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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 as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | | No. of occurrences | 1 | 0 | 0 | 0 | 0 | 2 | 0 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | | PKA_2003 | 47 | Network |
Shared_Object_PKA_2003, PKA, AC,
Gs | | This model consists of receptor-ligand interaction, G-protein activation, Adenylyl cyclase mediated formation of cAMP and activation of PKA in the neuron. Demonstration programs using this model described in Bhalla US. (2004) Biophys J. 87(2):733-44 to generate a dose-response curve using stochastic calculations are available here. |
L acting as a Molecule in PKA_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | L | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 0 | 1000 | Yes | | 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 PKA_2003 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. |
| | Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | 1 | L-bind-R | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 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. | | 2 | L-bind-R.Gabc | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 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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