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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 occurrences1021200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_Tuning
  • 76Network
    PKC Shared_Object_Ajay_Bhalla_2004_PKM_tuning PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC PKM 
    This model is taken from the Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the reference feedforward model from Figure 8a.

    MAPKK* acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPKK*
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • MAPK
    Pathway No. : 317
    01.5No
    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_2004_PKM_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK* /
    MAPKKtyr
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • MAPK
    Pathway No. : 317
    0.04629630.34explicit E-S complexSubstrate
    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
    2MAPKK* /
    MAPKKthr
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • MAPK
    Pathway No. : 317
    0.04629630.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.

    MAPKK* acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PPhosphatase2A  /
    MAPKK-deph
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_tuning

    Pathway No. : 312
  • 15.656864explicit E-S complexSubstrate
    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.

    MAPKK* acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras  /
    Raf-GTP-Ras.2
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • MAPK
    Pathway No. : 317
    0.1590940.34explicit E-S complexSubstrate
    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).
    2Raf*-GTP-Ras  /
    Raf*-GTP-Ras.2
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • MAPK
    Pathway No. : 317
    0.1590940.34explicit E-S complexSubstrate
    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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