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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 | 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* acting as a Molecule in mkp1_feedback_effects Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPKK* | mkp1_feedback_
effects
Accession No. : 4 | MAPK
Pathway No. : 35 | 0 | 1000 | 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 mkp1_feedback_effects Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | MAPKK* /
MAPKKtyr
| mkp1_feedback_
effects
Accession No. : 4 | MAPK
Pathway No. : 35 | 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, ratio of 4 to get k2=0.6. k1=0.75/46.6nM=2.7e-5 In terms of Michaelis-Menten rates, Km = 0.046, Vmax = 0.15, ratio = 4. | | 2 | MAPKK* /
MAPKKthr
| mkp1_feedback_
effects
Accession No. : 4 | MAPK
Pathway No. : 35 | 0.0462963 | 0.15 | 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 mkp1_feedback_effects Network
MAPKK* 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.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. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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