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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
MAPKK participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1002100

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • MAPK-bistability
    -fig1c
    		• 35Network
    Shared_Object_MAPK-bistability-fig1c,  Sos,  PKC,  
    MAPK,  PLA2,  Ras,  
    PDGFR 
    Model for figure 1c in Bhalla US et al. Science (2002) 297(5583):1018-23.
    The demo for this figure is available here. This synaptic signaling model is without the MKP-1 feedback, so it is bistable and remains so over long periods.

    MAPKK acting as a Molecule in      MAPK-bistability-fig1c Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    MAPKK
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• MAPK
    Pathway No. : 182    		0.181000No
    Conc is from Seger et al JBC 267:20 pp14373 (1992) mwt is 45/46 Kd We assume that phosphorylation on both ser and thr is needed for activiation. See Kyriakis et al Nature 358 417 1992 Init conc of total is 0.18

    MAPKK acting as a Substrate for an Enzyme in      MAPK-bistability-fig1c Network
     Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1RGR  /
    RGR.1
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• MAPK
    Pathway No. : 182    		0.1590910.1054explicit E-S complexSubstrate
    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.
    2Raf*-GTP-Ras  /
    Raf*-GTP-Ras.1
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• MAPK
    Pathway No. : 182    		0.1590910.1054explicit E-S complexSubstrate
    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.

    MAPKK acting as a Product of an Enzyme in      MAPK-bistability-fig1c Network
    Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PPhosphatase2A  /
    MAPKK-deph-ser
  • MAPK-bistability
    -fig1c
    Accession No. : 35
  • Shared_Object_
    MAPK-bistability
    -fig1c
    Pathway No. : 179
    		• 15.656664.16667explicit E-S complexSubstrate
    MAPKK-ser

    Product
    MAPKK
    See parent PPhostphatase2A description for rate details


    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.