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Molecule Parameter List for PLC_G*

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
PLC_G* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000010

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Synaptic_
    Network
  • 16Network
    Shared_Object_Synaptic_Network PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC CaRegulation 
    This model is an annotated version of the synaptic signaling network.
    The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated.
    Bhalla US Biophys J. 2002 Aug;83(2):740-52
    Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62

    PLC_G* acting as a Molecule in  
    Synaptic_Network Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PLC_G*
  • Synaptic_
    Network

    Accession No. : 16
  • PLC_g
    Pathway No. : 79
    01000No
    The phosphorylated form without calcium is not very active. I assume zero activity at zero calcium. As the halfmax for Ca binding is around 100 nM from Wahl et al JBC 267(15) 10447-10456 1992, it seems that basal calcium will account for respectable basal activity.

    PLC_G* acting as a Substrate in a reaction in  
    Synaptic_Network 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
    Ca_act_PLC_g*
  • Synaptic_
    Network

    Accession No. : 16
  • PLC_g
    Pathway No. : 79
    12
    (uM^-1 s^-1)
    10
    (s^-1)
    Kd(bf) = 0.8333(uM)-Substrate
    Ca
    PLC_G*

    Product
    Ca.PLC_g*
    Again, we refer to Homma et al and Wahl et al, for preference using Wahl et al JBC 267(15):10447-10456 1992. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. As we are phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 (Kf = 12) to match the reported half-max.



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