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Literature summary for 1.2.1.105 extracted from
- Resolution and reconstitution of pig heart 2-oxoglutarate dehydrogenase complex (1971), J. Biochem., 69, 1143-1147 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| dissociation of the 2-oxoglutarate dehydrogenase complex into two fractions on a calcium phosphate gel-cellulose column in the presence of 2.5 M urea and 1% ammonium sulfate releases lipoamide dehydrogenase. The second fraction precipitates with between 0.23 and 0.40 saturation of ammonium sulfate and exhibits 2-oxoglutarate dehydrogenase and lipoate succinyltransferase activities. All three of the isolated enzymes are required to catalyze a CoA and NAD-linked oxidation of 2-oxoglutarate | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| heart | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 5.25 | - |
native complex, pH not specified in the publication, temperature not specified in the publication | Sus scrofa |
| 5.58 | - |
reconstituted complex, pH not specified in the publication, temperature not specified in the publication | Sus scrofa |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the native enzyme complex has a polyhedral structure with a diameter of about 260 A, electron microscopy | Sus scrofa |
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