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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
MAPKK-ser participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1003300

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2007_PKM
  • 80Network
    Shared_Object_Ajay_Bhalla_2007_PKM PKC MAPK 
    Ras CaM PKM 
    This is a non-bistable model of ERKII signaling that also incorporates PKM synthesis triggered by Ca influx. It is a simplified variant of the model of Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80.

    MAPKK-ser acting as a Molecule in  
    Ajay_Bhalla_2007_PKM Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPKK-ser
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • MAPK
    Pathway No. : 371
    01.5No
    Intermediately phophorylated, assumed inactive, form of MAPKK

    MAPKK-ser acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2007_PKM Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras  /
    Raf-GTP-Ras.2
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • MAPK
    Pathway No. : 371
    0.1590960.34explicit 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_
    2007_PKM

    Accession No. : 80
  • MAPK
    Pathway No. : 371
    0.1590960.34explicit 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
    3PPhosphatase2A  /
    MAPKK-deph-ser
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 15.656664explicit E-S complexSubstrate
    MAPKK-ser

    Product
    MAPKK
       

    MAPKK-ser acting as a Product of an Enzyme in  
    Ajay_Bhalla_2007_PKM Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras  /
    Raf-GTP-Ras.1
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • MAPK
    Pathway No. : 371
    0.1590960.34explicit E-S complexSubstrate
    MAPKK

    Product
    MAPKK-ser
        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.1
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • MAPK
    Pathway No. : 371
    0.1590960.34explicit 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. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6
    3PPhosphatase2A  /
    MAPKK-deph
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 15.656664explicit 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.



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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