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Molecule Parameter List for R2C2

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
R2C2 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
  • AMPAR_CaMKII_
    strong_coupling
  • 64Network
    Shared_Object_AMPAR_CaMKII_strong_coupling CaMKII CaM 
    PP1 AMPAR_memb PP2B 
    PKA AC PP1_PSD 
    AMPAR 
    This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on.

    R2C2 acting as a Molecule in  
    AMPAR_CaMKII_strong_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    R2C2
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PKA
    Pathway No. : 277
    0.50.09No
    This is the R2C2 complex, consisting of 2 catalytic (C) subunits, and the R-dimer. See Taylor et al Ann Rev Biochem 1990 59:971-1005 for a review. The Doskeland and Ogreid review is better for numbers. Amount of PKA is about .5 uM.

    R2C2 acting as a Substrate in a reaction in  
    AMPAR_CaMKII_strong_coupling 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
  • cAMP-bind-site-B
    1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PKA
    Pathway No. : 277
    54
    (uM^-1 s^-1)
    33
    (s^-1)
    Kd(bf) = 0.6111(uM)-Substrate
    R2C2
    cAMP

    Product
    R2C2-cAMP
    Hasler et al FASEB J 6:2734-2741 1992 say Kd =1e-7M for type II, 5.6e-8 M for type I. Take mean which comes to 2e-13 #/cell Smith et al PNAS USA 78:3 1591-1595 1981 have better data. First kf/kb=2.1e7/M = 3.5e-5 (#/cell). Ogreid and Doskeland Febs Lett 129:2 287-292 1981 have figs suggesting time course of complete assoc is < 1 min.



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