| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
MAPKKthr
Enzyme Molecule:
MAPKK* | 0.0462963 | 0.15 | 4 | explicit E-S complex | MAPK-tyr
| MAPK*
|
| | Rate consts same as for MAPKKtyr. |
| 2 |
Enzyme Activity:
MAPKKtyr
Enzyme Molecule:
MAPKK* | 0.0462963 | 0.15 | 4 | explicit E-S complex | MAPK
| 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 |
| 3 |
Enzyme Activity:
MKP-1-synthesis
Enzyme Molecule:
nuc_MAPK* | 27.3632 | 0.0001 | 10 | explicit E-S complex | MKP-1-gene
| MKP-1
|
| | 5 Feb 2000 This is a crude model of activation of MKP1 production by MAPK. Time-course poorly constrained: 10 min to > 100 min. Rates are further constrained by the known degradation rates of MKP-1, also in this model. Peak MKP-1 is about 10 times basal (from Brondello et al Science 286:2514 1999). Max MAPK ~.25 uM, degradation 45 min. So this enz has to provide 22nM MKP every 45 min. |
| 4 |
Enzyme Activity:
MKP1*-thr-deph
Enzyme Molecule:
MKP-1** | 0.0666667 | 1 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | MAPK*
| MAPK-tyr
|
| | 3 Feb 2000. Same rates as MKP1 |
| 5 |
Enzyme Activity:
MKP1*-tyr-deph
Enzyme Molecule:
MKP-1** | 0.0666667 | 1 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | MAPK-tyr
| MAPK
|
| | 3 Feb 2000. Same rates as MKP-1. |
| 6 |
Enzyme Activity:
Raf-GTP-Ras*.1
Enzyme Molecule:
Raf-GTP-Ras* | 0.159091 | 0.105 | 4 | explicit E-S complex | MAPKK
| 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 |
| 7 |
Enzyme Activity:
Raf-GTP-Ras*.2
Enzyme Molecule:
Raf-GTP-Ras* | 0.159091 | 0.105 | 4 | explicit E-S complex | MAPKK-ser
| 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 |
| 8 |
Enzyme Activity:
RGR.1
Enzyme Molecule:
RGR | 0.159091 | 0.105 | 4 | explicit E-S complex | MAPKK
| 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 |
| 9 |
Enzyme Activity:
RGR.2
Enzyme Molecule:
RGR | 0.159091 | 0.105 | 4 | explicit E-S complex | MAPKK-ser
| 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 |
