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Molecule Parameter List for MAPK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by  color. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Statistics | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MAPK participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction |
| No. of occurrences | 1 | 0 | 0 | 1 | 2 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
oscillation | 9 | Network | Shared_Object_MAPK_MKP1_oscillation, PKC, MAPK, PLA2, Ras |
| This model relates to figure 5 in Bhalla US, Iyengar R. Chaos (2001) 11(1):221-226. It includes the model used for figures 2-4 and also has MKP-1 induction by MAPK activity in the synapse. PP2A is set to 0.16 uM and MKP synthesis is varied from 5x to 40 x basal to get a range of interesting behaviours. | |||
MAPK acting as a Molecule in MAPK_MKP1_oscillation Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPK | oscillation Accession No. : 9 | MAPK Pathway No. : 61 | 0.36 | 1000 | No | |
| conc is from Sanghera et al JBC 265 pp 52 (1990) A second calculation gives 3.1 uM, from same paper. They est MAPK is 1e-4x total protein, and protein is 15% of cell wt, so MAPK is 1.5e-5g/ml = 0.36uM. which is closer to our first estimate. Lets use this. | ||||||
MAPK acting as a Substrate for an Enzyme in MAPK_MKP1_oscillation Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| MAPKK* / MAPKKtyr | oscillation Accession No. : 9 | MAPK Pathway No. : 61 | 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 | |||||||
MAPK acting as a Product of an Enzyme in MAPK_MKP1_oscillation Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MKP-1** / MKP1*-tyr-deph | oscillation Accession No. : 9 | MAPK Pathway No. : 61 | 0.0666667 | 1 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MAPK-tyr Product MAPK |
| 3 Feb 2000. Same rates as MKP-1. | ||||||||
| 2 | MKP-1 / MKP1-tyr-deph | oscillation Accession No. : 9 | MAPK_MKP1_ oscillation Pathway No. : 59 | 0.0666667 | 1 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MAPK-tyr Product 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 | ||||||||