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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 |
2003 | 50 | Network | Shared_Object_MAPK_network_2003, PKC, PLA2, PLCbeta, Gq, MAPK, Ras, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC |
| This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 | |||
MAPK-tyr acting as a Molecule in MAPK_network_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPK-tyr | 2003 Accession No. : 50 | MAPK Pathway No. : 211 | 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 MAPK_network_2003 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKthr | 2003 Accession No. : 50 | MAPK Pathway No. : 211 | 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 | 2003 Accession No. : 50 | MAPK_network_ 2003 Pathway No. : 206 | 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 MAPK_network_2003 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKtyr | 2003 Accession No. : 50 | MAPK Pathway No. : 211 | 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 | 2003 Accession No. : 50 | MAPK_network_ 2003 Pathway No. : 206 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK* Product MAPK-tyr |
| See MKP1-tyr-deph | ||||||||