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Molecule Parameter List for craf-1*

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

craf-1* participated as	Molecule	Sum total of	Enzyme	Substrate of an enzyme	Product of an enzyme	Substrate in Reaction	Product in Reaction
No. of occurrences	40	0	0	80	80	79	39

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2007_ReacDiff2	83	Network	Shared_Object_Ajay_Bhalla_2007_ReacDiff, PKC, MAPK, Ras, CaM, PKM, chain, kinetics, PKC, MAPK, Ras, CaM, PKM, kinetics[1], PKC, MAPK, Ras, kinetics[3], CaM, PKM, kinetics[2], PKC, MAPK, Ras, CaM, PKM, PKC, MAPK, Ras, CaM, PKM, kinetics[4], PKC, MAPK, Ras, CaM, PKM, kinetics[5], PKC, MAPK, Ras, CaM, PKM, kinetics[6], PKC, MAPK, Ras, CaM, PKM, kinetics[7], PKC, MAPK, Ras, CaM, PKM, kinetics[8], PKC, MAPK, Ras, CaM, PKM, kinetics[9], PKC, MAPK, Ras, CaM, PKM, kinetics[10], PKC, MAPK, Ras, CaM, PKM, kinetics[11], PKC, MAPK, Ras, CaM, PKM, kinetics[12], PKC, MAPK, Ras, CaM, PKM, kinetics[13], PKC, MAPK, Ras, CaM, PKM, kinetics[14], PKC, MAPK, Ras, CaM, PKM, kinetics[15], PKC, MAPK, Ras, CaM, PKM, kinetics[16], PKC, MAPK, Ras, CaM, PKM, kinetics[17], PKC, MAPK, Ras, CaM, PKM, kinetics[18], PKC, MAPK, Ras, CaM, PKM, kinetics[19], PKC, MAPK, Ras, CaM, PKM, kinetics[20], PKC, MAPK, Ras, CaM, PKM, kinetics[21], PKC, MAPK, Ras, CaM, PKM, kinetics[22], PKC, MAPK, Ras, CaM, PKM, kinetics[23], PKC, MAPK, Ras, CaM, PKM, kinetics[24], PKC, MAPK, Ras, CaM, PKM, kinetics[25], PKC, MAPK, Ras, CaM, PKM, kinetics[26], PKC, MAPK, Ras, CaM, PKM, kinetics[27], PKC, MAPK, Ras, CaM, PKM, kinetics[28], PKC, MAPK, Ras, CaM, PKM, kinetics[29], PKC, MAPK, Ras, CaM, PKM, kinetics[30], PKC, MAPK, Ras, CaM, PKM, kinetics[31], PKC, MAPK, Ras, CaM, PKM, kinetics[32], PKC, MAPK, Ras, CaM, PKM, kinetics[33], PKC, MAPK, Ras, CaM, PKM, kinetics[34], PKC, MAPK, Ras, CaM, PKM, kinetics[35], PKC, MAPK, Ras, CaM, PKM, kinetics[36], PKC, MAPK, Ras, CaM, PKM, kinetics[37], PKC, MAPK, Ras, CaM, PKM, kinetics[38], PKC, MAPK, Ras, CaM, PKM
This is a 40-compartment reaction-diffusion-transport version of the Ajay_Bhalla_2007_PKM model. The original single-compartment model is repeated 40 times. In addition, a subset (27 out of 42) molecules can diffuse between compartments. Diffusion is implemented as a reaction between corresponding molecules in neighboring compartments. For D = 1e-12 m^2/sec (i.e., 1 micron^2/sec ) the kf and kb of this reaction for these 10 micron compartments are both 0.01/sec In addition, we have a forward (dendrite to soma) transport term of 1 microns/sec. This converts to a rate of 0.1/sec, but applies only to the kf. So the total kf of the diffusion 'reaction' is 0.11 for D = 1 micron^2/sec, and kb is 0.01. If D=0.1 micron^2/sec then kf = 0.101 and kb = 0.001. In addition this model has all molecules buffered in the first and last compartments. This boundary conditions says that the molecules are not drained out of the first compartment, nor do they all pile up in the last one. The stimulus file pkm_mapk22_transp_endbuf_D1e-13_Fig4CD which was used for the model to replicate Figure 4C and 4D from the paper.

