Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.2.1.19
-
RECOMMENDED NAME
GeneOntology No.
aminobutyraldehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
show the reaction diagram
A-stereospecific with respect to NAD+
-
4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
beta-Alanine metabolism
-
putrescine degradation I
-
putrescine degradation IV
-
putrescine degradation V
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4-aminobutanal dehydrogenase
-
-
-
-
4-aminobutyraldehyde dehydrogenase
-
-
-
-
4-aminobutyraldehyde dehydrogenase
-
-
4-aminobutyraldehyde dehydrogenase
Q8VWZ1, Q93YB2
-
ABAL dehydrogenase
-
-
-
-
ABALDH
P77674
-
ABALDH
Escherichia coli K12 MG1655
P77674
-
-
ABALDH
Q8VWZ1, Q93YB2
-
AMADH
-
-
AMADH
Q8VWZ1
-
AMADH1
Q8VWZ1
isozyme
AMADH2
Q93YB2
isozyme
aminoaldehyde dehydrogenase
Q8VWZ1
-
aminoaldehyde dehydrogenase
Q93YB2
-
dehydrogenase, aminobutyraldehyde
-
-
-
-
gamma-aminobutyraldehyde dehydroganase
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
P77674
-
gamma-aminobutyraldehyde dehydrogenase
Escherichia coli K12 MG1655
P77674
-
-
gamma-guanidinobutyraldehyde dehydrogenase
-
-
-
-
YdcW
P77674
-
YdcW
Escherichia coli K12 MG1655
P77674
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-98-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
DSM 1030, strictly anaerobic
-
-
Manually annotated by BRENDA team
putrescine grown cells
-
-
Manually annotated by BRENDA team
2 general aldehyde oxidases: A and B, both oxidize a range of aldehyde substrates, enzyme B is probably more specifically involved in putrescine degradation
-
-
Manually annotated by BRENDA team
strain Marburg, strictly anaerobic
-
-
Manually annotated by BRENDA team
Desulfovibrio vulgaris Marburg
strain Marburg, strictly anaerobic
-
-
Manually annotated by BRENDA team
strain K12 MG1655
SwissProt
Manually annotated by BRENDA team
Escherichia coli K12 MG1655
strain K12 MG1655
SwissProt
Manually annotated by BRENDA team
strain M1h, strictly anaerobic
-
-
Manually annotated by BRENDA team
Methanospirillum hungatei M1h
strain M1h, strictly anaerobic
-
-
Manually annotated by BRENDA team
cv. Lantra
UniProt
Manually annotated by BRENDA team
isozyme AMADH1
UniProt
Manually annotated by BRENDA team
isozyme AMADH2
Q93YB2
UniProt
Manually annotated by BRENDA team
A.T.C.C. 12633
-
-
Manually annotated by BRENDA team
A.T.C.C. 25571
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar-strain
Wistar-strain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Q8VWZ1, Q93YB2
AMADH participates in carnitine biosynthesis in plants; AMADH participates in carnitine biosynthesis in plants
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
show the reaction diagram
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + H+
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar-strain
-
17% the rate of 4-aminobutyraldehyde reduction
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
100% activity
-
-
?
3-aminopropionaldehyde + NADP+ + H2O
3-aminopropanoate + NADPH
show the reaction diagram
-
-
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
108% activity compared to 3-aminopropionaldehyde
-
-
?
3-cyanopropionaldehyde + NAD+ + H2O
3-cyanopropanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
99% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
12% activity compared to 3-aminopropionaldehyde
-
-
?
3-guanidinopropionaldehyde + NAD+ + H2O
3-guanidinopropanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
17% activity compared to 3-aminopropionaldehyde
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino-2-hydroxybutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
20% activity compared to 3-aminopropionaldehyde
-
-
?
4-amino-2-hydroxybutyraldehyde + NAD+ + H2O
4-amino2-hydroxybutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
13% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
ir
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
ir
-
-
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
specific for
-
?, ir
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
specific for
-
ir
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
involved in the arginine decarboxylase pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
gamma-aminobutyrate metabolism
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
degradation of agmatine
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
-
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Methanospirillum hungatei M1h
-
-, role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Desulfovibrio vulgaris Marburg
-
-, role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-, synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-, involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-, P77674
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-
51% of activity with 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
Escherichia coli K12 MG1655
P77674
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
82% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutanoate + NADPH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
36% activity compared to 3-aminopropionaldehyde
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
show the reaction diagram
-, P77674
-
-
-
?
