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 |
Network | 16 | Network | Shared_Object_Synaptic_Network, PKC, PLA2, PLCbeta, Gq, MAPK, Ras, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC, CaRegulation |
| 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 Biophys J. 2002 Aug;83(2):740-52 Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62 | |||
MAPK-tyr acting as a Molecule in Synaptic_Network Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPK-tyr | Network Accession No. : 16 | MAPK Pathway No. : 75 | 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 Synaptic_Network Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKthr | Network Accession No. : 16 | MAPK Pathway No. : 75 | 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 | Network Accession No. : 16 | Synaptic_ Network Pathway No. : 70 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK-tyr Product MAPK |
| The original kinetics from Bhalla and Iyengar Science 1999 have now been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. The main constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. See Charles et al 1993 PNAS 90:5292-5296 and Charles et al Oncogene 7:187-190 Effective Km : 67 nM kcat = 1.43 umol/min/mg | ||||||||
MAPK-tyr acting as a Product of an Enzyme in Synaptic_Network Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKtyr | Network Accession No. : 16 | MAPK Pathway No. : 75 | 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, ratio of 4 to get k2=0.6. k1=0.75/46.6nM=2.7e-5 In terms of Michaelis-Menten rates, Km = 0.046, Vmax = 0.15, ratio = 4. | ||||||||
| 2 | MKP-1 / MKP1-thr-deph | Network Accession No. : 16 | Synaptic_ Network Pathway No. : 70 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK* Product MAPK-tyr |
| See MKP1-tyr-deph | ||||||||
color.