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Molecule Parameter List for PLC_G* | 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 |
PLC_G* 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 | 1 | 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 |
PLC_G* acting as a Molecule in Synaptic_Network Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | PLC_G* | Synaptic_ Network Accession No. : 16 | PLC_g Pathway No. : 79 | 0 | 1000 | No | The phosphorylated form without calcium is not very active. I assume zero activity at zero calcium. As the halfmax for Ca binding is around 100 nM from Wahl et al JBC 267(15) 10447-10456 1992, it seems that basal calcium will account for respectable basal activity. |
PLC_G* 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 | Ca_act_PLC_g* | Synaptic_ Network Accession No. : 16 | PLC_g Pathway No. : 79 | 12 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 0.8333(uM) | - | Substrate Ca PLC_G*
Product Ca.PLC_g*
| Again, we refer to Homma et al and Wahl et al, for preference using Wahl et al JBC 267(15):10447-10456 1992. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. As we are phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 (Kf = 12) to match the reported half-max. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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