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Literature summary for 6.2.1.5 extracted from
- Some physical parameters of succinyl-coenzyme A synthetase of Eschericha coli (1974), Can. J. Biochem., 52, 594-598.
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 29600 | - |
1 * 29600 (alpha) + 1 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
| 29600 | - |
2 * 29600 (alpha) + 2 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
| 38700 | - |
1 * 29600 (alpha) + 1 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
| 38700 | - |
2 * 29600 (alpha) + 2 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
| 141000 | - |
tertameric form, sedimentation equilibrium measurement | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + succinate + CoA | - |
Escherichia coli | ADP + phosphate + succinyl-CoA | - |
? |  |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 1 * 29600 (alpha) + 1 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
| tetramer | 2 * 29600 (alpha) + 2 * 38700 (beta), at concentrations above 1 mg/ml the enzyme exists predominantly as an alpha2beta2 tetramer, at lower concentrations, a significant fraction of the enzyme dissociates to an alphabeta dimer, SDS-PAGE | Escherichia coli |
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