EC Number | General Stability | Organism |
---|---|---|
2.3.1.61 | lyophilized enzyme loses more than 50% of its original activity | Sus scrofa |
2.3.1.61 | stable to frequent freezing and thawing | Sus scrofa |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.61 | 41000 | - |
24 * 41000, sedimentation equilibrium | Sus scrofa |
2.3.1.61 | 48000 | - |
24 * 48000, SDS-PAGE | Sus scrofa |
2.3.1.61 | 958000 | - |
analytical ultracentrifugation | Sus scrofa |
2.3.1.61 | 992000 | 1027000 | different preparations of the enzyme, analytical ultracentrifugation | Sus scrofa |
2.3.1.61 | 1000000 | - |
sedimentation equlibrium | Sus scrofa |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.61 | succinyl-CoA + dihydrolipoamide | Sus scrofa | plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex | CoA + S-succinyldihydrolipoamide | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.61 | Sus scrofa | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.61 | - |
Sus scrofa |
EC Number | Renatured (Comment) | Organism |
---|---|---|
2.3.1.61 | 10% recovery of enzyme activity after renaturation of SDS denatured enzyme (3%) | Sus scrofa |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.3.1.61 | heart | - |
Sus scrofa | - |
2.3.1.61 | muscle | - |
Sus scrofa | - |
EC Number | Storage Stability | Organism |
---|---|---|
2.3.1.61 | -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 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.61 | succinyl-CoA + dihydrolipoamide | - |
Sus scrofa | CoA + S-succinyldihydrolipoamide | - |
? | |
2.3.1.61 | succinyl-CoA + dihydrolipoamide | plays both a catalytic and a structural role in the 2-oxoglutarate dehydrogenase complex | Sus scrofa | CoA + S-succinyldihydrolipoamide | - |
? | |
2.3.1.61 | succinyl-CoA + dihydrolipoic acid | - |
Sus scrofa | CoA + succinyldihydrolipoate | - |
? | |
2.3.1.61 | succinyl-CoA + dihydrolipoyllysine | - |
Sus scrofa | CoA + succinyldihydrolipoyllysine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.61 | polymer | 24 * 48000, SDS-PAGE | Sus scrofa |
2.3.1.61 | polymer | 24 * 41000, sedimentation equilibrium | Sus scrofa |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.61 | 30 | - |
at pH 7.2 | Sus scrofa |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.61 | 70 | - |
loss of activity is slow up to 70°C, but rapid beyond 75°C | Sus scrofa |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.61 | 7.2 | - |
- |
Sus scrofa |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.61 | Lipoyl-protein | enzyme contains 8 mol of protein-bound lipoic acid per mol of enzyme | Sus scrofa |