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Literature summary for 1.2.1.19 extracted from
- Properties of gamma-aminobutyraldehyde dehydrogenase from Escherichia coli (1987), Biochimie, 69, 1161-1168.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NADH | competitive inhibitor with respect to NAD+ | Escherichia coli |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0313 | - |
DELTA1-pyrroline | - |
Escherichia coli | |
| 0.0538 | - |
NAD+ | - |
Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | no requirement for bivalent cations | Escherichia coli |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 95000 | - |
2 * 95000, SDS-PAGE | Escherichia coli |
| 195000 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-aminobutanal + NAD+ + H2O | Escherichia coli | role in putrescine degradative pathway | 4-aminobutanoate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
K-12 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| from putrescine-grown cells, using ammonium sulfate fractionation and column chromatography on Sephacryl S-300, DEAE-Sephacel and Blue-Sepharose CL6B | Escherichia coli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-aminobutanal + NAD+ + H2O | - |
Escherichia coli | 4-aminobutanoate + NADH + H+ | - |
? | |
| 4-aminobutanal + NAD+ + H2O | role in putrescine degradative pathway | Escherichia coli | 4-aminobutanoate + NADH + H+ | - |
? | |
| DELTA1-pyrroline + NAD+ + H2O | - |
Escherichia coli | 4-aminobutanoate + NADH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 95000, SDS-PAGE | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
increase in dehydrogenase capacity from 25°C to 75°C | Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
- |
35 | up to 5 min, stable | Escherichia coli |
| 35 | - |
unstable above | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.4 | - |
in the presence of sodium citrate buffer | Escherichia coli |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 7 | at pH 4.0 and pH 7.0: about 60% of activity maximum | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | absolutely dependent on | Escherichia coli | |
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