| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
act_
transcription
Enzyme Molecule:
nuc_MAPK* | 3.99997 | 0.004 | 4 | explicit E-S complex | nucleotides
| MKP3_synthesis
|
| | |
| 2 |
Enzyme Activity:
kenz
Enzyme Molecule:
MKP3_synthesis | 0.199998 | 0.01 | 4 | explicit E-S complex | MKP3_AA
| MKP-3
|
| | |
| 3 |
Enzyme Activity:
MKP3-thr-deph
Enzyme Molecule:
MKP-3 | 10.0001 | 4 | 4 | explicit E-S complex | MAPK*
| MAPK-tyr
|
| | See MKP1-tyr-deph Km is twice as high to avoid saturation. |
| 4 |
Enzyme Activity:
MKP3-tyr-deph
Enzyme Molecule:
MKP-3 | 10.0001 | 4 | 4 | explicit E-S complex | MAPK-tyr
| MAPK
|
| | The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg Km for MKP3 is set to 267 nM, twice as high as MKP1 version, to lessen substrate saturation. |
