EC Number   |
Subunits |
Reference |
|---|
    2.7.1.30 | dimer or tetramer |
2 or 4 * 60000, in solution, the enzyme exists in a dimer-tetramer equilibrium |
722712 |
| 2.7.1.30 | hexamer |
Tk-GK has a hexameric form with a threefold axis in the crystal lattice |
-, 761561 |
| 2.7.1.30 | homodimer |
2 * 60400, calculated from amino acid sequence |
738553 |
| 2.7.1.30 | homodimer |
2 x 57289 (501 residues plus an additional six N-terminal residues from the linker region), mass spectrometry |
705779 |
| 2.7.1.30 | homodimer |
crystal structure |
702293 |
| 2.7.1.30 | homotetramer |
dimer-tetramer equilibrium in solution, tetramer in the crystal |
701931 |
| 2.7.1.30 | monomer |
1 * 53000 |
641288 |
| 2.7.1.30 | More |
in the absence of glycerol, Tk-GK is a dimer in solution. In the presence of its glycerol substrate, it becomes a hexamer consisting of three symmetrical dimers about the threefold axis. Through glycerol binding, all Tk-GK molecules in the hexamer are in closed form as a result of domain-motion. The closed form of Tk-GK has 10fold higher ATP affinity than the open form of Tk-GK. The hexamer structure stabilizes the closed conformation and enhances ATP binding affinity when the glycerol kinase is bound to glycerol |
-, 761561 |
| 2.7.1.30 | tetramer |
- |
641309 |
| 2.7.1.30 | tetramer |
4 * 50000, SDS-PAGE |
641328 |
