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Molecule Parameter List for MAPK-tyr | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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-tyr 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 | 2 | 2 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
| 3d_fold_model | 8 | Network | Shared_Object_3d_fold_model, PKC, MAPK, PLA2, Ras |
| This model is an annotated version of the synaptic signaling network. The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated Bhalla US, Ram PT, Iyengar R. Science. 2002 Aug 9;297(5583):1018-23. | |||
MAPK-tyr acting as a Molecule in 3d_fold_model Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPK-tyr | 3d_fold_model Accession No. : 8 | MAPK Pathway No. : 56 | 0 | 1000 | No | |
| Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. | ||||||
MAPK-tyr acting as a Substrate for an Enzyme in 3d_fold_model Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKthr | 3d_fold_model Accession No. : 8 | MAPK Pathway No. : 56 | 0.0462963 | 0.15 | 4 | explicit E-S complex | Substrate MAPK-tyr Product MAPK* |
| Rate consts same as for MAPKKtyr. | ||||||||
| 2 | MKP-1 / MKP1-tyr-deph | 3d_fold_model Accession No. : 8 | 3d_fold_model Pathway No. : 54 | 0.0666667 | 1 | 4 | explicit E-S complex | 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 | ||||||||
MAPK-tyr acting as a Product of an Enzyme in 3d_fold_model Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKtyr | 3d_fold_model Accession No. : 8 | MAPK Pathway No. : 56 | 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 | MKP-1 / MKP1-thr-deph | 3d_fold_model Accession No. : 8 | 3d_fold_model Pathway No. : 54 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK* Product MAPK-tyr |
| See MKP1-tyr-deph | ||||||||