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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	25	0	0	50	50	25	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2007_ReacDiff3	84	Network	Shared_Object_Ajay_Bhalla_2007_ReacDiff3, PKC, PLA2, MAPK, PLA2, Ras, CaM, chain, kinetics, PKC, MAPK, Ras, CaM, kinetics[1], PKC, PLA2, MAPK, Ras, CaM, kinetics[2], PKC, PLA2, MAPK, Ras, CaM, kinetics[3], PKC, PLA2, MAPK, Ras, CaM, kinetics[4], PKC, PLA2, MAPK, Ras, CaM, kinetics[5], PKC, PLA2, MAPK, Ras, MAPK, CaM, kinetics[6], PKC, PLA2, MAPK, Ras, CaM, kinetics[7], PKC, PLA2, MAPK, Ras, CaM, PKC, kinetics[8], PLA2, MAPK, Ras, CaM, kinetics[9], PKC, PLA2, MAPK, Ras, CaM, kinetics[10], PKC, PLA2, MAPK, Ras, CaM, kinetics[11], PKC, PLA2, MAPK, Ras, CaM, kinetics[12], PKC, PLA2, Ras, CaM, kinetics[13], PKC, PLA2, MAPK, Ras, CaM, kinetics[14], PKC, PLA2, MAPK, Ras, CaM, kinetics[15], PKC, PLA2, MAPK, Ras, kinetics[16], CaM, PKC, PLA2, MAPK, Ras, CaM, kinetics[17], PKC, PLA2, MAPK, Ras, CaM, kinetics[18], PKC, PLA2, MAPK, Ras, CaM, kinetics[19], PKC, PLA2, MAPK, Ras, CaM, kinetics[20], PKC, PLA2, MAPK, Ras, CaM, kinetics[21], PKC, PLA2, MAPK, Ras, CaM, kinetics[22], PKC, PLA2, MAPK, Ras, CaM, kinetics[23], PKC, PLA2, MAPK, Ras, CaM
This is a 25-compartment reaction-diffusion version of the Ajay_Bhalla_2007_bistable model. The original single-compartment model is repeated 25 times. In addition, a subset (33 out of 50) molecules can diffuse between compartments. Diffusion is implemented as a reaction between corresponding molecules in neighboring compartments. Here D = 1e-13 m^2/sec (i.e., 0.1 micron^2/sec ) so the kf and kb of this reaction for these 10 micron compartments are both 0.001/sec. The basal calcium level in this model is held at 95 nM which is rather close to threshold for the flip to the active state. This is necessary to sustain active propagation of activation. The stimulus file bis6-propgn_D1e-13_FigEF which was used for the model to replicate Figure 4E and 4F from the paper.

craf-1* acting as a Molecule in Ajay_Bhalla_2007_ReacDiff3 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 921	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 928	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 940	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 934	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 946	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 952	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 958	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 960	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 965	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 971	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 977	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 983	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 989	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 995	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1006	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1012	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1018	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1024	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1030	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1036	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1042	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1048	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1054	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1060	0	125.7	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	MAPK Pathway No. : 1066	0	125.7	No

craf-1* acting as a Substrate for an Enzyme in Ajay_Bhalla_2007_ReacDiff3 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_ReacDiff3 Accession No. : 84	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff3 Pathway No. : 918	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_ReacDiff3 Accession No. : 84	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff3 Pathway No. : 918	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_ReacDiff3 Accession No. : 84	kinetics Pathway No. : 926	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_ReacDiff3 Accession No. : 84	kinetics Pathway No. : 926	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_ReacDiff3 Accession No. : 84	kinetics[1] Pathway No. : 931	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_ReacDiff3 Accession No. : 84	kinetics[1] Pathway No. : 931	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_ReacDiff3 Accession No. : 84	kinetics[2] Pathway No. : 937	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_ReacDiff3 Accession No. : 84	kinetics[2] Pathway No. : 937	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_ReacDiff3 Accession No. : 84	kinetics[3] Pathway No. : 943	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_ReacDiff3 Accession No. : 84	kinetics[3] Pathway No. : 943	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_ReacDiff3 Accession No. : 84	kinetics[4] Pathway No. : 949	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_ReacDiff3 Accession No. : 84	kinetics[4] Pathway No. : 949	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_ReacDiff3 Accession No. : 84	kinetics[5] Pathway No. : 955	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_ReacDiff3 Accession No. : 84	kinetics[5] Pathway No. : 955	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_ReacDiff3 Accession No. : 84	kinetics[6] Pathway No. : 962	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_ReacDiff3 Accession No. : 84	kinetics[6] Pathway No. : 962	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_ReacDiff3 Accession No. : 84	kinetics[7] Pathway No. : 968	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_ReacDiff3 Accession No. : 84	kinetics[7] Pathway No. : 968	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_ReacDiff3 Accession No. : 84	kinetics[8] Pathway No. : 975	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_ReacDiff3 Accession No. : 84	kinetics[8] Pathway No. : 975	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_ReacDiff3 