| |
Enzyme Molecule /
Enzyme Activity | Pathway Name /
Pathway No. | Km
(uM) | kcat
(s^-1) | Ratio
(k2/k3) | Enzyme Type | Reagents |
| 1 | MAPKK* /
MAPKKtyr | MAPK
Pathway No. 211 | 0.0462963 | 0.15 | 4 | explicit E-S complex | Substrate:
MAPK
Product :
MAPK-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* /
MAPKKthr | MAPK
Pathway No. 211 | 0.0462963 | 0.15 | 4 | explicit E-S complex | Substrate:
MAPK-tyr
Product :
MAPK*
|
| | Rate consts same as for MAPKKtyr. |
| 3 | Raf-GTP-Ras* /
Raf-GTP-Ras*.1 | MAPK
Pathway No. 211 | 0.159091 | 0.105 | 4 | explicit E-S complex | Substrate:
MAPKK
Product :
MAPKK-ser
|
| | Kinetics are the same as for the craf-1* activity, ie., k1=1.1e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6 |
| 4 | Raf-GTP-Ras* /
Raf-GTP-Ras*.2 | MAPK
Pathway No. 211 | 0.159091 | 0.105 | 4 | explicit E-S complex | Substrate:
MAPKK-ser
Product :
MAPKK*
|
| | 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 |
and 
color.
arrow indicates that ordering is done according to ascending or descending order.