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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
cAMP_pathway25Network
Shared_Object_cAMP_pathway,  PKA,  AC,  
Gs 
This is a model of the canonical cAMP signaling pathway:
Ligand->Receptor->G-protein->Cyclase->cAMP->PKA.
It also includes phosphodiesterases to balance out cAMP formation.Bhalla US Methods Enzymol. 2002;345:3-23

R2C2 acting as a Molecule in  cAMP_pathway Network
NameAccession NamePathway NameInitial Conc.
(uM)		Volume
(fL)		Buffered
R2C2cAMP_pathway
Accession No. : 25		PKA
Pathway No. : 135		0.51000No
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  cAMP_pathway 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
    		• cAMP_pathway
    Accession No. : 25    		PKA
    Pathway No. : 135    		54
    (uM^-1 s^-1)    		33
    (s^-1)    		Kd(bf) = 0.6111(uM)-Substrate
    R2C2
    cAMP

    Product
    cAMP.R2C2
    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.


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