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Molecule Parameter List for G*GTP | 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 | Osc_Ca_
IP3metabolism | 24 | Network |
MIPP, CaMKII, CaM,
PKC, IP3-3K, Gq,
PLCbeta, 134_dephos, 145_dephos,
IP4-system, IHP-system, 1345_dephos,
CaRegulation, Othmer-Tang-model | | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It differs from the NonOsc_Ca_IP3metabolism network in the CaRegulation module and in InsP3 receptor kinetics. Details of InsP3 receptor kinetics have been adapted from the Othmer-Tang model for oscillatory Ca dynamics. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
G*GTP acting as a Molecule in Osc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | G*GTP | Osc_Ca_
IP3metabolism
Accession No. : 24 | Gq
Pathway No. : 125 | 0 | 1000 | No | | Activated G protein. Berstein et al indicate that about 20-40% of the total Gq alpha should bind GTP at steady stimulus. |
G*GTP acting as a Substrate in a reaction in Osc_Ca_IP3metabolism 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 | Inact-G | Osc_Ca_
IP3metabolism
Accession No. : 24 | Gq
Pathway No. : 125 | 0.0133
(s^-1) | 0
(s^-1) | - | - | Substrate
G*GTP
Product
G*GDP
| | | From Berstein et al JBC 267:12 8081-8088 1992, kcat for GTPase activity of Gq is only 0.8/min. | | 2 | PLC-bind-Gq | Osc_Ca_
IP3metabolism
Accession No. : 24 | PLCbeta
Pathway No. : 126 | 2.52
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.3968(uM) | - | Substrate
G*GTP
PLC
Product
PLC-Gq
| | | this binding does not produce active PLC. This step was needed to implement the described (Smrcka et al) increase in affinity for Ca by PLC once Gq was bound. The tempkin are the same as the binding step for Ca-PLC to Gq. Kd is constrained by detailed balance. | | 3 | Act-PLC-by-Gq | Osc_Ca_
IP3metabolism
Accession No. : 24 | PLCbeta
Pathway No. : 126 | 25.2
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0397(uM) | - | Substrate
G*GTP
PLC-Ca
Product
PLC-Ca-Gq
| | | Affinity for Gq is > 20 nM (Smrcka et al Science251 804-807 1991) so [Gq].kf = kb so 40nM * 6e5 = kb/kf = 24e3 so kf = 4.2e-5, kb =1 |
G*GTP acting as a Product in a reaction in Osc_Ca_IP3metabolism 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 | Basal-Act-G | Osc_Ca_
IP3metabolism
Accession No. : 24 | Gq
Pathway No. : 125 | 0.0001
(s^-1) | 0
(uM^-1 s^-1) | - | - | Substrate
G-GDP
Product
BetaGamma
G*GTP
| | | This is the basal exchange of GTP for GDP. So slow as to be nearly negligible. | | 2 | Activate-Gq | Osc_Ca_
IP3metabolism
Accession No. : 24 | Gq
Pathway No. : 125 | 0.01
(s^-1) | 0
(uM^-2 s^-1) | - | - | Substrate
Rec-Glu-Gq
Product
BetaGamma
G*GTP
Rec-Glu
| | | This reaction is the critical one for activation of Gq. It probably encapsulates multiple steps. In this approximation the receptor-ligand- Gprotein complex splits up into GTP.Galpha, rec.ligand complex, and Gbetagamma. There is a hidden step of exchange of GDP for GTP. The reaction does not take these into account since it is assumed that both GTP and GDP levels are tightly regulated by metabolic control. This is the kcat==k3 stage of the Rec-Glu ezymatic activation of Gq. From Berstein et al actiation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec From Nakamura et al J physiol Lond 474:1 35-41 1994 see time courses. Also (Berstein) 15-40% of gprot is in GTP-bound form on stim. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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