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Molecule Parameter List for Gs-alpha | 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 |
| Gs-alpha 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 | 3 | 0 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | Synaptic_
Network | 16 | Network |
Shared_Object_Synaptic_Network, PKC, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC, CaRegulation | This model is an annotated version of the synaptic signaling network.
The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated.
Bhalla US Biophys J. 2002 Aug;83(2):740-52
Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62 |
Gs-alpha acting as a Molecule in Synaptic_Network Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | Gs-alpha | Synaptic_
Network
Accession No. : 16 | Shared_Object_
Synaptic_
Network
Pathway No. : 70 | 0 | 1000 | No | | This is actualy GTP.Gs_alpha, the active form of Gs. Resting Gs-alpha is nearly zero. |
Gs-alpha acting as a Substrate in a reaction in Synaptic_Network 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 | Gs-bind-AC2 | Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 499.998
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.002(uM) | - | Substrate
AC2
Gs-alpha
Product
AC2-Gs
| | | Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer Jacobowitz's thesis data indicates it is more like 2 nM. Jacobowitz, PhD Thesis, Mount Sinai School of Medicine. | | 2 | Gs-bind-AC1 | Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 126
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0079(uM) | - | Substrate
AC1
Gs-alpha
Product
AC1-Gs
| | | Half-max 8nM from Tang et al JBC266:13 8595-8603 kb/kf = 8 nM = 4800#/cell Also assume rapid binding of 1/sec. | | 3 | Gs-bind-AC2* | Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 833.28
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0012(uM) | - | Substrate
AC2*
Gs-alpha
Product
AC2*-Gs
| | | Various references: Jacobowitz et al JBC 268(6):3829-3892 show that AC2 has a 2x rise in basal activation on phosphorylation, and a 2x rise in forskolin stimulated activation. Yoshimura and Cooper JBC 1993 268(7):4604-4607 say that type II is stimulated 9x over basal. Lustig et al 1993 JBC 268(19):13900-13905 syow a 2x activation by PDBu, and the Gs stimulated response is increased 2x-4x by PDBu. To match all these results with the binding of the unphosphorylated form we use a Kd of 1.2 nM here as compared with the Kd of 2 nM for the unphosphorylated reaction. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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