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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 | MAPK_network_
2003 | 50 | Network |
Shared_Object_MAPK_network_2003, PKC, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC | | This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 |
PLC_G* acting as a Molecule in MAPK_network_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | PLC_G* | MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 0 | 1000 | No | | |
PLC_G* acting as a Substrate in a reaction in MAPK_network_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 | | Ca_act_PLC_g* | MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 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. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. Did some curve comparisons, and instead of 316 nM giving a kf of 5.27e-5, we will use 8e-5 for kf. 16 Sep 97. As we are now phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 to match the curves. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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