| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| 1 | PKC-active /
PKC-act-raf
| EGFR_MAPK
Accession No. : 58 | Shared_Object_
EGFR_MAPK
Pathway No. : 229 | 66.6667 | 4 | 4 | explicit E-S complex | Substrate
craf-1
Product
craf-1*
|
| | Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC |
| 2 | PKC-active /
PKC-inact-GAP
| EGFR_MAPK
Accession No. : 58 | Shared_Object_
EGFR_MAPK
Pathway No. : 229 | 3.33333 | 4 | 4 | explicit E-S complex | Substrate
GAP
Product
GAP*
|
| | Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review. |
| 3 | PKC-active /
PKC-act-GEF
| EGFR_MAPK
Accession No. : 58 | Shared_Object_
EGFR_MAPK
Pathway No. : 229 | 3.33333 | 4 | 4 | explicit E-S complex | Substrate
inact-GEF
Product
GEF*
|
| | Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X |
color.