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Literature summary for 1.2.1.19 extracted from
- NAD+-aminoaldehyde dehydrogenase candidates for 4-aminobutyrate (GABA) and beta-alanine production during terminal oxidation of polyamines in apple fruit (2015), FEBS Lett., 589, 2695-2700 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene AMADH1, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH1 in Arabidopsis thaliana Col-0 protoplasts | Malus domestica |
| gene AMADH2, sequence comparisons and phylogenetic analysis, recombinant expression of GFP-tagged isozyme PsAMADH2 in Arabidopsis thaliana Col-0 protoplasts | Malus domestica |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Malus domestica | |
| 0.0086 | - |
3-aminopropanal | pH 9.8, temperature not specified in the publication, isozyme MdAMADH2 | Malus domestica |  |
| 0.016 | - |
3-aminopropanal | pH 9.8, temperature not specified in the publication, isozyme MdAMADH1 | Malus domestica | |
| 0.0338 | - |
NAD+ | pH 9.8, temperature not specified in the publication, isozyme MdAMADH1 | Malus domestica | |
| 0.0828 | - |
NAD+ | pH 9.8, temperature not specified in the publication, isozyme MdAMADH2 | Malus domestica | |
| 0.0848 | - |
4-aminobutanal | pH 9.8, temperature not specified in the publication, isozyme MdAMADH1 | Malus domestica | |
| 0.16 | - |
4-aminobutanal | pH 9.8, temperature not specified in the publication, isozyme MdAMADH2 | Malus domestica | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Malus domestica | 5829 | - |
| peroxisome | - |
Malus domestica | 5777 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-aminopropanal + NAD+ + H2O | Malus domestica | - |
3-aminopropanoate + NADH + H+ | - |
? | |
| 4-aminobutanal + NAD+ + H2O | Malus domestica | - |
4-aminobutanoate + NADH + 2 H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Malus domestica | A0A0E3T3B5 | - |
- |
| Malus domestica | A0A0E3T552 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| fruit | - |
Malus domestica | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-aminopropanal + NAD+ + H2O | - |
Malus domestica | 3-aminopropanoate + NADH + H+ | - |
? | |
| 3-aminopropanal + NAD+ + H2O | best substrate | Malus domestica | 3-aminopropanoate + NADH + H+ | - |
? | |
| 4-aminobutanal + NAD+ + H2O | - |
Malus domestica | 4-aminobutanoate + NADH + 2 H+ | - |
? | |
| 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 | Malus domestica | ? | - |
? | |
| 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 | Malus domestica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 54600, about, sequence calculation | Malus domestica |
| ? | x * 55000, about, sequence calculation | Malus domestica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 4-aminobutanal dehydrogenase | - |
Malus domestica |
| AMADH | - |
Malus domestica |
| AMADH1 | - |
Malus domestica |
| AMADH2 | - |
Malus domestica |
| MdAMADH1 | - |
Malus domestica |
| MdAMADH2 | - |
Malus domestica |
| NAD+-aminoaldehyde dehydrogenase | - |
Malus domestica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.8 | - |
- |
Malus domestica |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | 11 | activity range, profile overview | Malus domestica |
| 7.5 | 11.5 | activity range, profile overview | Malus domestica |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Malus domestica | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the aldehyde dehydrogenase 10 family | Malus domestica |
| physiological function | the enzyme produces gamma-butyric acid, GABA, and beta-alanine from 4-aminobutanal and 3-aminopropanal , respectively | Malus domestica |
| physiological function | the enzyme produces gamma-butyric acid, GABA, and beta-alanine from 4-aminobutanal and 3-aminopropanal, respectively | Malus domestica |
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Release 2023.1 (January 2023)
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