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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 | mkp1_feedback_ effects | 4 | Network | Shared_Object_mkp1_feedback_effects, Sos, PKC, MAPK, PLA2, Ras, PDGFR | This is a network involving the MAPK-PKC feedback loop with input from the PDGFR in the synapse. The distinctive feature of this model is that it includes MKP-1 induction by MAPK, and the consequent inhibitory regulation of MAPK and the feedback loop. Lots of interesting dynamics arise from this. This link provides supplementary material for the paper Bhalla US et al. Science (2002) 297(5583):1018-23. In the form of several example simulations and demos for the figures in the paper. |
MAPKK-ser acting as a Molecule in mkp1_feedback_effects Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | MAPKK-ser | mkp1_feedback_ effects Accession No. : 4 | MAPK Pathway No. : 35 | 0 | 1000 | No | Intermediately phophorylated, assumed inactive, form of MAPKK |
MAPKK-ser acting as a Substrate for an Enzyme in mkp1_feedback_effects Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | RGR / RGR.2 | mkp1_feedback_ effects Accession No. : 4 | MAPK Pathway No. : 35 | 0.159091 | 0.105 | 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 = 5.5e-6, k2 = .42, k3 = 0.105 | 2 | Raf*-GTP-Ras / Raf*-GTP-Ras.2 | mkp1_feedback_ effects Accession No. : 4 | MAPK Pathway No. : 35 | 0.159091 | 0.105 | 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. | 3 | PPhosphatase2A / MAPKK-deph-ser | mkp1_feedback_ effects Accession No. : 4 | Shared_Object_ mkp1_feedback_ effects Pathway No. : 32 | 15.6566 | 6 | 4.16667 | explicit E-S complex | Substrate MAPKK-ser
Product MAPKK
| | See parent PPhostphatase2A description for rate details |
MAPKK-ser acting as a Product of an Enzyme in mkp1_feedback_effects Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | RGR / RGR.1 | mkp1_feedback_ effects Accession No. : 4 | MAPK Pathway No. : 35 | 0.159091 | 0.105 | 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=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. | 2 | Raf*-GTP-Ras / Raf*-GTP-Ras.1 | mkp1_feedback_ effects Accession No. : 4 | MAPK Pathway No. : 35 | 0.159091 | 0.105 | 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. They report Km for MAPKK of 0.8 uM. and a Vmax of ~500 fm/min/ug. These parms cannot reach the observed 4X stimulation of MAPK. So we increase the affinity, ie, raise k1 5x to 5.5e-6 which is equivalent to 5-fold reduction in Km to about 0.16. This is, of course, dependent on the amount of MAPKK present. | 3 | PPhosphatase2A / MAPKK-deph | mkp1_feedback_ effects Accession No. : 4 | Shared_Object_ mkp1_feedback_ effects Pathway No. : 32 | 15.6566 | 6 | 4.16667 | explicit E-S complex | Substrate MAPKK*
Product MAPKK-ser
| | See: Kyriakis JM, App H, Zhang XF, Banerjee P, Brautigan DL, Rapp UR, Avruch J. (1992) Nature 358(6385):417-21. Ahn NG, Seger R, Krebs EG. (1992) Curr Opin Cell Biol. 4(6):992-999 for this pathway. Refer parent PPhosphatase2A for parameters. |
| 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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