craf-1* acting as a Molecule in Ajay_Bhalla_2007_ReacDiff2 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 686	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 692	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 699	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 704	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 710	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 716	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 722	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 728	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 734	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 740	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 746	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 752	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 758	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 764	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 770	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 776	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 782	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 788	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 794	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 800	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 806	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 812	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 818	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 824	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 830	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 836	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 842	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 848	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 854	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 860	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 866	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 872	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 878	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 884	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 890	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 896	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 902	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 908	0.012	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 679	0.012	1.5	Yes
craf-1*	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	MAPK Pathway No. : 914	0.012	1.5	Yes

craf-1* acting as a Substrate for an Enzyme in Ajay_Bhalla_2007_ReacDiff2 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
2	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
3	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics Pathway No. : 684	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
4	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics Pathway No. : 684	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
5	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[1] Pathway No. : 690	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
6	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[1] Pathway No. : 690	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
7	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[2] Pathway No. : 697	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
8	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[2] Pathway No. : 697	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
9	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[3] Pathway No. : 694	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
10	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[3] Pathway No. : 694	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
11	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[4] Pathway No. : 708	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
12	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[4] Pathway No. : 708	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
13	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[5] Pathway No. : 714	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
14	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[5] Pathway No. : 714	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
15	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[6] Pathway No. : 720	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
16	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[6] Pathway No. : 720	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
17	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[7] Pathway No. : 726	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
18	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[7] Pathway No. : 726	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
19	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[8] Pathway No. : 732	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
20	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[8] Pathway No. : 732	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
21	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[9] Pathway No. : 738	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
22	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[9] Pathway No. : 738	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
23	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[10] Pathway No. : 744	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
24	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[10] Pathway No. : 744	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
25	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[11] Pathway No. : 750	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
26	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[11] Pathway No. : 750	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
27	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[12] Pathway No. : 756	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
28	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[12] Pathway No. : 756	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
29	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[13] Pathway No. : 762	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
30	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[13] Pathway No. : 762	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
31	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[14] Pathway No. : 768	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
32	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[14] Pathway No. : 768	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
33	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[15] Pathway No. : 774	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
34	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[15] Pathway No. : 774	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
35	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[16] Pathway No. : 780	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
36	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[16] Pathway No. : 780	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
37	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[17] Pathway No. : 786	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
38	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[17] Pathway No. : 786	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
39	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[18] Pathway No. : 792	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
40	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[18] Pathway No. : 792	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
41	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[19] Pathway No. : 798	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
42	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[19] Pathway No. : 798	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
43	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[20] Pathway No. : 804	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
44	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[20] Pathway No. : 804	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
45	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[21] Pathway No. : 810	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
46	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[21] Pathway No. : 810	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
47	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[22] Pathway No. : 816	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
48	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[22] Pathway No. : 816	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
49	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[23] Pathway No. : 822	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
50	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[23] Pathway No. : 822	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
51	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[24] Pathway No. : 828	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
52	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[24] Pathway No. : 828	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
53	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[25] Pathway No. : 834	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
54	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[25] Pathway No. : 834	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
55	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[26] Pathway No. : 840	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
56	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[26] Pathway No. : 840	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
57	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[27] Pathway No. : 846	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
58	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[27] Pathway No. : 846	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
59	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[28] Pathway No. : 852	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
60	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[28] Pathway No. : 852	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
61	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[29] Pathway No. : 858	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
62	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[29] Pathway No. : 858	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
63	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[30] Pathway No. : 864	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
64	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[30] Pathway No. : 864	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
65	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[31] Pathway No. : 870	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
66	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[31] Pathway No. : 870	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
67	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[32] Pathway No. : 876	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
68	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[32] Pathway No. : 876	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
69	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[33] Pathway No. : 882	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
70	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[33] Pathway No. : 882	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
71	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[34] Pathway No. : 888	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
72	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[34] Pathway No. : 888	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
73	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[35] Pathway No. : 894	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
74	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[35] Pathway No. : 894	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
75	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[36] Pathway No. : 900	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
76	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[36] Pathway No. : 900	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
77	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[37] Pathway No. : 906	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
78	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[37] Pathway No. : 906	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms
79	MAPK* / MAPK*-feedback	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[38] Pathway No. : 912	25.6405	10	4	explicit E-S complex	Substrate craf-1* Product craf-1**
	Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK notes.*
80	PPhosphatase2A / craf-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[38] Pathway No. : 912	15.6567	6	4	explicit E-S complex	Substrate craf-1* Product craf-1
	See parent PPhosphatase2A for parms

