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Molecule Parameter List for Rec-Glu-Gq

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

Rec-Glu-Gq 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	2

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.

Rec-Glu-Gq acting as a Molecule in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
Rec-Glu-Gq	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	Gq Pathway No. : 334	0	1.5	No

Rec-Glu-Gq 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
Activate-Gq	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	Gq Pathway No. : 334	0.01 (s^-1)	0 (uM^-2 s^-1)	-	-	Substrate Rec-Glu-Gq Product BetaGamma G*GTP Rec-Glu
This is the kcat==k3 stage of the Rec-Glu ezymatic activation of Gq. From Berstein et al actiation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec From Nakamura et al J physiol Lond 474:1 35-41 1994 see time courses. Also (Berstein) 15-40% of gprot is in GTP-bound form on stim.

Rec-Glu-Gq 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
1	Rec-Glu-bind-Gq	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	Gq Pathway No. : 334	0.006 (uM^-1 s^-1)	0.0001 (s^-1)	Kd(bf) = 0.0167(uM)	-	Substrate G-GDP Rec-Glu Product Rec-Glu-Gq
	This is the k1-k2 equivalent for enzyme complex formation in the binding of Rec-Glu to Gq. See Fay et al Biochem 30 5066-5075 1991. kf = 5e-5 which is nearly the same as calculated by Fay et al. (4.67e-5) kb = .04 June 1996: Closer reading of Fay et al suggests that kb <= 0.0001, so kf = 1e-8 by detailed balance. This reaction appears to be neglible.
2	Glu-bind-Rec-Gq	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	Gq Pathway No. : 334	16.8003 (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