|
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 MAPKK-ser | 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) |
MAPKK-ser acting as a Molecule in Ajay_Bhalla_2007_Bistable Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPKK-ser | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0 | 125.7 | No | | Intermediately phophorylated, assumed inactive, form of MAPKK |
MAPKK-ser 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 | Raf-GTP-Ras /
Raf-GTP-Ras.2 | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.159096 | 0.3 | 4 | explicit E-S complex | Substrate
MAPKK-ser
Product
MAPKK*
| | | Kinetics are the same as for the craf_1* activity, ie., k1=5.5e-6, k2=0.42, k3 = 0.105 These are basedo n Force et al PNAS USA 91 1270-1274, 1994., but k1 is scaled up 5x (ie., Km is scaled down 5x to the value used here and for craf_1* activity: Km = 0.1591). | | 2 | Raf*-GTP-Ras /
Raf*-GTP-Ras.2 | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.159096 | 0.3 | 4 | explicit E-S complex | Substrate
MAPKK-ser
Product
MAPKK*
| | | Same kinetics as other c-raf activated forms. See Force et al PNAS 91 1270-1274 1994. k1 = 1.1e-6, k2 = .42, k3 = 1.05 raise k1 to 5.5e-6 | | 3 | PPhosphatase2A /
MAPKK-deph-ser | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 15.6566 | 6 | 4 | explicit E-S complex | Substrate
MAPKK-ser
Product
MAPKK
| | | |
MAPKK-ser 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 | Raf-GTP-Ras /
Raf-GTP-Ras.1 | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.159096 | 0.3 | 4 | explicit E-S complex | Substrate
MAPKK
Product
MAPKK-ser
| | | Kinetics are the same as for the craf_1* activity, ie., k1=5.5e-6, k2=0.42, k3 = 0.105 These are basedo n Force et al PNAS USA 91 1270-1274, 1994., but k1 is scaled up 5x (ie., Km is scaled down 5x to the value used here and for craf_1* activity: Km = 0.1591). | | 2 | Raf*-GTP-Ras /
Raf*-GTP-Ras.1 | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0.159096 | 0.3 | 4 | explicit E-S complex | Substrate
MAPKK
Product
MAPKK-ser
| | | Kinetics are the same as for the craf-1* activity, ie., k1=1.1e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6 | | 3 | PPhosphatase2A /
MAPKK-deph | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 15.6566 | 6 | 4 | explicit E-S complex | Substrate
MAPKK*
Product
MAPKK-ser
| | | See: Kyriakis et al Nature 358 pp 417-421 1992 Ahn et al Curr Op Cell Biol 4:992-999 1992 for this pathway. See parent PPhosphatase2A for parms. |
| 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. |
|
