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Molecule Parameter List for Gs-alpha

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
Gs-alpha participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000030

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

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

    Accession No. : 16
  • Shared_Object_
    Synaptic_
    Network

    Pathway No. : 70
  • 01000No
    This is actualy GTP.Gs_alpha, the active form of Gs. Resting Gs-alpha is nearly zero.

    Gs-alpha 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
    1Gs-bind-AC2
  • Synaptic_
    Network

    Accession No. : 16
  • AC
    Pathway No. : 85
    499.998
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 0.002(uM)-Substrate
    AC2
    Gs-alpha

    Product
    AC2-Gs
      Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer Jacobowitz's thesis data indicates it is more like 2 nM. Jacobowitz, PhD Thesis, Mount Sinai School of Medicine.
    2Gs-bind-AC1
  • Synaptic_
    Network

    Accession No. : 16
  • AC
    Pathway No. : 85
    126
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 0.0079(uM)-Substrate
    AC1
    Gs-alpha

    Product
    AC1-Gs
      Half-max 8nM from Tang et al JBC266:13 8595-8603 kb/kf = 8 nM = 4800#/cell Also assume rapid binding of 1/sec.
    3Gs-bind-AC2*
  • Synaptic_
    Network

    Accession No. : 16
  • AC
    Pathway No. : 85
    833.28
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 0.0012(uM)-Substrate
    AC2*
    Gs-alpha

    Product
    AC2*-Gs
      Various references: Jacobowitz et al JBC 268(6):3829-3892 show that AC2 has a 2x rise in basal activation on phosphorylation, and a 2x rise in forskolin stimulated activation. Yoshimura and Cooper JBC 1993 268(7):4604-4607 say that type II is stimulated 9x over basal. Lustig et al 1993 JBC 268(19):13900-13905 syow a 2x activation by PDBu, and the Gs stimulated response is increased 2x-4x by PDBu. To match all these results with the binding of the unphosphorylated form we use a Kd of 1.2 nM here as compared with the Kd of 2 nM for the unphosphorylated reaction.



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