4-aminobutyraldehyde + NADP+ + H2O
4-aminobutanoate + NADPH
show the reaction diagram
Escherichia coli K12 MG1655
P77674
-
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
22% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidino-2-hydroxybutyraldehyde + NAD+ + H2O
4-guanidino-2-hydroxybutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
25% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
-
-, involved in the L-arginine catabolism
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
Pseudomonas putida P2
-
-, involved in the L-arginine catabolism
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH
show the reaction diagram
-
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH
show the reaction diagram
-
52% of activity with 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
29% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
30% activity compared to 3-aminopropionaldehyde
-
-
?
4-guanidinobutyraldehyde + NADP+ + H2O
4-guanidinobutanoate + NADPH
show the reaction diagram
-
-
-
-
?
4-ureidobutyraldehyde + NAD+
4-ureidobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
5-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
show the reaction diagram
-
-
-
?
5-aminovaleraldehyde + NAD+ + H2O
5-aminovalerate + NADH + H+
show the reaction diagram
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar-strain
-
-
-
?
aminoacetaldehyde + NAD+ + H2O
aminoacetate + NADH
show the reaction diagram
-
12% of activity with 3-aminopropionaldehyde
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine acid + NADH + H+
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar-strain
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
-
-
-
?
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
-, P77674
-
-
-
-
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
Escherichia coli K12 MG1655
P77674
-
-
-
-
butyraldehyde + NAD+ + H2O
butyrate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-
-
?
capronaldehyde + NAD+ + H2O
capronate + NADH + H+
show the reaction diagram
Rattus norvegicus, Rattus norvegicus Wistar-strain
-
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
35% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-3-aminopropionaldehyde + NAD+ + H2O
gamma-butyrobetaine + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
54% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
45% activity compared to 3-aminopropionaldehyde
-
-
?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N,N-trimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
48% activity compared to 3-aminopropionaldehyde
-
-
?
N,N-dimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
57% activity compared to 3-aminopropionaldehyde
-
-
?
N,N-dimethyl-4-aminobutyraldehyde + NAD+ + H2O
N,N-dimethyl-4-aminobutanoate + NADH + H+
show the reaction diagram
-, Q8VWZ1, Q93YB2
80% activity compared to 3-aminopropionaldehyde
-
-
?
N-(3-aminopropyl)-4-aminobutyraldehyde + NAD+ + H2O
N-(3-aminopropyl)-4-aminobutanoate + NADH
show the reaction diagram
-
11% of activity with 3-aminopropionaldehyde
-
-
?
N-acetyl-3-aminopropionaldehyde + NAD+ + H2O
N-acetyl-3-aminopropionate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
-
-
-
?
propionaldehyde + NAD+ + H2O
propionate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-
-
?
succinate semialdehyde + NAD+
succinate + NADH + H+
show the reaction diagram
-
-
-
?
succinate semialdehyde + NAD+
succinate + NADH + H+
show the reaction diagram
-
24% the rate of 4-aminobutyraldehyde reduction
-
?
succinate semialdehyde + NAD+
succinate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
show the reaction diagram
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
show the reaction diagram
-
-
-
?
valeraldehyde + NAD+ + H2O
valerate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
-
-
?
isobutyraldehyde + NAD+ + H2O
isobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
very low activity with: succinate semialdehyde
-
-
-
additional information
?
-
-
very low activity with: succinate semialdehyde
-
-
-
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
?
-
-
very low activity with benzaldehyde, propionaldehyde
-
-
-
additional information
?
-
-
N-acetyl-4-aminobutyraldehyde and 3-aminopropionaldehyde are poor substrates of the enzyme
-
-
-
additional information
?
-
-
not: DELTA1-piperidine, glutamic semialdehyde, succinic semialdehyde, malonic semialdehyde
-
-
-
additional information
?
-
-, Q8VWZ1, Q93YB2
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
?
-
-, Q8VWZ1, Q93YB2
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
?
