DOQCS database

NCBS Home page

Accession List

Pathway List

Authorized Users

Help

News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

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_ReacDiff1_ 1e-13	82	Network	Shared_Object_Ajay_Bhalla_2007_ReacDiff1_1e-13, PKC, MAPK, Ras, CaM, PKM, chain, kinetics, PKC, MAPK, Ras, CaM, PKM, kinetics[1], PKC, MAPK, Ras, CaM, PKM, kinetics[2], PKC, MAPK, Ras, CaM, PKM, kinetics[3], PKC, MAPK, Ras, CaM, PKM, kinetics[4], PKC, MAPK, Ras, CaM, PKM, kinetics[5], PKC, MAPK, Ras, kinetics[6], CaM, PKM, 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
This is a 25-compartment reaction-diffusion version of the Ajay_Bhalla_2007_PKM model. The original single-compartment model is repeated 25 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. For D = 1e-13 m^2/sec (i.e., 0.1 micron^2/sec ) the kf and kb are 0.001/sec. The stimulus file pkm_mapk22_diff_1e-13_Fig4B which was used for the model to replicate Figure 4B from the paper. pkm_mapk22_diff_1e-13_Fig4H replicate Figure 4H. pkm_mapk22_diff_1e-13_Fig4I replicate Figure 4I.

craf-1* acting as a Molecule in Ajay_Bhalla_2007_ReacDiff1_1e-13 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 528	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 535	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 541	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 547	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 553	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 559	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 565	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 571	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 577	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 583	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 589	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 595	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 601	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 607	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 613	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 619	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 625	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 631	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 637	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 643	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 649	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 655	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 661	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 667	0	1.5	No
craf-1*	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	MAPK Pathway No. : 673	0	1.5	No

craf-1* acting as a Substrate for an Enzyme in Ajay_Bhalla_2007_ReacDiff1_1e-13 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_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	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_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	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_ReacDiff1_1e-13 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_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	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_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	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	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	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
36	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	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
38	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	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
40	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	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
42	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	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
44	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	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
46	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	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
48	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	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
50	PPhosphatase2A / craf**-deph	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	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_ReacDiff1_1e-13 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_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	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_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	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.

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.