EC Number   |
Subunits |
Reference |
|---|
    1.4.1.13 | dimer |
1 * 145000 + 1 * 55000, SDS-PAGE |
391440 |
| 1.4.1.13 | dimer |
1 * 158000 + 1 * 54000, SDS-PAGE |
391449 |
| 1.4.1.13 | dimer |
1 * 160000 + 1 * 56000 |
391459 |
| 1.4.1.13 | heterodimer |
- |
676331 |
| 1.4.1.13 | homodimer |
2 * 200000, cryoelectron microscopy and small angle X-ray scattering |
687801 |
| 1.4.1.13 | homohexamer |
6 * 200000, cryoelectron microscopy and small angle X-ray scattering, the hexamer exhibits a concentration-dependent equilibrium with monomers and dimers, in solution the hexamer is destabilized by high ionic strength and to a lower extent by the reaction product NADP+ |
687801 |
| 1.4.1.13 | More |
analysis by synchrotron radiation x-ray solution scattering, alpha subunit and alphabeta holoenzyme are tetrameric in solution, beta subunit is a mixture of monomers and dimers. The (alphabeta)4 holoenzyme is similar to the tetrameric alpha4 complex with the beta subunits occupying the periphery, thus allowing independent catalytic activities of the alphabeta protomers |
656149 |
| 1.4.1.13 | More |
modelling of unliganded alpha subunit as well as in complex with L-glutamine and 2-oxoglutarate, subunit exists in a catalytically inactive conformation unable to bind glutamine, and in a catalytically competent conformation, which is stabilized by the glutamine substrate. Binding of L-methionine sulfone causes a coordinated rigid-body motion that results in the inactive conformation |
657306 |
| 1.4.1.13 | octamer |
4 * 135000 + 4 * 50000, SDS-PAGE |
391446 |
| 1.4.1.13 | octamer |
4 * 53000 + 4 * 135000, SDS-PAGE, urea polyacrylamide gel electrophoresis |
391438 |
