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Molecule Parameter List for PKC-DAG

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
PKC-DAG participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000011

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.

    PKC-DAG acting as a Molecule in      MAPK-bistability-fig1c Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    PKC-DAG
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• PKC
    Pathway No. : 181    		01000No
    This is a DAG-bound intermediate used in synergistic activation of PKC by DAG and AA.

    PKC-DAG 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
    PKC-n-DAG-AA
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• PKC
    Pathway No. : 181    		0.018
    (uM^-1 s^-1)    		2
    (s^-1)    		Kd(bf) = 111.1111(uM)-Substrate
    AA
    PKC-DAG

    Product
    PKC-DAG-AA
    This is one of the more interesting steps. Mechanistically it does not seem necessary at first glance. Turns out that one needs this step to quantitatively match the curves in Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and Shinomura et al 1991 PNAS 88:5149-5153. There is a synergy between DAG and AA activation even at low Ca levels, which is most simply represented by this reaction. Tau is assumed to be fast. Kd comes from matching the experimental curves.

    PKC-DAG acting as a Product 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
    PKC-n-DAG
  • MAPK-bistability
    -fig1c
    Accession No. : 35
    		• PKC
    Pathway No. : 181    		0.0006
    (uM^-1 s^-1)    		0.1
    (s^-1)    		Kd(bf) = 166.6667(uM)-Substrate
    DAG
    PKC-cytosolic

    Product
    PKC-DAG
    Binding of PKC to DAG, non-Ca dependent. Kf based on Shinomura et al PNAS 88 5149-5153 1991 Tau estimated as fast and here it is about the same time-course as the formation of DAG so it will not be rate-limiting.


    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.