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Molecule Parameter List for PKC-active

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-active participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1110000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • NonOsc_Ca_
    IP3metabolism
  • 23Network
    MIPP CaMKII CaM 
    PKC IP3-3K CaRegulation 
    Gq PLCbeta 134_dephos 
    145_dephos IP4-system IHP-system 
    1345_dephos 
    This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. The calcium response is non-oscillatory. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    PKC-active acting as a Molecule in  
    NonOsc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PKC-active
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • PKC
    Pathway No. : 108
    01000No
    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-active acting as a Summed Molecule in  
    NonOsc_Ca_IP3metabolism Network
    Accession NamePathway NameTargetInput
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • PKC
    Pathway No. : 108
    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-active acting as an Enzyme in  
    NonOsc_Ca_IP3metabolism Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKC-active /
    PKC-phos
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • PKC
    Pathway No. : 108
    30.000844explicit E-S complexSubstrate
    IP3_3K

    Product
    IP3_3K*1
    rates referred from standard PKC phosphorylation rates



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