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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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | MAPK_network_
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 | MAPK_network_
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 | MAPK_network_
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 | MAPK_network_
2003
Accession No. : 50 | Shared_Object_
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 | MAPK_network_
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 | MAPK_network_
2003
Accession No. : 50 | Shared_Object_
MAPK_network_
2003
Pathway No. : 206 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate
MAPK*
Product
MAPK-tyr
| | | See MKP1-tyr-deph |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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