craf-1* acting as a Product of an Enzyme in Ajay_Bhalla_2007_ReacDiff2 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
2	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
3	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics Pathway No. : 684	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
4	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics Pathway No. : 684	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
5	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[1] Pathway No. : 690	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
6	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[1] Pathway No. : 690	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
7	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[2] Pathway No. : 697	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
8	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[2] Pathway No. : 697	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
9	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[3] Pathway No. : 694	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
10	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[3] Pathway No. : 694	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
11	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[4] Pathway No. : 708	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
12	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[4] Pathway No. : 708	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
13	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[5] Pathway No. : 714	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
14	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[5] Pathway No. : 714	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
15	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[6] Pathway No. : 720	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
16	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[6] Pathway No. : 720	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
17	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[7] Pathway No. : 726	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
18	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[7] Pathway No. : 726	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
19	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[8] Pathway No. : 732	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
20	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[8] Pathway No. : 732	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
21	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[9] Pathway No. : 738	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
22	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[9] Pathway No. : 738	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
23	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[10] Pathway No. : 744	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
24	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[10] Pathway No. : 744	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
25	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[11] Pathway No. : 750	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
26	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[11] Pathway No. : 750	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
27	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[12] Pathway No. : 756	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
28	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[12] Pathway No. : 756	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
29	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[13] Pathway No. : 762	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
30	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[13] Pathway No. : 762	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
31	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[14] Pathway No. : 768	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
32	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[14] Pathway No. : 768	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
33	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[31] Pathway No. : 870	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
34	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[15] Pathway No. : 774	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
35	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[15] Pathway No. : 774	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
36	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[16] Pathway No. : 780	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
37	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[16] Pathway No. : 780	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
38	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[17] Pathway No. : 786	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
39	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[17] Pathway No. : 786	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
40	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[18] Pathway No. : 792	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
41	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[18] Pathway No. : 792	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
42	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[19] Pathway No. : 798	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
43	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[19] Pathway No. : 798	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
44	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[20] Pathway No. : 804	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
45	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[20] Pathway No. : 804	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
46	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[21] Pathway No. : 810	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
47	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[21] Pathway No. : 810	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
48	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[22] Pathway No. : 816	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
49	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[22] Pathway No. : 816	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
50	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[23] Pathway No. : 822	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
51	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[23] Pathway No. : 822	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
52	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[24] Pathway No. : 828	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
53	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[24] Pathway No. : 828	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
54	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[25] Pathway No. : 834	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
55	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[25] Pathway No. : 834	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
56	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[26] Pathway No. : 840	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
57	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[26] Pathway No. : 840	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
58	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[27] Pathway No. : 846	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
59	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[27] Pathway No. : 846	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
60	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[28] Pathway No. : 852	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
61	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[28] Pathway No. : 852	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
62	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[29] Pathway No. : 858	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
63	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[29] Pathway No. : 858	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
64	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[30] Pathway No. : 864	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
65	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[30] Pathway No. : 864	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
66	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[31] Pathway No. : 870	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
67	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[32] Pathway No. : 876	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
68	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[32] Pathway No. : 876	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
69	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[33] Pathway No. : 882	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
70	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[33] Pathway No. : 882	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
71	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[34] Pathway No. : 888	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
72	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[34] Pathway No. : 888	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
73	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[35] Pathway No. : 894	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
74	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[35] Pathway No. : 894	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
75	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[36] Pathway No. : 900	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
76	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[36] Pathway No. : 900	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
77	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[37] Pathway No. : 906	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
78	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[37] Pathway No. : 906	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
79	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[38] Pathway No. : 912	20.0005	4	4	explicit E-S complex	Substrate craf-1 Product craf-1*
	Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
80	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[38] Pathway No. : 912	15.6567	6	4	explicit E-S complex	Substrate craf-1 Product** craf-1*
	Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.

