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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
  • MAPK_MKP1_
    oscillation
  • 9Network
    Shared_Object_MAPK_MKP1_oscillation PKC MAPK 
    PLA2 Ras 
    This model relates to figure 5 in Bhalla US, Iyengar R. Chaos (2001) 11(1):221-226. It includes the model used for figures 2-4 and also has MKP-1 induction by MAPK activity in the synapse. PP2A is set to 0.16 uM and MKP synthesis is varied from 5x to 40 x basal to get a range of interesting behaviours.

    MAPKK-ser acting as a Molecule in  
    MAPK_MKP1_oscillation Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPKK-ser
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    01000No
    Intermediately phophorylated, assumed inactive, form of MAPKK

    MAPKK-ser acting as a Substrate for an Enzyme in  
    MAPK_MKP1_oscillation Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras*  /
    Raf-GTP-Ras*.2
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    0.1590910.1054explicit 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
    2RGR  /
    RGR.2
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    0.1590910.1054explicit 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
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 15.656664.16667explicit E-S complexSubstrate
    MAPKK-ser

    Product
    MAPKK

    MAPKK-ser acting as a Product of an Enzyme in  
    MAPK_MKP1_oscillation Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras*  /
    Raf-GTP-Ras*.1
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    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. 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
    2RGR  /
    RGR.1
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    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. 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
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 15.656664.16667explicit 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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