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Molecule Parameter List for GAP*

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
GAP* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000110

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.

    GAP* acting as a Molecule in      MAPK-bistability-fig1c Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    GAP*
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• Ras
    Pathway No. : 184    		01000No
    Phosphorylated and inactive GAP. See Boguski and McCormick 1993 Nature 366:643-654 for a review.

    GAP* 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
    PKC-active  /
    PKC-inact-GAP
  • MAPK-bistability
    -fig1c
    Accession No. : 35
  • Shared_Object_
    MAPK-bistability
    -fig1c
    Pathway No. : 179
    		• 66.6667254explicit E-S complexSubstrate
    GAP

    Product
    GAP*
    Rate consts are PKC generic rates. This reaction inactivates GAP. The reaction is from the Boguski and McCormick 1993 review in Nature 366:643-654 The phosphorylation Vmax is 6x higher to account for balance of GDP-Ras:GDP-Ras.

    GAP* acting as a Substrate in a reaction in      MAPK-bistability-fig1c Network
    Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reaction are not consider.
    NameAccession NamePathway NameKfKbKdtauReagents
    dephosph-GAP
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• Ras
    Pathway No. : 184    		0.1
    (s^-1)    		0
    (s^-1)    		--Substrate
    GAP*

    Product
    GAP
    Assume a reasonably good rate for dephosphorylating it, 0.1/sec. This fits well with resting levels of active kinase and the degree of activation as well as time-course of turnoff of Ras activation, but data is quite indirect.


    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.