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Molecule Parameter List for R

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
R participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000020

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

R acting as a Molecule in  
cAMP_pathway Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
RcAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
0.08331000No
A typical number of receptors per cell is about 50000.

R 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
1L-bind-RcAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
0.1
(uM^-1 s^-1)
0.1
(s^-1)
Kd(bf) = 1(uM)-Substrate
L
R

Product
L.R
  Ligand binding to receptor. From Gether et al JBC 270:28268-28275 (1995) the binding to the purified receptor is at about 1 uM, but the conformational change only happens at 30 uM. We'll take 1 uM for this, since it is already much weaker binding than to the R.Gs complex. The time-course from this paper appears remarkably slow, based on physiological data I estimate more like 10 sec.
2R-bind-GabccAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
0.2
(uM^-1 s^-1)
0.1
(s^-1)
Kd(bf) = 0.5(uM)-Substrate
GDP.Gabc
R

Product
R.GDP.Gabc
  Receptor binding to Gs. Scale it to the same slow rates described by Fay et al for L.R to L.R.G. From detailed balance, Kd is 50.