Accession No. : 84	kinetics[9] Pathway No. : 980	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_ReacDiff3 Accession No. : 84	kinetics[9] Pathway No. : 980	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_ReacDiff3 Accession No. : 84	kinetics[10] Pathway No. : 986	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_ReacDiff3 Accession No. : 84	kinetics[10] Pathway No. : 986	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_ReacDiff3 Accession No. : 84	kinetics[11] Pathway No. : 992	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_ReacDiff3 Accession No. : 84	kinetics[11] Pathway No. : 992	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_ReacDiff3 Accession No. : 84	kinetics[12] Pathway No. : 998	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_ReacDiff3 Accession No. : 84	kinetics[12] Pathway No. : 998	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_ReacDiff3 Accession No. : 84	kinetics[13] Pathway No. : 1003	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_ReacDiff3 Accession No. : 84	kinetics[13] Pathway No. : 1003	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_ReacDiff3 Accession No. : 84	kinetics[14] Pathway No. : 1009	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_ReacDiff3 Accession No. : 84	kinetics[14] Pathway No. : 1009	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_ReacDiff3 Accession No. : 84	kinetics[15] Pathway No. : 1015	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_ReacDiff3 Accession No. : 84	kinetics[15] Pathway No. : 1015	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_ReacDiff3 Accession No. : 84	kinetics[16] Pathway No. : 1020	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_ReacDiff3 Accession No. : 84	kinetics[16] Pathway No. : 1020	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_ReacDiff3 Accession No. : 84	kinetics[17] Pathway No. : 1027	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_ReacDiff3 Accession No. : 84	kinetics[17] Pathway No. : 1027	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_ReacDiff3 Accession No. : 84	kinetics[18] Pathway No. : 1033	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_ReacDiff3 Accession No. : 84	kinetics[18] Pathway No. : 1033	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_ReacDiff3 Accession No. : 84	kinetics[19] Pathway No. : 1039	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_ReacDiff3 Accession No. : 84	kinetics[19] Pathway No. : 1039	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_ReacDiff3 Accession No. : 84	kinetics[20] Pathway No. : 1045	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_ReacDiff3 Accession No. : 84	kinetics[20] Pathway No. : 1045	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_ReacDiff3 Accession No. : 84	kinetics[21] Pathway No. : 1051	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_ReacDiff3 Accession No. : 84	kinetics[21] Pathway No. : 1051	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_ReacDiff3 Accession No. : 84	kinetics[22] Pathway No. : 1057	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_ReacDiff3 Accession No. : 84	kinetics[22] Pathway No. : 1057	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_ReacDiff3 Accession No. : 84	kinetics[23] Pathway No. : 1063	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_ReacDiff3 Accession No. : 84	kinetics[23] Pathway No. : 1063	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_ReacDiff3 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_ReacDiff3 Accession No. : 84	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff3 Pathway No. : 918	66.6665	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_ReacDiff3 Accession No. : 84	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff3 Pathway No. : 918	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_ReacDiff3 Accession No. : 84	kinetics Pathway No. : 926	66.6665	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_ReacDiff3 Accession No. : 84	kinetics Pathway No. : 926	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_ReacDiff3 Accession No. : 84	kinetics[1] Pathway No. : 931	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[1] Pathway No. : 931	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_ReacDiff3 Accession No. : 84	kinetics[2] Pathway No. : 937	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[2] Pathway No. : 937	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_ReacDiff3 Accession No. : 84	kinetics[3] Pathway No. : 943	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[3] Pathway No. : 943	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_ReacDiff3 Accession No. : 84	kinetics[4] Pathway No. : 949	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[4] Pathway No. : 949	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_ReacDiff3 Accession No. : 84	kinetics[5] Pathway No. : 955	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[5] Pathway No. : 955	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_ReacDiff3 Accession No. : 84	kinetics[6] Pathway No. : 962	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[6] Pathway No. : 962	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_ReacDiff3 Accession No. : 84	kinetics[7] Pathway No. : 968	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[7] Pathway No. : 968	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_ReacDiff3 Accession No. : 84	kinetics[8] Pathway No. : 975	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[8] Pathway No. : 975	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_ReacDiff3 Accession No. : 84	kinetics[9] Pathway No. : 980	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[9] Pathway No. : 980	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_ReacDiff3 Accession No. : 84	kinetics[10] Pathway No. : 986	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[10] Pathway No. : 986	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_ReacDiff3 Accession No. : 84	kinetics[11] Pathway No. : 992	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[11] Pathway