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Molecule Parameter List for Ca.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

Ca.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	1	0	1	1	1

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning	77	Network	Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning,  PKC,  PLA2,   PLCbeta,  Ras,  Gq,   MAPK,  EGFR,  Sos,   PLC_g,  CaMKII,  CaM,   PP1,  PP2B,  PKA,   AC,  MKP3,  PKM
This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a.

Ca.PLC_g* acting as a Molecule in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
Ca.PLC_g*	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	PLC_g Pathway No. : 338	0	1.5	No

Ca.PLC_g* acting as an Enzyme in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
Ca.PLC_g* / PIP2_hydrolysis	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	PLC_g Pathway No. : 338	19.7917	57	4	explicit E-S complex	Substrate PIP2 Product DAG IP3
Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that this has 7X higher affinity for substrate than control.

Ca.PLC_g* acting as a Product of an Enzyme in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
L.EGFR  / phosph_PLC_g	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	EGFR Pathway No. : 336	0.333337	0.2	4	explicit E-S complex	Substrate Ca.PLC_g Product Ca.PLC_g*
Hsu et al JBC 266:1 603-608 1991 Km = 385 +- 100 uM, Vm = 5.1 +-1 pmol/min/ug for PLC-771. Other sites have similar range, but are not stim as much by EGF. k1 = 2.8e-2/385/6e5 = 1.2e-10. Phenomenally slow. But Sherrill and Kyte say turnover # for angiotensin II is 5/min for cell extt, and 2/min for placental. Also see Okada et al for Shc rates which are much faster.

Ca.PLC_g* acting as a Substrate in a reaction in  Ajay_Bhalla_2004_PKM_MKP3_Tuning 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
dephosph_PLC_g	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	PLC_g Pathway No. : 338	0.05 (s^-1)	0 (s^-1)	-	-	Substrate Ca.PLC_g* Product Ca.PLC_g

Ca.PLC_g* acting as a Product in a reaction in  Ajay_Bhalla_2004_PKM_MKP3_Tuning 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*	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	PLC_g Pathway No. : 338	11.9997 (uM^-1 s^-1)	10 (s^-1)	Kd(bf) = 0.8334(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.