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Literature summary for 1.2.7.11 extracted from
- Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium (1981), Eur. J. Biochem., 116, 587-594.
General Stability
| General Stability | Organism |
|---|---|
| the enzymes requires high salt concentrations for stability. The half-life at 0.1 M KCl in 50 mM Tris/HC1 pH 8.0 is 3 h at 0°C | Halobacterium salinarum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| CoA | substrate inhibition | Halobacterium salinarum |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.07 | - |
2-oxobutyrate | pH and temperature not specified in the publication | Halobacterium salinarum | |
| 0.07 | - |
oxidized ferredoxin | cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication | Halobacterium salinarum | |
| 0.07 | - |
oxidized ferredoxin | cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication | Halobacterium salinarum | |
| 0.1 | - |
pyruvate | pH and temperature not specified in the publication | Halobacterium salinarum | |
| 1.1 | - |
2-oxoglutarate | pH and temperature not specified in the publication | Halobacterium salinarum | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | intact enzyme molecule contains two [4Fe-4S](2+,1+) clusters | Halobacterium salinarum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 42000 | - |
2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE | Halobacterium salinarum |
| 86000 | - |
2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE | Halobacterium salinarum |
| 165000 | - |
sedimentation velocity experiments | Halobacterium salinarum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Halobacterium salinarum | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Halobacterium salinarum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxobutyrate + CoA + oxidized ferredoxin | - |
Halobacterium salinarum | propanoyl-CoA + CO2 + reduced ferredoxin | - |
? | |
| 2-oxoglutarate + CoA + 2 oxidized ferredoxin | specific activity under optimal conditions is 36% of the specific activity with 2-oxobutyrate | Halobacterium salinarum | succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
| pyruvate + CoA + 2 oxidized ferredoxin | specific activity under optimal conditions is 65% of the specific activity with 2-oxobutyrate | Halobacterium salinarum | acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 2 * 86000 (alpha) + 2 * 42000 (beta), SDS-PAGE | Halobacterium salinarum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 52 | - |
- |
Halobacterium salinarum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | 52 | the enzyme is twice as active at 52°C as at 25°C | Halobacterium salinarum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Halobacterium salinarum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 8 | 9 | pH 8.0: 65% of maximal activity, pH 9.0: optimum, inactive below pH 7.0 | Halobacterium salinarum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| thiamine diphosphate | intact enzyme molecule contains two molecules of thiamin diphosphate | Halobacterium salinarum | |
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