TABLE 1.
Kinetic parameters of binary binding between wild type PRMT1 and different H4 peptides
These parameters were yielded from a global simulation of the stopped-flow kinetics based on the model shown in Fig. 4C. NC, not constrained.
| Peptide | k1 (range) | k1 (range) | Kd1 | k2 (range) | k−2 (range) | Kd2 (range) |
|---|---|---|---|---|---|---|
| s−1·μm−1 | s−1 | μm | s−1·μm−1 | s−1 | μm | |
| H4 | 79 (63–110) | 115 (92–161) | 1.46 | 0.51 (0.21–18) | 84 (>18) | 164 (120–300) |
| H4me1 | 74 (65–159) | 34 (18–41) | 0.46 | 0.77 (>0.01) | 25 (NC) | 32 (NC) |
| H4me2a | 90 (78–107) | 144 (125–172) | 1.6 | 0.41 (0.21–1) | 76 (16–377) | 185 (160–230) |