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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.