cofactor binding site of the enzyme molecule
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
4-8 mM, full reactivation after inactivation due to overnight dialysis against 50 mM phosphate pH 7
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.285
Betaine aldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.003
Capronaldehyde
-
same value with benzaldehyde, constant substrate 1 mM NAD+
0.01
3-aminopropionaldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.075
3-aminopropionaldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.018
4-Aminobutyraldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.029
4-Aminobutyraldehyde
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.081
4-Aminobutyraldehyde
-
400 mM phosphate preparation, constant substrate 1 mM NAD+
0.17
4-Aminobutyraldehyde
isozyme AMADH1, 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
0.011
4-Guanidinobutyraldehyde
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C
0.054
acetaldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
6.9
acetaldehyde
-
400 mM phosphate preparation, constant substrate 1 mM NAD+
0.01
N,N,N-trimethyl-4-aminobutyraldehyde
isozyme AMADH1, 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
0.04
NAD+
isozyme AMADH1, 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
0.252
Succinic semialdehyde
-
400 mM phosphate preparation, constant substrate 1 mM NAD+
5.428
Succinic semialdehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
0.005
-
wild type strain, succinate used as C-source and NH3 used as N-source
0.047
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and NH3 used as N-source
0.056
-
4-aminobutyrate positive mutant, succinate used as C-source and NH3 used as N-source
0.073
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and as N-source
0.211
-
putrescine positive mutant, putrescine used as C-source and as N-source
0.24
-
putrescine positive mutant, putrescine used as C-source and NH3 used as N-source
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 9.5
-
optimum toward 4-guanidinobutyraldehyde and 5-aminovaleraldehyde
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
4-aminobutyraldehyde, at pH 6.5: about 30% of activity maximum, at pH 9.0: about 70% of activity maximum
6.9 - 8.5
-
at pH 6.9: about 30% of activity maximum, at pH 8.5: about 65% of activity maximum
7 - 10
7 - 10
-
4-guanidinobutyraldehyde, at pH 7.0: about 35% of activity maximum, at pH 10.0: about 50% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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 many regions such as the precentral gyrus, postcentral gyrus, occipital cortex, olfactory area, hippocampus, thalamus, caudate nucleus, lentiform nucleus, and cerebellum
in etiolated seedlings, AMADH activity in extracts from shoot apices is higher than those determined for stem segments
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
30 min, pH 5.0-8.0, stable; for 30 min, in 100 mM K-phosphate buffer, pH 7, allmost all activity retained; for 30 min, in 100 mM Na-acetate buffer, pH 5, allmost all activity retained; for 30 min, in 100 mM Na-bicine buffer, pH 8, allmost all activity retained
50
60
70
-
for 5 min, 3% activity recovered; for 5 min, NAD+ present during heating, 16% activity recovered
50
-
for 5 min, thermal denaturation of both 4-aminobutyraldehyde dehydrogenase and 4-guanidinobutyraldehyde dehydrogenase activities observed
50
-
for 5 min, 63% activity recovered; for 5 min, NAD+ present during heating, 100% activity recovered
60
-
for 5 min, thermal denaturation of both 4-aminobutyraldehyde dehydrogenase and 4-guanidinobutyraldehyde dehydrogenase activities observed
60
-
for 5 min, 33% activity recovered; for 5 min, NAD+ present during heating, 53% activity recovered
60
-
for 15 min, in 100 mM K-phosphate buffer, pH 7, 35% of activity lost; pH 7.0, 15 min, 35% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 250 mM phosphate, pH 6.8, in the presence of 4 mM dithiothreitol, activity decreases by 20-30% after 7 days, freezing resultes in complete inactivation
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q, TSK-GEL
-
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
from putrescine-grown cells, using ammonium sulfate fractionation and column chromatography on Sephacryl S-300, DEAE-Sephacel and Blue-Sepharose CL6B
-
from putrescine-grown cells, using column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, Sephadex G-200, Hydroxylapatite and Sephadex G-200 in 150 mM NaCl
-
to homogeneity by ammonium sulfate precipitation, anion-exchange chromatography and hydrophobic interaction chromatography
using ammonium sulfate fractionation and column chromatography on DEAE-cellulose, AMP-Sepharose, Sephadex G-200 and NAD+-Sepharose
-
using CM-trisacryl, DEAE-Sephacel, 5'-AMP-Sepharose affinity chromatography, and fast protein liquid chromatography on a mono-Q column
-
using column chromatography on DEAE-cellulose, DEAE-Toyopearl, Toyopearl HW-55 and Affi-Gel Blue
-
using column chromatography on DEAE-cellulose, hydroxylapatite, Sephacryl S-300 and Phenyl-Superose and isoelectrofocusing
-
using column chromatography on hydroxylapatite, precipitation with ammonium sulfate, column chromatography on Sephacryl S-300, Phenyl-superose, 5'-AMP-Sepharose and hydroxylapatite
-
using protamine, ammonium sulfate, acetone and column chromatography on DEAE-cellulose
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
changes in O2 availability and cellular redox balance due to stress may directly influence the activity of 4-aminobutyraldehyde dehydrogenase, thereby restricting 4-aminobutyrate formation
-
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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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.19)
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