-
-, Q8VWZ1, Q93YB2
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
?
-
-, Q8VWZ1, Q93YB2
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
?
-
Rattus norvegicus Wistar-strain
-
very low activity with: succinate semialdehyde, very low activity with benzaldehyde, propionaldehyde
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
ir
-
-
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
involved in the arginine decarboxylase pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
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+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
gamma-aminobutyrate metabolism
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
degradation of agmatine
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
-
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Methanospirillum hungatei M1h, Desulfovibrio vulgaris Marburg
-
role in putrescine degradative pathway
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid in brain
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + H+
show the reaction diagram
Rattus norvegicus Wistar-strain
-
involved in the metabolism of biogenic amines and in the synthesis of 4-aminobutyric acid
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutyrate + NADH + H+
show the reaction diagram
Pseudomonas putida, Pseudomonas putida P2
-
involved in the L-arginine catabolism
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
absolutely dependent on
NAD+
-
both enzymes A and B
NAD+
-
highly specific for
NAD+
Q8VWZ1, Q93YB2
preferred cofactor over NADP+; preferred cofactor over NADP+
NADP+
-
both enzymes A and B
NADP+
-
rate of dehydrogenation about 4% those with NAD+
NADP+
-
no enzyme activity found
NADP+
-
no enzyme activity found
NADP+
Q8VWZ1, Q93YB2
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%
additional information
-
not NADP+
-
additional information
-
not NADP+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
10% activation by 2 mM observed with 0.1 mM capronaldehyde as substrate
additional information
-
no requirement for bivalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Carboxy-2'-hydroxy-5'-sulfoformazylbenzene
-
zincon
acetaldehyde
-
strongly inhibits 4-aminobutyraldehyde oxidation
Cationic buffers
-
-
-
iodoacetamide
-
-
ion-exchange resins
-
-
-
monoiodoacetate
-
slowly
N-ethylmaleimide
-
-
N-ethylmaleimide
-
inactivation ocurrs due to interaction with a cysteine residue located at or near the cofactor binding site of the enzyme molecule
NADH
-
competitive inhibitor with respect to NAD+
p-chloromercuribenzoate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
4-8 mM, full reactivation after inactivation due to overnight dialysis against 50 mM phosphate pH 7
additional information
-, Q8VWZ1
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0015
-
3-aminopropionaldehyde
-
37C, pH 8.7
0.01
-
3-aminopropionaldehyde
Q8VWZ1, Q93YB2
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.075
-
3-aminopropionaldehyde
Q8VWZ1, Q93YB2
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.15
-
3-aminopropionaldehyde
-
-
0.015
-
4-Aminobutanal
-
-
0.002
-
4-Aminobutyraldehyde
-
37C, pH 8.7
0.005
-
4-Aminobutyraldehyde
-
E3 isozyme
0.018
-
4-Aminobutyraldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.02612
-
4-Aminobutyraldehyde
-
-
0.029
-
4-Aminobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.041
-
4-Aminobutyraldehyde
-, P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
0.065
-
4-Aminobutyraldehyde
-
-
0.081
-
4-Aminobutyraldehyde
-
400 mM phosphate preparation, constant substrate 1 mM NAD+
0.083
-
4-Aminobutyraldehyde
-
-
0.109
-
4-Aminobutyraldehyde
-
constant substrate 1 mM NAD+
0.17
-
4-Aminobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.26
-
4-Aminobutyraldehyde
-
pH 8.0
0.5
-
4-Aminobutyraldehyde
-
E2 isozyme
0.8
-
4-Aminobutyraldehyde
-
E1 isozyme
0.83
-
4-Aminobutyraldehyde
-
pH 9.5
0.007
-
4-Guanidinobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.011
-
4-Guanidinobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.013
-
4-Guanidinobutyraldehyde
-
37C, pH 8.7
0.085
-
4-Guanidinobutyraldehyde
-
-
