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Literature summary for 2.3.1.61 extracted from
- Mammalian alpha-keto acid dehydrogenase complexes. 8. Properties and subunit composition of the pig heart lipoate succinyltransferase (1974), J. Biol. Chem., 249, 191-198.
General Stability
| General Stability | Organism |
|---|---|
| lyophilized enzyme loses more than 50% of its original activity | Sus scrofa |
| stable to frequent freezing and thawing | Sus scrofa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41000 | - |
24 * 41000, sedimentation equilibrium | Sus scrofa |
| 48000 | - |
24 * 48000, SDS-PAGE | Sus scrofa |
| 958000 | - |
analytical ultracentrifugation | Sus scrofa |
| 992000 | 1027000 | different preparations of the enzyme, analytical ultracentrifugation | Sus scrofa |
| 1000000 | - |
sedimentation equlibrium | Sus scrofa |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-CoA + dihydrolipoamide | Sus scrofa | plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex | CoA + S-succinyldihydrolipoamide | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Sus scrofa |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| 10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%) | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Sus scrofa | - |
| muscle | - |
Sus scrofa | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -18°C, 0.05 M potassium phosphate buffer, pH 7.0, containing 0.05 mM EDTA, stable for over 6 months without significant loss of activity, despite frequent freezing and thawing | Sus scrofa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| succinyl-CoA + dihydrolipoamide | - |
Sus scrofa | CoA + S-succinyldihydrolipoamide | - |
? | |
| succinyl-CoA + dihydrolipoamide | plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex | Sus scrofa | CoA + S-succinyldihydrolipoamide | - |
? | |
| succinyl-CoA + dihydrolipoic acid | - |
Sus scrofa | CoA + succinyldihydrolipoate | - |
? | |
| succinyl-CoA + dihydrolipoyllysine | - |
Sus scrofa | CoA + succinyldihydrolipoyllysine | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| polymer | 24 * 48000, SDS-PAGE | Sus scrofa |
| polymer | 24 * 41000, sedimentation equilibrium | Sus scrofa |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
at pH 7.2 | Sus scrofa |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
loss of activity is slow up to 70°C, but rapid beyond 75°C | Sus scrofa |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
- |
Sus scrofa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Lipoyl-protein | enzyme contains 8 mol of protein-bound lipoic acid per mol of enzyme | Sus scrofa | |
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