EC Number   |
Subunits |
Reference |
|---|
    2.6.1.16 | ? |
? * 77000, SDS-PAGE |
639914 |
| 2.6.1.16 | ? |
x * 68600, calculated for native protein, x * 69600, calculated, and x * 69400, SDS-PAGE, His-tagged protein, respectively |
684758 |
| 2.6.1.16 | ? |
x * 79000, SDS-PAGE |
739575 |
| 2.6.1.16 | ? |
x * 80047, calculated, x * 90000, SDS-PAGE |
737920 |
| 2.6.1.16 | dimer |
2 * 70000, calculated by means of crystalline structure determined by X ray diffraction |
639932 |
| 2.6.1.16 | dimer |
2 * 70800, SDS-PAGE |
639922 |
| 2.6.1.16 | dimer |
sedimentation velocity experiments show that at low concentration the enzyme is mainly present as a dimer. At a higher protein concentration the equilibrium between the two forms of GlmS is significantly displaced toward the oligomeric form |
721419 |
| 2.6.1.16 | dimer |
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer |
722779 |
| 2.6.1.16 | hexamer |
the enzyme is regulated by a morpheein-type allosteric mechanism, in which functional dimeric GlmS is in equilibrium with the inactive hexamer |
722779 |
| 2.6.1.16 | homotetramer |
4 * 39500, hexose phosphate-isomerizing domain, Superdex 200 HR 10/30 gel filtration |
671896 |
