1.2.1.19: aminobutyraldehyde dehydrogenase
This is an abbreviated version!
For detailed information about aminobutyraldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.19
-
1.2.1.19
-
badhs
-
choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
-
glycinebetaine
-
3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
-
aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
-
4-aminobutyrate
-
synthesis
- 1.2.1.19
-
badhs
- choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
- glycinebetaine
- 3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
- aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
- 4-aminobutyrate
- synthesis
Reaction
Synonyms
4-aminobutanal dehydrogenase, 4-aminobutyraldehyde dehydrogenase, ABAL dehydrogenase, ABALDH, ALDH10A8, ALDH10A9, AMADH, AMADH1, AMADH2, aminoaldehyde dehydrogenase, BADH, betaine aldehyde dehydrogenase, dehydrogenase, aminobutyraldehyde, EC 1.5.1.35, gadbh, gamma-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydroganase, gamma-aminobutyraldehyde dehydrogenase, gamma-guanidinobutyraldehyde dehydrogenase, MdAMADH1, MdAMADH2, More, NAD+-aminoaldehyde dehydrogenase, NAD+-dependent aminoaldehyde dehydrogenase, PatD, PsAMADH 1, PsAMADH 2, SlAMADH1, SlAMADH2, YdcW, ZmAMADH1a, ZmAMADH1b, ZmAMADH2
ECTree
Advanced search results
General Information
General Information on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
evolution
the enzyme is a member of the aldehyde dehydrogenase 10 family
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
malfunction
-
a mutant strain with disrupted gene gabdh shows an increase in gamma-aminobutyric acid (GABA), glutamate, succinate, and spermidine levels demonstrating a link between spermidine degradation and GABA synthesis in cyanobacteria. A DELTAgad:DELTAkgd strain shows upregulated expression of gene gadbh. Transcription levels of genes related to GABA metabolism in WT and mutants, overview
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
metabolism
enzyme LrAMADH2 is not involved in glycine betaine biosynthesis
metabolism
in higher plants, glycine betaine (GB) is synthesized by two-step oxidation of choline. The first step is catalyzed by ferredoxin-dependent choline monooxygenase (CMO, EC 1.14.15.7) to produce betaine aldehyde (BAL). BAL is converted to GB by aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.19) containing the activities of betaine aldehyde dehydrogenase (BADH)
metabolism
-
mannose treatment improves glutamate (Glu) content and the activity of diamine oxidase (DAO), and reduces gamma-aminobutyric acid transaminase (GABA-T) activity, which enriches GABA biosynthesis. Mannose treatment enhances the activities of diamine oxidase (DAO), polyamine oxidase (PAO), and 4-aminobutyraldehyde dehydrogenase (ABALDH), and increases the conversion rate of free polyamine. Mannose treatment may boost the accumulation of GABA in sprouting broccoli, via enhancing GAD activity and providing more glutamate. GABA is degraded by GABA-T, which uses pyruvate or glyoxalate as amino acceptor to convert GABA into succinate semialdehyde (SSA). SSA dehydrogenase catalyzes the irreversible NADP+-dependent oxidation of SSA to succinate. GABA-T activity is significantly reduced in broccoli sprouts under mannose treatment in late growth stage. Polyamines are mainly about free Put, free Spd and free Spm. Arginine is converted to fPut via alternative arginase and ornithine decarboxylase. fPut in turn is converted to fSpd and fSpm via spermidine synthase and spermine synthase, respectively. PAO is responsible for catalyzing the oxidation or back-conversion of fSpm and fSpd, resulting in the formation of 1,3-diaminopropane, and their degradation to 4-aminobutyraldehyde. DAO catalyze the degradation of fPut to 4-aminobutyraldehyde, which in turn are converted to GABA by ABALDH
the enzyme produces gamma-butyric acid, GABA, and beta-alanine from 4-aminobutanal and 3-aminopropanal , respectively
physiological function
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
physiological function
isozyme LrAMADH1 shows low betaine aldehyde dehydrogenase activity, but is proved as bona fide BADH, which involves in glycine betaine (GB) synthesis in planta and responds to salt stress in Lycium ruthenicum plants
physiological function
-
role of gamma-aminobutanal dehydrogenase in maintaining an intact tricarboxylic acid cycle in Synechocystis. The mutational analysis suggests a possible existence of the Spd to gamma-AB to GABA pathway in Synechocystis
-
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
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
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
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
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
additional information
AMADH2 lacks Ile445, that is contained in all enzymes with BADH activity (EC 1.2.1.8)
additional information
AMADH2 lacks Ile445, that is contained in all enzymes with BADH activity (EC 1.2.1.8)
additional information
-
AMADH2 lacks Ile445, that is contained in all enzymes with BADH activity (EC 1.2.1.8)
additional information
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity
additional information
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity
additional information
-
for Ile445 containing AMADHs, the existence of Asn290 rather than Thr290 leads to detectable BADH activity