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Molecule Parameter List for L

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
L 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

L acting as a Molecule in  
cAMP_pathway Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
LcAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
01000Yes
This ligand could be any of several which bind to the beta adrenergic receptor and other G-protein coupled receptors which activate AC. For the sake of argument, call it isoproterenol.

L 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.
2L-bind-R.GabccAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
5
(uM^-1 s^-1)
0.1
(s^-1)
Kd(bf) = 0.02(uM)-Substrate
L
R.GDP.Gabc

Product
L.R.GDP.Gabc
  From Seifert et al Mol. Pharmacol 56:348-358 (1999) The EC50 for ISO is about 20 nM.



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