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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
  • Ajay_Bhalla_
    2007_Bistable
  • 79Network
    Shared_Object_Ajay_Bhalla_2007_Bistable PKC PLA2 
    MAPK Ras CaM 
    This is a model of ERKII signaling which is bistable due to feedback. The feedback occurs through ERKII phosphorylation of phospholipase A2 (PLA2), leading to increased production of arachidonic acid (AA), which activates protein kinase C (PKC) which activates c-Raf which is upstream of ERKII.
    The model is a highly simplified variant of more detailed bistable models of MAPK signaling (Bhalla US, Iyengar R. Science. 1999 Jan 15;283(5400):381-7, Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80)

    MAPKK acting as a Molecule in  
    Ajay_Bhalla_2007_Bistable Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPKK
  • Ajay_Bhalla_
    2007_Bistable

    Accession No. : 79
  • MAPK
    Pathway No. : 366
    0.5125.7No
    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 Ortiz et al 1995 J Neurosci 15(2):1285-1297 suggest that levels are higher in hippocampus than other brain regions, and further elevated in synapses. Estimate 3x higher levels than before, at 0.5 uM. Similar results from Schipper et al 1999 Neuroscience 93(2):585-595 but again lacking in quantitation.

    MAPKK acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2007_Bistable Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1Raf-GTP-Ras  /
    Raf-GTP-Ras.1
  • Ajay_Bhalla_
    2007_Bistable

    Accession No. : 79
  • MAPK
    Pathway No. : 366
    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_Bistable

    Accession No. : 79
  • MAPK
    Pathway No. : 366
    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

    MAPKK acting as a Product of an Enzyme in  
    Ajay_Bhalla_2007_Bistable Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PPhosphatase2A  /
    MAPKK-deph-ser
  • Ajay_Bhalla_
    2007_Bistable

    Accession No. : 79
  • Shared_Object_
    Ajay_Bhalla_
    2007_Bistable

    Pathway No. : 363
  • 15.656664explicit E-S complexSubstrate
    MAPKK-ser

    Product
    MAPKK



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