|
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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | Ajay_Bhalla_
2007_Bistable | 79 | Network |
Shared_Object_Ajay_Bhalla_2007_Bistable, PKC, PLA2,
MAPK, Ras, CaM | This is a model of ERKII signaling which is bistable due to feedback. The feedback occurs through ERKII phosphorylation of phospholipase A2 (PLA2), leading to increased production of arachidonic acid (AA), which activates protein kinase C (PKC) which activates c-Raf which is upstream of ERKII.
The model is a highly simplified variant of more detailed bistable models of MAPK signaling (Bhalla US, Iyengar R. Science. 1999 Jan 15;283(5400):381-7, Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80) |
MAPK-tyr acting as a Molecule in Ajay_Bhalla_2007_Bistable Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPK-tyr | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0 | 125.7 | 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 Ajay_Bhalla_2007_Bistable Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | MAPKK* /
MAPKKthr | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.0462968 | 0.3 | 4 | explicit E-S complex | Substrate
MAPK-tyr
Product
MAPK*
| | | Rate consts same as for MAPKKtyr. | | 2 | MKP-1 /
MKP1-tyr-deph | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 0.133331 | 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 Ajay_Bhalla_2007_Bistable Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | MAPKK* /
MAPKKtyr | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.0462968 | 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 | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 0.133331 | 4 | 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. |
|
