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Literature summary for 1.5.5.1 extracted from
- Electron-transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox, and catalytic properties (1985), Biochemistry, 24, 3913-3921.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.00031 | - |
hydroquinone electron-transferring flavoprotein | - |
Sus scrofa | |
| 0.00032 | - |
electron-transferring flavoprotein | - |
Sus scrofa |  |
| 0.0077 | - |
semiquinone electron-transferring flavoprotein | - |
Sus scrofa |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Sus scrofa | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+/Fe3+ | enzyme contains a single 4Fe-1S cluster per subunit and flavin | Sus scrofa |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 69000 | - |
x * 69000, SDS-PAGE | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| submitochondrial particles, cholate extract, ammonium sulfate, DEAE-Bio gel, hydroxyapatite | Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.093 | - |
- |
Sus scrofa |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -70°C, 1-2 mg/ml protein, 20% glycerol, several months, no loss in activity | Sus scrofa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol | - |
Sus scrofa | semiquinone electron transferring flavoprotein + ubiquinone | - |
r | |
| reduced electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinone | - |
Sus scrofa | electron-transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-pentyl-1,4-benzoquinol | - |
r | |
| reduced electron-transferring flavoprotein + nitro blue tetrazolium | - |
Sus scrofa | electron transferring-flavoprotein + reduced nitro blue tetrazolium | - |
? | |
| semiquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinone | disproportion and comproportion with ubiqinone-1 as the terminal oxidant | Sus scrofa | electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + 2,3-dimethoxy-5-methyl-6-(3-methylbut-2-en)-1,4-benzoquinol | - |
r | |
| semiquinone electron transferring flavoprotein + ubiquinone | - |
Sus scrofa | electron-transferring flavoprotein + hydroquinone electron transferring flavoprotein + ubiquinol | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 69000, SDS-PAGE | Sus scrofa |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 78 | - |
electron-transferring flavoprotein | comproportionation of electron-transferring flavoprotein and hydroquinone electron-transferring flavoprotein | Sus scrofa | |
| 200 | - |
electron-transferring flavoprotein | disproportion of semiquinone electron-transferring flavoprotein | Sus scrofa | |
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