Table 1.
AAs alter the PEP binding affinity of PKM2 and vice versa
The concentration of PKM2 was kept constant at 1.6 μm for all of the studies. In the top two rows, the binding affinities of PKM2 for PEP and ADP were calculated in the absence and presence of AAs with 5 mm MgCl2 in the buffer. In the bottom three rows, binding affinities of PKM2 for the AAs in the absence and presence of PEP (2 mm) + MgCl2 (1 mm) and MgCl2 (1 mm) are shown (related to Figs. 2 and 3).
| Titrant | Ligand (concentration in mm) | Kd |
|---|---|---|
| μm | ||
| PEP | 10 ± 2 | |
| Asn (1) | 0.27 ± 0.0 | |
| Asp (1) | 0.29 ± 0.01 | |
| Val (1) | 81 ± 21 | |
| Val (10) | 505 ± 26 | |
| ADP | 237 ± 54 | |
| Asn (1) | 345 ± 33 | |
| Asp (1) | 585 ± 188 | |
| Val (1) | 363 ± 57 | |
| Asn | 11 ± 2 | |
| PEP (2) + MgCl2 (1) | 2 ± 0 | |
| MgCl2 (1) | 27 ± 5 | |
| Asp | 35 ± 7 | |
| PEP (2) + MgCl2 (1) | 8 ± 1 | |
| MgCl2 (1) | 95 ± 16 | |
| Val | 757 ± 120 | |
| PEP (2) + MgCl2 (1) | 4296 ± 604 | |
| MgCl2 (1) | 2170 ± 317 |