EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.1.3.39 | NAD+ | stimulates slightly | Pseudomonas sp. | |
4.1.3.39 | NADH | stimulates | Pseudomonas sp. |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.10 | overexpression in Escherichia coli | Pseudomonas sp. |
4.1.3.39 | gene dmpG encodes the enzyme in the dmp operon together with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex | Pseudomonas sp. |
EC Number | General Stability | Organism |
---|---|---|
1.2.1.10 | activity is highest in HEPES buffer and somewhat lower in phosphate buffer, activity in Tris buffer is about half the rate in HEPES buffer | Pseudomonas sp. |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.3.39 | Zn2+ | strong inhibition | Pseudomonas sp. |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.1.3.39 | Mn2+ | stimulates 6-8fold at 1 mM | Pseudomonas sp. | |
4.1.3.39 | additional information | no effect by Mg2+ and Ca2+ | Pseudomonas sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.2.1.10 | 32500 | - |
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate | Pseudomonas sp. |
1.2.1.10 | 39000 | - |
2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate | Pseudomonas sp. |
1.2.1.10 | 148000 | - |
gel filtration, molecular mass of enzyme complex, occurs in complex with 4-hydroxy-2-ketovalerate | Pseudomonas sp. |
4.1.3.39 | 35000 | - |
2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE | Pseudomonas sp. |
4.1.3.39 | 40000 | - |
2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE | Pseudomonas sp. |
4.1.3.39 | 148000 | - |
enzyme in complex with aldehyde dehydrogenase, EC 1.2.1.10, gel filtration | Pseudomonas sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.10 | acetaldehyde + CoA + NAD+ | Pseudomonas sp. | - |
acetyl-CoA + NADH | - |
? | |
1.2.1.10 | acetaldehyde + CoA + NAD+ | Pseudomonas sp. CF 600 | - |
acetyl-CoA + NADH | - |
? | |
4.1.3.39 | 4-hydroxy-2-oxovalerate | Pseudomonas sp. | - |
pyruvate + acetaldehyde | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.10 | Pseudomonas sp. | - |
- |
- |
1.2.1.10 | Pseudomonas sp. CF 600 | - |
- |
- |
4.1.3.39 | Pseudomonas sp. | - |
gene dmpG | - |
4.1.3.39 | Pseudomonas sp. CF 600 | - |
gene dmpG | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.10 | - |
Pseudomonas sp. |
4.1.3.39 | co-purification with aldehyde dehydrogenase, EC 1.2.1.10, to homogeneity in a 5-step chromatographic procedure | Pseudomonas sp. |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.3.39 | 4.2 | - |
purified enzyme | Pseudomonas sp. |
EC Number | Storage Stability | Organism |
---|---|---|
1.2.1.10 | -80°C, 10 mM phosphate buffer, pH 7.5, 1 mM dithiothreitol | Pseudomonas sp. |
4.1.3.39 | -80°C, purified native enzyme, stable for at least 6 months | Pseudomonas sp. |
4.1.3.39 | 4-6°C, purified native enzyme, stable for at least 6 days | Pseudomonas sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.10 | acetaldehyde + CoA + NAD+ | - |
Pseudomonas sp. | acetyl-CoA + NADH | - |
? | |
1.2.1.10 | acetaldehyde + CoA + NAD+ | - |
Pseudomonas sp. CF 600 | acetyl-CoA + NADH | - |
? | |
1.2.1.10 | formaldehyde + CoA + NAD+ | - |
Pseudomonas sp. | formyl-CoA + NADH | - |
? | |
1.2.1.10 | formaldehyde + CoA + NAD+ | - |
Pseudomonas sp. CF 600 | formyl-CoA + NADH | - |
? | |
1.2.1.10 | isobutyraldehyde + CoA + NAD+ | - |
Pseudomonas sp. | isobutyryl-CoA + NADH | - |
? | |
1.2.1.10 | isobutyraldehyde + CoA + NAD+ | - |
Pseudomonas sp. CF 600 | isobutyryl-CoA + NADH | - |
? | |
1.2.1.10 | n-butyraldehyde + CoA + NAD+ | - |
Pseudomonas sp. | n-butyryl-CoA + NADH | - |
? | |
1.2.1.10 | n-butyraldehyde + CoA + NAD+ | - |
Pseudomonas sp. CF 600 | n-butyryl-CoA + NADH | - |
? | |
1.2.1.10 | propanal + CoA + NAD+ | initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde | Pseudomonas sp. | propionyl-CoA + NADH | - |
? | |
1.2.1.10 | propanal + CoA + NAD+ | initial rate of reaction with propanal is 2.7fold slower than that with acetaldehyde | Pseudomonas sp. CF 600 | propionyl-CoA + NADH | - |
? | |
4.1.3.39 | 4-hydroxy-2-oxovalerate | - |
Pseudomonas sp. | pyruvate + acetaldehyde | - |
? | |
4.1.3.39 | 4-hydroxy-2-oxovalerate | the enzyme utilizes the L-(S)-isomer or the racemate | Pseudomonas sp. | pyruvate + acetaldehyde | - |
? | |
4.1.3.39 | additional information | the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA | Pseudomonas sp. | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.1.10 | tetramer | 2 * 32500 + 2 * 39000, determined by nucleotide sequence, SDS-PAGE, two subunits of aldehyde dehydrogenase (acylating) and two of 4-hydroxy-2-ketovalerate | Pseudomonas sp. |
4.1.3.39 | More | the enzyme is encoded in the dmp operon with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex | Pseudomonas sp. |
4.1.3.39 | tetramer | 2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE | Pseudomonas sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.3.39 | 4-hydroxy-2-ketovalerate aldolase | - |
Pseudomonas sp. |
4.1.3.39 | HOA | - |
Pseudomonas sp. |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.3.39 | 25 | - |
assay at | Pseudomonas sp. |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
4.1.3.39 | 8.5 | 9 | - |
Pseudomonas sp. |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.10 | 6.5 | 8.5 | activity increases gradually over pH range from 6.5 to 8.5 | Pseudomonas sp. |
4.1.3.39 | 6.5 | 9 | - |
Pseudomonas sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.10 | CoA | - |
Pseudomonas sp. | |
1.2.1.10 | NAD+ | - |
Pseudomonas sp. | |
1.2.1.10 | NADH | rate of reaction with NADP+ is only 7% of that with NAD+ | Pseudomonas sp. |