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Molecule Parameter List for PKC-DAG-AA*

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-AA* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1100001

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Osc_Ca_
    IP3metabolism
  • 32Network
    MIPP CaMKII CaM 
    PKC IP3-3K Gq 
    PLCbeta 134_dephos 145_dephos 
    IP4-system IHP-system 1345_dephos 
    CaRegulation Othmer-Tang-model 
    This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    PKC-DAG-AA* acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PKC-DAG-AA*
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • PKC
    Pathway No. : 161
    01000No
    Membrane translocated form of PKC-DAG-AA complex.

    PKC-DAG-AA* acting as a Summed Molecule in  
    Osc_Ca_IP3metabolism Network
    Accession NamePathway NameTargetInput
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • PKC
    Pathway No. : 161
    PKC-activePKC-DAG-AA*
    PKC-Ca-memb*
    PKC-Ca-AA*
    PKC-DAG-memb*
    PKC-basal*
    PKC-AA*
    This is the total active PKC. It is the sum of the respective activities of PKC-basal* PKC-Ca-memb* PKC-DAG-memb* PKC-Ca-AA* PKC-DAG-AA* PKC-AA* I treat PKC here in a two-state manner: Either it is in an active state (any one of the above list) or it is inactive. No matter what combination of stimuli activate the PKC, I treat it as having the same activity. The scaling comes in through the relative amounts of PKC which bind to the respecive stimuli. The justification for this is the mode of action of PKC, which like most Ser/Thr kinases has a kinase domain normally bound to and blocked by a regulatory domain. I assume that all the activators simply free up the kinase domain. A more general model would incorporate a different enzyme activity for each combination of activating inputs, as well as for each substrate. The current model seems to be a decent and much simpler approximation for the available data. One caveat of this way of representing PKC is that the summation procedure assumes that PKC does not saturate with its substrates. If this assumption fails, then the contributing PKC complexes would experience changes in availability which would affect their balance. Given the relatively low percentage of PKC usually activated, and its high throughput as an enzyme, this is a safe assumption under physiological conditions.

    PKC-DAG-AA* acting as a Product in a reaction in  
    Osc_Ca_IP3metabolism 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-act-by-DAG-A
    A
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • PKC
    Pathway No. : 161
    2
    (s^-1)
    0.2
    (s^-1)
    Keq = 0.1(uM)0.455secSubstrate
    PKC-DAG-AA

    Product
    PKC-DAG-AA*
    Membrane translocation step for PKC-DAG-AA complex. Rates from matching concentration-effect data in our two main references: Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and Shinomura et al 1988 PNAS 88: 5149-5153



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