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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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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
root growth of single loss-of-function mutants is more sensitive to salinity than wild-type plants, and this is accompanied by reduced GABA accumulation; root growth of single loss-of-function mutants is more sensitive to salinity than wild-type plants, and this is accompanied by reduced GABA accumulation
metabolism
physiological function
additional information
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family; the enzyme is a member of the aldehyde dehydrogenase 10 family
metabolism
AMADH participates in carnitine biosynthesis in plants; AMADH participates in carnitine biosynthesis in plants
metabolism
-
as alternative to GABA production by glutamate decarboxylation, another route for the production of GABA via putrescine is established in Corynebacterium glutamicum
physiological function
the enzyme produces gamma-butyric acid, GABA, and beta-alanine from 4-aminobutanal and 3-aminopropanal , respectively; the enzyme produces gamma-butyric acid, GABA, and beta-alanine from 4-aminobutanal and 3-aminopropanal, respectively
physiological function
the enzyme shows maximal activity and catalytic efficiency with NAD+ and 3-aminopropanal, followed by 4-aminobutanal. Negligible activity is obtained with betaine aldehyde. NAD+ reduction is accompanied by the production of gamma-aminobutyrate, GABA, and beta-alanine, respectively, with 4-aminobutanal and 3-aminopropanal as substrates; the enzyme shows maximal activity and catalytic efficiency with NAD+ and 3-aminopropanal, followed by 4-aminobutanal. Negligible activity is obtained with betaine aldehyde. NAD+ reduction is accompanied by the production of gamma-aminobutyrate, GABA, and beta-alanine, respectively, with 4-aminobutanal and 3-aminopropanal as substrates
additional information
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
additional information
-
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
additional information
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
additional information
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
additional information
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
additional information
-
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid
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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
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 + 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+
-
-
-
?
3aminopropanal+ NAD+ + H2O
3-aminobutanoate + 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-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
high activity
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
best substrate
-
-
?
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 + 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-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+
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+
-
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 + 2 H+
-
-
-
?
4-guanidinobutyraldehyde + NAD+ + H2O
4-guanidinobutanoate + NADH + 2 H+
-
-
-
?
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 + 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-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
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
no activity with betaine aldehyde, propionaldehyde, and acetaldehyde
-
-
-
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-aminobutanal. Very low activity with betaine aldehyde
-
-
-
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-aminobutanal. Very low activity with betaine aldehyde
-
-
-
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-aminobutanal. Very low activity with betaine aldehyde
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
?
-
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 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
?
-
-
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
-
-
-
additional information
?
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate
-
-
-
additional information
?
-
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
-
-
-
additional information
?
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
-
-
-
additional information
?
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
-
-
-
additional information
?
-
-
identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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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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
3-aminobutanal + NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
Q9S795, Q9STS1
best substrate
-
-
?
3aminopropanal+ NAD+ + H2O
3-aminobutanoate + NADH + 2 H+
C0P9J6, C6KEM4, G5DDC2
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
Q9S795, Q9STS1
best substrate
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
A0A0E3T3B5, A0A0E3T552
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
Q8VWZ1, Q93YB2
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
B6ECN9
-
-
-
?
3-aminopropanal + NAD+ + H2O
3-aminopropanoate + NADH + 2 H+
C0P9J6, C6KEM4, G5DDC2
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
Q9S795, Q9STS1
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
A0A0E3T3B5, A0A0E3T552
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
Q8VWZ1, Q93YB2
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
B6ECN9
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH + 2 H+
C0P9J6, C6KEM4, G5DDC2
-
-
-
?