craf-1* acting as a Substrate in a reaction in Ajay_Bhalla_2007_ReacDiff2 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	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
2	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
3	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
4	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics Pathway No. : 684	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
5	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
6	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[1] Pathway No. : 690	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
7	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
8	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[2] Pathway No. : 697	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
9	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
10	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[3] Pathway No. : 694	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
11	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
12	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[4] Pathway No. : 708	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
13	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
14	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[5] Pathway No. : 714	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
15	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
16	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[6] Pathway No. : 720	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
17	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
18	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[7] Pathway No. : 726	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
19	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
20	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[8] Pathway No. : 732	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
21	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
22	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[9] Pathway No. : 738	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
23	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
24	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[10] Pathway No. : 744	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
25	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
26	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[11] Pathway No. : 750	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
27	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
28	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[12] Pathway No. : 756	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
29	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
30	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[13] Pathway No. : 762	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
31	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
32	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[14] Pathway No. : 768	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
33	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
34	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[15] Pathway No. : 774	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
35	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
36	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[16] Pathway No. : 780	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
37	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
38	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[17] Pathway No. : 786	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
39	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
40	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[18] Pathway No. : 792	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
41	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
42	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[19] Pathway No. : 798	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
43	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
44	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[20] Pathway No. : 804	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
45	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
46	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[21] Pathway No. : 810	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
47	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
48	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[22] Pathway No. : 816	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
49	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
50	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[23] Pathway No. : 822	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
51	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
52	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[24] Pathway No. : 828	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
53	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
54	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[25] Pathway No. : 834	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
55	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
56	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[26] Pathway No. : 840	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
57	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
58	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[27] Pathway No. : 846	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
59	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
60	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[28] Pathway No. : 852	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
61	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
62	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[29] Pathway No. : 858	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
63	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
64	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[30] Pathway No. : 864	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
65	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
66	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[31] Pathway No. : 870	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
67	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
68	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[32] Pathway No. : 876	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
69	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
70	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[33] Pathway No. : 882	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
71	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
72	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[34] Pathway No. : 888	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
73	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
74	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[35] Pathway No. : 894	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
75	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
76	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[36] Pathway No. : 900	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
77	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
78	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[37] Pathway No. : 906	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
79	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	kinetics[38] Pathway No. : 912	9.9998 (uM^-1 s^-1)	0.5 (s^-1)	Kd(bf) = 0.05(uM)	-	Substrate GTP-Ras craf-1* Product Raf*-GTP-Ras
	Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.

craf-1* acting as a Product in a reaction in Ajay_Bhalla_2007_ReacDiff2 Network

	Name	Accession Name	Pathway Name	Kf	Kb	Kd	tau	Reagents
1	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
2	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
3	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
4	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
5	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
6	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
7	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
8	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
9	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
10	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
11	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
12	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
13	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
14	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
15	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
16	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
17	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
18	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
19	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
20	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
21	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
22	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
23	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
24	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
25	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
26	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
27	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
28	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
29	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
30	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
31	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
32	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
33	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
34	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
35	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
36	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
37	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
38	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*
39	diff	Ajay_Bhalla_ 2007_ReacDiff2 Accession No. : 83	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff Pathway No. : 677	0.101 (s^-1)	0.001 (s^-1)	Keq = 0.0099(uM)	9.804sec	Substrate craf-1* Product craf-1*

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