Enter a Search String |
| Special character and space not allowed in the query term. Search string should be at least 2 characters long. |
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 |
| mTOR_pathway | 92 | Network | Shared_Object_mTOR_pathway, AKT_mod, S6Kinase, PI3K_mod, TrKB_mod, mTOR_model, MAPK, PKC, 4E-BP_mod, Ras, Sos, 43S_complex, CaM |
| This model consists of various sub-modules. They are as follows: 1) BDNF receptor signaling 2) AKT signaling 3) 4E-BP model 4) S6 Kinase model 5) CaMKIII model 6) Protein synthesis model 7) CaM 8) PKC 9) MAPK model. | |||
MAPK-tyr acting as a Molecule in mTOR_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPK-tyr | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 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 mTOR_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK_star / MAPKKthr | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 0.0462963 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr Product MAPK_star |
| Rate consts same as for MAPKKtyr. | ||||||||
| 2 | MKP-1 / MKP1-tyr-deph | mTOR_pathway Accession No. : 92 | mTOR_pathway Pathway No. : 1097 | 7.00001 | 4 | 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 mTOR_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK_star / MAPKKtyr | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 0.0462963 | 0.3 | 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 | mTOR_pathway Accession No. : 92 | mTOR_pathway Pathway No. : 1097 | 7.00001 | 4 | 4 | explicit E-S complex | Substrate MAPK_star Product MAPK-tyr |
| See MKP1-tyr-deph | ||||||||