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+
Desulfovibrio vulgaris Marburg / DSM 2119
-
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+
NAD+
binding structure and site; binding structure and site; binding structure and site
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
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-guanidinobutyraldehyde
substrate inhibition; substrate inhibition
4-propionylaminobutanal
causes substrate inhibition at high concentration
-
N,N,N-trimethyl-4-aminobutyraldehyde
substrate inhibition; substrate inhibition
N-ethylmaleimide
-
inactivation ocurrs due to interaction with a cysteine residue located at or near the cofactor binding site of the enzyme molecule
additional information
-
addition of 4-aminobutyric acid, GABA, to the growth medium hardly affects growth of Corynebacterium glutamicum, since a half-inhibitory concentration of 1.1 M GABA is determined
-
additional information
EDTA has no significant effect on the enzyme activity
-
additional information
isozyme PsAMADH 1 shows no substrate inhibition
-
additional information
isozyme PsAMADH 1 shows no substrate inhibition
-
additional information
no substrate inhibtiion by betaine aldehyde, 3-pyridine carboxaldehyde, 4-pyridine carboxaldehyde, and 4-aminobutanal
-
additional information
-
no substrate inhibtiion by betaine aldehyde, 3-pyridine carboxaldehyde, 4-pyridine carboxaldehyde, and 4-aminobutanal
-
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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
1.42
2,2-dimethyl-4-aminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.506
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.003
Capronaldehyde
-
same value with benzaldehyde, constant substrate 1 mM NAD+
0.266
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.477
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.366
2-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
-
0.638
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.0935
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.183
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.189
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.525
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.0086
3-aminopropanal
pH 9.8, temperature not specified in the publication, isozyme MdAMADH2
0.016
3-aminopropanal
pH 9.8, temperature not specified in the publication, isozyme MdAMADH1
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
0.13
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, 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
-
0.531
3-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.0651
3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
0.49 - 2
3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
0.0848
4-aminobutanal
pH 9.8, temperature not specified in the publication, isozyme MdAMADH1
0.16
4-aminobutanal
pH 9.8, temperature not specified in the publication, isozyme MdAMADH2
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+
0.285
Betaine aldehyde
-
250 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
0.0132
NAD+
with 4-aminobutanal, pH 8.5, 22°C, recombinant enzyme
0.0208
NAD+
with 3-aminopropanal, pH 8.5, 22°C, recombinant enzyme
0.0338
NAD+
pH 9.8, temperature not specified in the publication, isozyme MdAMADH1
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
0.0736
NAD+
with 3-aminopropanal, pH 9.5, 22°C, recombinant enzyme
0.0828
NAD+
pH 9.8, temperature not specified in the publication, isozyme MdAMADH2
0.086
NAD+
with 4-aminobutanal, pH 9.5, 22°C, recombinant enzyme
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+
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
2,2-dimethyl-4-aminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
5.8
2,2-dimethyl-4-propionylaminobutanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
1.41
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
14.4
2,2-dimethyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
1.2
2-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
-
2.87
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
12.1
2-methyl-3-butyrylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
2.03
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
6.49
2-methyl-3-propionylaminopropanal
isozyme PsAMADH 2, pH 9.0, 30°C
-
2.32
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 1, pH 9.0, 30°C
-
4.08
2-methyl-4-propionylaminobutanal
isozyme PsAMADH 2, 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
-
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
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
40
NAD+
with 3-aminopropanal, pH 8.5, 22°C, recombinant enzyme
60
NAD+
with 3-aminopropanal, pH 9.5, 22°C, recombinant enzyme
150
NAD+
with 4-aminobutanal, pH 9.5, 22°C, recombinant enzyme
260
NAD+
with 4-aminobutanal, pH 8.5, 22°C, recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
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
9.4 - 9.8
9.5
10.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
AMADH activity increases with a pH ranging from pH 3.0 to pH 8.0, but it decreases drastically when pH continuously rises from pH 8.0 to pH 10.0. At pH 9.0, the activity decreases by 75% compared to pH 8.0
6.5 - 11
the enzyme retains approximately 20% of its maximal substrate-limited, 3-aminopropanal-dependent activity at pH 7.5 and is inactive at pH 6.5; the enzyme retains approximately 20% of its maximal substrate-limited, 3-aminopropanal-dependent activity at pH 7.5 and is inactive at pH 6.5
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
37
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TEMPERATURE RANGE
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
additional information
-
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 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
additional information
isozyme tissue distribution, overview; isozyme tissue distribution, overview
additional information
-
isozyme tissue distribution, overview; isozyme tissue distribution, overview
additional information
isozyme tissue distribution, overview; isozyme tissue distribution, overview; isozyme tissue distribution, overview
additional information
isozyme tissue distribution, overview; isozyme tissue distribution, overview; isozyme tissue distribution, overview
additional information
isozyme tissue distribution, overview; isozyme tissue distribution, overview; isozyme tissue distribution, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
AtALDH10A8 is cytosolic, although the N-terminal 140 amino acid sequence of AtALDH10A8 localizes to the plastid and to the leucoplast
AtALDH10A8 is cytosolic, although the N-terminal 140 amino acid sequence of AtALDH10A8 localizes to the plastid and to the leucoplast
probably, SlAMADH1 ends with a tripeptide SKN, which is not a peroxisomal targeting signal
the isozyme carries the SKL C-terminal peroxisomal targeting signal (PTS-1)
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
?
