EC Number   |
Subunits |
Reference  |
|---|
    4.1.1.18 | ? |
? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits |
37283 |
| 4.1.1.18 | ? |
x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength |
-, 37289 |
| 4.1.1.18 | dimer |
2 * 44000, SDS-PAGE |
37290 |
| 4.1.1.18 | ? |
x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length |
-, 37293 |
| 4.1.1.18 | monomer |
1 * 95000, SDS-PAGE |
37297 |
| 4.1.1.18 | decamer |
10 * 80000, SDS-PAGE |
37299 |
| 4.1.1.18 | heptamer |
7 * 79000, SDS-PAGE |
-, 37300 |
| 4.1.1.18 | dimer |
2 * 42000, SDS-PAGE |
654982 |
| 4.1.1.18 | More |
enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity |
665713 |
| 4.1.1.18 | hexamer |
isozyme TT1465, crystallization data |
-, 666850 |
