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Molecule Parameter List for Glu | 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 |
| Glu 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 | Osc_Ca_
IP3metabolism | 32 | 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 is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
Glu acting as a Molecule in Osc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | Glu | Osc_Ca_
IP3metabolism
Accession No. : 32 | Gq
Pathway No. : 163 | 0 | 1000 | Yes | | Varying the amount of (steady state) glu between .01 uM and up, the final amount of G*GTP complex does not change much. This means that the system should be reasonably robust wr to the amount of glu in the synaptic cleft. It would be nice to know how fast it is removed. Schoepp et al 1990 TIPS 11:508-515 give a range of Glu EC50 from rat brain in the range 120 to 1000 uM. Nicoletti 1986 PNAS 83:1931-1935 and Schoepp and Johnson 1989 J Neurochem 53:1865-1870 give an off time of at least 30 sec. |
Glu 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 | RecLigandBinding | Osc_Ca_
IP3metabolism
Accession No. : 32 | Gq
Pathway No. : 163 | 16.8
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.5952(uM) | - | Substrate
Glu
mGluR
Product
Rec-Glu
| | | From Martin et al FEBS Lett 316:2 191-196 1993 we have Kd = 600 nM Assuming kb = 10/sec, we get kf = 10/(0.6 uM * 6e5) = 2.8e-5 1/sec/# The off time for Glu seems pretty slow: Nicoletti et al 1986 PNAS 83:1931-1935 and Schoepp and Johnson 1989 J Neurochem 53 1865-1870 indicate it is at least 30 sec. Here we are a little faster because this is only a small part of the off rate, the rest coming from the Rec-Gq complex. | | 2 | Glu-bind-Rec-Gq | Osc_Ca_
IP3metabolism
Accession No. : 32 | Gq
Pathway No. : 163 | 16.8
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.006(uM) | - | Substrate
Glu
Rec-Gq
Product
Rec-Glu-Gq
| | | From Fay et al kb3 = kb = 1.06e-3 which is rather slow. k+1 = kf = 2.8e7 /M/sec= 4.67e-5/sec use 5e-5. However, the Kd from Martin et al may be more appropriate, as this is Glu not the system from Fay. kf = 2.8e-5, kb = 10 Let us compromise. since we have the Fay model, keep kf = k+1 = 2.8e-5. But kb (k-3) is .01 * k-1 from Fay. Scaling by .01, kb = .01 * 10 = 0.1 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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