No. : 992	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_ReacDiff3 Accession No. : 84	kinetics[12] Pathway No. : 998	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[12] Pathway No. : 998	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_ReacDiff3 Accession No. : 84	kinetics[13] Pathway No. : 1003	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[13] Pathway No. : 1003	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_ReacDiff3 Accession No. : 84	kinetics[14] Pathway No. : 1009	66.6665	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_ReacDiff3 Accession No. : 84	kinetics[14] Pathway No. : 1009	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_ReacDiff3 Accession No. : 84	kinetics[15] Pathway No. : 1015	66.6665	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	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[15] Pathway No. : 1015	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.
35	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[16] Pathway No. : 1020	66.6665	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
36	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[16] Pathway No. : 1020	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.
37	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[17] Pathway No. : 1027	66.6665	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
38	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[17] Pathway No. : 1027	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.
39	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[18] Pathway No. : 1033	66.6665	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
40	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[18] Pathway No. : 1033	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.
41	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[19] Pathway No. : 1039	66.6665	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
42	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[19] Pathway No. : 1039	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.
43	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[20] Pathway No. : 1045	66.6665	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
44	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[20] Pathway No. : 1045	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.
45	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[21] Pathway No. : 1051	66.6665	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
46	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[21] Pathway No. : 1051	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.
47	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[22] Pathway No. : 1057	66.6665	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
48	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[22] Pathway No. : 1057	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.
49	PKC-active / PKC-act-raf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[23] Pathway No. : 1063	66.6665	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
50	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[23] Pathway No. : 1063	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_ReacDiff3 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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff3 Pathway No. : 918	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.
2	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics Pathway No. : 926	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[1] Pathway No. : 931	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.
4	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[2] Pathway No. : 937	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[3] Pathway No. : 943	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.
6	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[4] Pathway No. : 949	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[5] Pathway No. : 955	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.
8	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[6] Pathway No. : 962	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[7] Pathway No. : 968	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.
10	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[8] Pathway No. : 975	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[9] Pathway No. : 980	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.
12	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[10] Pathway No. : 986	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[11] Pathway No. : 992	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.
14	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[12] Pathway No. : 998	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[13] Pathway No. : 1003	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.
16	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[14] Pathway No. : 1009	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[15] Pathway No. : 1015	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.
18	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[16] Pathway No. : 1020	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[17] Pathway No. : 1027	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.
20	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[18] Pathway No. : 1033	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[19] Pathway No. : 1039	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.
22	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[20] Pathway No. : 1045	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[21] Pathway No. : 1051	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.
24	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[22] Pathway No. : 1057	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	Ras-act-craf	Ajay_Bhalla_ 2007_ReacDiff3 Accession No. : 84	kinetics[23] Pathway No. : 1063	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.

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