| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
1 | MAPKK_star / MAPKKtyr
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.0463 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK_dash_tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
2 | MAPKK_star / MAPKKthr
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.0463 | 0.3 | 4 | explicit E-S complex | Substrate MAPK_dash_tyr
Product MAPK_star
|
| Rate consts same as for MAPKKtyr. |
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
1 | bRaf_Rap1GTP / braf_dash_Rap1_ dash_GTP2
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.16 | 0.3 | 4 | explicit E-S complex | Substrate MAPKK_dash_ser
Product MAPKK_star
|
| |
2 | Raf_dash_GTP_ dash_Ras / Raf_dash_GTP_ dash_Ras.2
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.1591 | 0.3 | 4 | explicit E-S complex | Substrate MAPKK_dash_ser
Product MAPKK_star
|
| Kinetics are the same as for the craf_1* activity, ie., k1=5.5e-6, k2=0.42, k3 = 0.105 These are basedo n Force et al PNAS USA 91 1270-1274, 1994., but k1 is scaled up 5x (ie., Km is scaled down 5x to the value used here and for craf_1* activity: Km = 0.1591). |
3 | braf_dash_GTP_ dash_Ras / braf_dash_GTP_ dash_Ras2
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.16 | 0.2 | 4 | explicit E-S complex | Substrate MAPKK_dash_ser
Product MAPKK_star
|
| |
4 | Raf_star_dash_ GTP_dash_Ras / Raf_star_dash_ GTP_dash_Ras.2
| mRNA synthesis Accession No. : 94 | kinetics Pathway No. : 1112 | 0.1591 | 0.3 | 4 | explicit E-S complex | Substrate MAPKK_dash_ser
Product MAPKK_star
|
| Same kinetics as other c-raf activated forms. See Force et al PNAS 91 1270-1274 1994. k1 = 1.1e-6, k2 = .42, k3 = 1.05 raise k1 to 5.5e-6 |