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Molecule Parameter List for AC2-Gs

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
AC2-Gs participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1010001

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

    AC2-Gs acting as a Molecule in  
    Synaptic_Network Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    AC2-Gs
  • Synaptic_
    Network

    Accession No. : 16
  • AC
    Pathway No. : 85
    01000No
    This is the generic Gs-Stimulated form of AC2

    AC2-Gs acting as an Enzyme in  
    Synaptic_Network Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    AC2-Gs /
    kenz
  • Synaptic_
    Network

    Accession No. : 16
  • AC
    Pathway No. : 85
    20184Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    ATP

    Product
    cAMP
    Vmax is assumed to be the same as for AC1. This is consistent since there is a good match between the mixture of ACs tested by Smigel 1986 JBC 261(4):1976-1982 who has 8.27 umol/min/mg with forskolin stimulated AC. Tang et al JBC 266(13):8595-8603 have an almost identical Vmax of 8 umol/min/mg for AC1. This comes to a Vmax of 18/sec. The Km is pretty immaterial since the vast excess of ATP means that the enzyme will normally be saturated. This is a pretty fast enzyme. Note that the saturation of the enzyme means that the regulatory reactions have to involve the complex rather than the free enzyme.

    AC2-Gs acting as a Product 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
    Gs-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.



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