0.13
-
4-Guanidinobutyraldehyde
-
pH 9.5
0.16
-
4-Guanidinobutyraldehyde
-
pH 8.0
0.26
-
4-Guanidinobutyraldehyde
-
-
0.2
-
5-Aminovaleraldehyde
-
-
0.054
-
acetaldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.111
-
acetaldehyde
-
constant substrate 1 mM NAD+
6.9
-
acetaldehyde
-
400 mM phosphate preparation, constant substrate 1 mM NAD+
0.285
-
Betaine aldehyde
-
250 mM phosphate preparation, constant substrate 1 mM NAD+
0.005
-
Butyraldehyde
-
constant substrate 1 mM NAD+
0.016
-
Butyraldehyde
-
-
0.196
-
Butyraldehyde
-, P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
0.003
-
Capronaldehyde
-
same value with benzaldehyde, constant substrate 1 mM NAD+
0.018
-
DELTA1-pyrroline
-
-
0.0313
-
DELTA1-pyrroline
-
-
0.016
-
Isobutyraldehyde
-
constant substrate 1 mM NAD+
0.01
-
N,N,N-trimethyl-4-aminobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
-
0.021
-
N,N,N-trimethyl-4-aminobutyraldehyde
Q8VWZ1, Q93YB2
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
-
0.011
-
NAD+
-
37C, pH 8.7
0.02006
-
NAD+
-
-
0.037
-
NAD+
-
-
0.04
-
NAD+
Q8VWZ1, Q93YB2
isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.0538
-
NAD+
-
-
0.055
-
NAD+
Q8VWZ1, Q93YB2
isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20C
0.07
-
NAD+
-
constant substrate 2 mM 4-aminobutyraldehyde
0.186
-
NAD+
-
constant substrate 0.1 mM capronaldehyde
0.256
-
NAD+
-
constant substrate 0.2 mM isotbutyraldehyde
0.886
-
NAD+
-
constant substrate 2 mM acetaldehyde
0.013
-
propionaldehyde
-
constant substrate 1 mM NAD+
0.0225
-
putrescine
-
-
-
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+
0.004
-
Valeraldehyde
-
constant substrate 1 mM NAD+
0.013
-
Valeraldehyde
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.7
-
4-Aminobutyraldehyde
-, P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
0.3
-
Butyraldehyde
-, P77674
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-
NH3 used as N-source
0.001
-
-
-
0.005
-
-
wild type strain, succinate used as C-source and NH3 used as N-source
0.009
-
-
cells grown on succinate and NH3
0.01
-
-
histidine used as N-source
0.015
-
-
L-glutamate used as growth substrate
0.017
-
-
4-aminobutyrate used as N-source
0.024
-
-
putrescine used as N-source
0.029
-
-
L-arginine used as growth substrate
0.038
-
-
D-arginine used as growth substrate
0.045
-
-
4-guanidinobutyrate used as growth substrate
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
0.062
-
-
cells grown on L-glutamate
0.064
-
-
cells grown on 4-aminobutyric acid
0.073
-
-
4-aminobutyrate positive mutant, 4-aminobutyrate used as C-source and as N-source
0.086
-
-
2-ketoarginine used as growth substrate
0.092
-
-
putrescine used as growth substrate
0.12
-
-
CS101B pyrrolidine negative strain
0.122
-
-
agmatine used as growth substrate
0.148
-
-
cells grown on 4-guanidinobutyraldehyde
0.15
-
-
M20 strain
0.156
-
-
cells grown on 4-guanidinobutyric acid
0.211
-
-
putrescine positive mutant, putrescine used as C-source and as N-source
0.22
-
-
-
0.24
-
-
putrescine positive mutant, putrescine used as C-source and NH3 used as N-source
0.33
-
-
cells grown on L-arginine
0.96
-
-
CS101A strain
0.975
-
-
CS101B strain
11.6
-
-
purified enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.4
-
-
in the presence of sodium citrate buffer
8
-
-
3-aminopropanal
8
-
-
optimum toward 4-aminobutyraldehyde
8.5
9.5
-
optimum toward 4-guanidinobutyraldehyde and 5-aminovaleraldehyde
8.6
-
-
-
9
10
-
4-aminobutanal
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
7
-
at pH 4.0 and pH 7.0: about 60% of activity maximum
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
-
4-guanidinobutyraldehyde, at pH 7.0: about 35% of activity maximum, at pH 10.0: about 50% of activity maximum
7
8.3
-
highly active between
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
-
-
-
75
-
-
increase in dehydrogenase capacity from 25C to 75C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
in many regions such as the precentral gyrus, postcentral gyrus, occipital cortex, olfactory area, hippocampus, thalamus, caudate nucleus, lentiform nucleus, and cerebellum
Manually annotated by BRENDA team
