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Molecule Parameter List for R2C2-cAMP3

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-cAMP3 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000011

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
fig3_CaMKII2Network
Shared_Object_fig3_CaMKII CaMKII CaM 
PP1 PP2B PKA 
AC 
This is the model file for figure 3 from Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. It is a model of the Ca activation of CaMKII and other CaM-activated enzymes. It includes the regulatory phosphatases PP1 and PP2B (Calcineurin) acting on CaMKII and also includes CaM-activated adenylyl cyclase and PKA in the synapse.
Demonstration script files for generating the figures in the paper, including figure 3, are available here.

R2C2-cAMP3 acting as a Molecule in  
fig3_CaMKII Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
R2C2-cAMP3fig3_CaMKII
Accession No. : 2
PKA
Pathway No. : 17
01000No
R2C2 complex consisting of 2 catalytic (C) subunits, and the R-dimer with 3 cAMP molecules bound to it.

R2C2-cAMP3 acting as a Substrate in a reaction in  
fig3_CaMKII 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-A
    2
  • fig3_CaMKII
    Accession No. : 2
    PKA
    Pathway No. : 17
    75
    (uM^-1 s^-1)
    32.5
    (s^-1)
    Kd(bf) = 0.4333(uM)-Substrate
    R2C2-cAMP3
    cAMP

    Product
    R2C2-cAMP4
    Now cAMP shows effects of cooperativity and PKA has a low Kd for cAMP.

    R2C2-cAMP3 acting as a Product in a reaction in  
    fig3_CaMKII 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-A
    1
  • fig3_CaMKII
    Accession No. : 2
    PKA
    Pathway No. : 17
    75
    (uM^-1 s^-1)
    110
    (s^-1)
    Kd(bf) = 1.4667(uM)-Substrate
    R2C2-cAMP2
    cAMP

    Product
    R2C2-cAMP3
    Kf = 75 /sec/uM, Kb = 110 /sec; This site has higher Kd for cAMP (kinetics within bovine myocardium)
    Dagfinn Ogreid and Stein Ove Doskeland (1981) FEBS Lett. 129(2):287-292



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