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Molecule Parameter List for DAG

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

DAG 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	2	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2007_PKM	80	Network	Shared_Object_Ajay_Bhalla_2007_PKM,  PKC,  MAPK,   Ras,  CaM,  PKM
This is a non-bistable model of ERKII signaling that also incorporates PKM synthesis triggered by Ca influx. It is a simplified variant of the model of Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80.

DAG acting as a Molecule in  Ajay_Bhalla_2007_PKM Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
DAG	Ajay_Bhalla_ 2007_PKM Accession No. : 80	Shared_Object_ Ajay_Bhalla_ 2007_PKM Pathway No. : 369	12.1999	1.5	Yes

DAG acting as a Substrate in a reaction in  Ajay_Bhalla_2007_PKM 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	PKC-act-by-DAG	Ajay_Bhalla_ 2007_PKM Accession No. : 80	PKC Pathway No. : 370	0.008 (uM^-1 s^-1)	8.6348 (s^-1)	Kd(bf) = 1079.377(uM)	-	Substrate DAG PKC-Ca Product PKC-Ca-DAG
	Need est of rate. Assume it is fast Obtained from param search kf raised 10 X : see Shinomura et al PNAS 88 5149-5153 1991. kf changed from 3.865e-7 to 2.0e-7 in line with closer analysis of Shinomura data. 26 June 1996: Corrected DAG data: reduce kf 15x from 2e-7 to 1.333e-8
2	PKC-n-DAG	Ajay_Bhalla_ 2007_PKM Accession No. : 80	PKC Pathway No. : 370	0.0006 (uM^-1 s^-1)	0.1 (s^-1)	Kd(bf) = 166.6656(uM)	-	Substrate DAG PKC-cytosolic Product PKC-DAG
	kf raised 10 X based on Shinomura et al PNAS 88 5149-5153 1991 closer analysis of Shinomura et al: kf now 1e-8 (was 1.66e-8). Further tweak. To get sufficient AA synergy, increase kf to 1.5e-8 26 June 1996: Corrected DAG levels: reduce kf by 15x from 1.5e-8 to 1e-9