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Molecule Parameter List for MAPKK* | 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* acting as a Molecule in Ajay_Bhalla_2007_Bistable Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPKK* | Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | MAPK
Pathway No. : 366 | 0 | 125.7 | No | | MAPKK phosphorylates MAPK on both the tyr and thr residues, first tyr then thr. Refs: Seger et al JBC267:20 pp 14373 1992 The MAPKK itself is phosphorylated on ser as well as thr residues. Let us assume that the ser goes first, and that the sequential phosphorylation is needed. See Kyriakis et al Nature 358 417-421 1992 |
MAPKK* acting as 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 | 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. |
MAPKK* acting as a Substrate for an Enzyme in Ajay_Bhalla_2007_Bistable Network
MAPKK* 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.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 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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