Rattus norvegicus Wistar-strain
-
-
-
Manually annotated by BRENDA team
Escherichia coli K12 MG1655
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar-strain
-
-
-
Manually annotated by BRENDA team
Rattus norvegicus Wistar-strain
-
-
-
Manually annotated by BRENDA team
-, Q8VWZ1
in etiolated seedlings, AMADH activity in extracts from root tips is higher than those determined for stem segments
Manually annotated by BRENDA team
-, Q8VWZ1
in etiolated seedlings, AMADH activity in extracts from shoot apices is higher than those determined for stem segments
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Pseudomonas putida P2, Rattus norvegicus Wistar-strain
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51000
-
-, P77674
single subunit, SDS-PAGE
55000
-
-
gel filtration
83000
-
-
gel filtration
112000
-
-
gel filtration
115000
-
-
gel filtration
117000
-
Q8VWZ1, Q93YB2
gel filtration
120000
-
Q8VWZ1, Q93YB2
gel filtration
195000
-
-
gel filtration
202000
-
-, P77674
native protein, gel-filtration
210000
-
-
-
228000
-
-
gel filtration, PAGE
240000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 64000
dimer
-
2 * 95000, SDS-PAGE
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 52000, SDS-PAGE
dimer
Q8VWZ1, Q93YB2
x-ray crystallography; x-ray crystallography
dimer
Rattus norvegicus Wistar-strain
-
2 * 51000, SDS-PAGE; 2 * 52000, SDS-PAGE
-
monomer
-
1 * 55000, SDS-PAGE
tetramer
-
4 * 57000, SDS-PAGE
tetramer
-
4 * 51000
tetramer
-, P77674
4 * 51000
tetramer
Escherichia coli K12 MG1655
-
4 * 51000
-
trimer
-
3 * 75000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 20C; 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 20C
Q8VWZ1, Q93YB2
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
most stable at neutral pH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
stable over several months
-15
-
-
retains 70% of activity when stored for 2 weeks
0
35
-
up to 5 min, stable
2
-
-
80% loss of activity after overnight storage
28
-
-
temperature higher than 28C promotes slow activation
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
35
-
-
unstable above
40
-
-
64% loss of activity after 10 min
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
70
-
-
for 5 min, 3% activity recovered; for 5 min, NAD+ present during heating, 16% activity recovered
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-mercaptoethanol and NAD+, stabilization
-
NAD+ and sulfhydryl compounds are necessary for stabilization
-
2-mercaptoethanol and NAD+, no stabilization
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Glycerol
-
stable in 30% with 5 mM mercaptoethanol + 5 mM EDTA
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2C, overnight, purified enzyme, 20% loss of activity
-
-20C, 25% glycerol, retaines almost full activity, one year
-
-20C, several months
-
4C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q, TSK-GEL
-
using CM-trisacryl, DEAE-Sephacel, 5'-AMP-Sepharose affinity chromatography, and fast protein liquid chromatography on a mono-Q column
-
from putrescine-grown cells, using ammonium sulfate fractionation and column chromatography on Sephacryl S-300, DEAE-Sephacel and Blue-Sepharose CL6B
-
to homogeneity by ammonium sulfate precipitation, anion-exchange chromatography and hydrophobic interaction chromatography
-, P77674
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
Q8VWZ1, Q93YB2
using protamine, ammonium sulfate, acetone and column chromatography on DEAE-cellulose
-
using column chromatography on DEAE-cellulose
-
using column chromatography on DEAE-cellulose, DEAE-Toyopearl, Toyopearl HW-55 and Affi-Gel Blue
-
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
-
using ammonium sulfate fractionation and column chromatography on DEAE-cellulose, AMP-Sepharose, Sephadex G-200 and NAD+-Sepharose
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
;
Q8VWZ1, Q93YB2
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-, Q8VWZ1
AMADH may participate in processes of adaptation to stress events caused by mechanical injury, which involve polyamine catabolism, GABA production and lignification