x * 54600, about, sequence calculation; x * 55000, about, sequence calculation
dimer
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site
dimer
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site; plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site
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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
wild-type SlAMADH1 with 5 mM NAD+is crystallized over a reservoir containing 23% PEG 1000, 0.1 M HEPES, pH 7.5, mutant E260A of SlAMADH1 with 5 mM NAD+ is crystallized over a reservoir containing 15% PEG 1500, 0.1 M imidazole, pH 7.0, and 10% glycerol, sitting drop vapor diffusion method, cryoprotectant solution consits of mother liquor supplemented with 25% PEG 400 for SlAMADH1 or 20% glycerol for the E260A mutant, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model
wild-type ZnAMADH1a with 5 mM NAD+ is crystallized over a reservoir containing 16% PEG 4000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, sitting drop vapor diffusion method, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model
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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
purified enzyme, pH 8.0, rapid inactivation above 50°C, loss of almost 50% activity at 60°C
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
-
native enzyme 27.22fold from germinated seeds by ammonium sulfate fractionation, desalting gel filtration, and anion exchange chromatography
recombinant His-tagged enzyme from in Escherichia coli by affinity chromatography; recombinant His-tagged enzyme from in Escherichia coli by affinity chromatography
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
DNA and amino acid sequence determination and analysis, sequence comparisons
gene AMADH1, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH1 in Arabidopsis thaliana Col-0 protoplasts; gene AMADH2, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH2 in Arabidopsis thaliana Col-0 protoplasts
gene ataldh10A8, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplast, recombinant expression of His-tagged enzyme in in Escherichia coli; gene ataldh10A9, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana protoplast, recombinant expression of His-tagged enzyme in in Escherichia coli
gene patD, recombinant expression in Corynebacterium glutamicum strain ATCC 13032 with deleted gabTDP operon and cgmA gene
-
isozyme SlAMADH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme SlAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
isozyme ZmAMADH1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme ZmAMADH1b, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis; isozyme ZmAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
AtALDH109 gene is expressed constitutively in Arabidopsis thaliana, although it has been reported to be weakly induced by salinity and dehydration; AtALDH10A8 gene is expressed constitutively in Arabidopsis thaliana, although it has been reported to be weakly induced by salinity and dehydration
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of a ataldh10A8 T-DNA-insertion mutant that has lower levels of GABA than wild-type plants in response to salinity treatment and are more prone to salinity stress; generation of a ataldh10A9 T-DNA-insertion mutant that has lower levels of GABA than wild-type plants in response to salinity treatment and are more prone to salinity stress
additional information
generation of a ataldh10A8 T-DNA-insertion mutant that has lower levels of GABA than wild-type plants in response to salinity treatment and are more prone to salinity stress; generation of a ataldh10A9 T-DNA-insertion mutant that has lower levels of GABA than wild-type plants in response to salinity treatment and are more prone to salinity stress
additional information
-
a putrescine-producing recombinant Corynebacterium glutamicum strain is converted into a 4-aminobutyric acid, GABA, producing strain by heterologous expression of putrescine transaminase (PatA) and gamma-aminobutyraldehyde dehydrogenase (PatD) genes from Escherichia coli. The resultant strain produces 5.3 g/l of GABA. GABA production is improved further by adjusting the concentration of nitrogen in the culture medium, by avoiding the formation of the by-product N-acetylputrescine and by deletion of the genes for GABA catabolism and GABA re-uptake
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
the enzyme is useful for GABA production in an engineered strain of Corynebacterium glutamicum produces 5.3 g/l of GABA
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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