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Molecule Parameter List for L.R.GDP.Gabc | 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 |
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.R.GDP.Gabc acting as a Molecule in PKA_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | L.R.GDP.Gabc | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 0 | 1000 | No | | This is the ternary complex, where all the action happens. There are actually a lot more steps here, including a final step where the GTP binds the L.R.Ga complex and causes the release of GTP.Ga from the L.R. For simplicity this is excluded. |
L.R.GDP.Gabc 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 | | Activate-Gs | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 0.025
(s^-1) | 0
(uM^-2 s^-1) | - | - | Substrate
L.R.GDP.Gabc
Product
GTP.Ga
Gbg
L.R
| | This step combines several stages in GTP.Galpha release. From Berstein et al activation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec. From Brandt and Ross JBC 261(4):1656-1664 (1986) and Ransan et al Biochem J 283(2):519-524 (1992) rates around 2.5/min to 1.5/min are better. |
L.R.GDP.Gabc acting as a Product 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.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. | | 2 | L.R-bind-Gabc | PKA_2003
Accession No. : 47 | Gs
Pathway No. : 198 | 10.0002
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.01(uM) | - | Substrate
GDP.Gabc
L.R
Product
L.R.GDP.Gabc
| | | See Fay et al Biochem 30 5066-5075 1991. kf is 0.01/sec but does not account for Gs levels. kb is 0.0001/sec. The fraction of RG is about 50%, so we can estimate Kd at about the same as for Gs basal levels. This rate has to be faster since it has to feed GTP.Ga into the system faster than the GTPase. Waldhoer et al Mol Pharmacol 53:808-818 1988 say affinity for A1adenosine/Gi is 10 nM. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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