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Molecule Parameter List for PKC-active

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

*PKC-active* 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	25	75	0	0	0	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.

PKC-active acting as a Molecule in Ajay_Bhalla_2007_ReacDiff1_1e-13 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	0	1.5	No
PKC-active	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	0	1.5	No

PKC-active acting as a Summed Molecule in Ajay_Bhalla_2007_ReacDiff1_1e-13 Network

	Accession Nane	Pathway Name	Target	Input
1	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

2	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

3	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

4	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

5	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

6	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

7	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

8	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

9	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

10	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

11	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

12	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

13	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

14	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

15	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

16	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

17	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

18	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

19	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

20	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

21	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

22	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

23	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

24	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

25	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	PKC-active	PKC-Ca-memb* PKC-DAG-memb* PKM-zeta

PKC-active acting as 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	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
3	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	Shared_Object_ Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Pathway No. : 526	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
4	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
5	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
6	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics Pathway No. : 533	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
7	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
8	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
9	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[1] Pathway No. : 539	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
10	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
11	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
12	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[2] Pathway No. : 545	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
13	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
14	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
15	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[3] Pathway No. : 551	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
16	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
17	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
18	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[4] Pathway No. : 557	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
19	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
20	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
21	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[5] Pathway No. : 563	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
22	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
23	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
24	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[6] Pathway No. : 567	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
25	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
26	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
27	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[7] Pathway No. : 575	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
28	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
29	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
30	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[8] Pathway No. : 581	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
31	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
32	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
33	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[9] Pathway No. : 587	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
34	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
35	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
36	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[10] Pathway No. : 593	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
37	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
38	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
39	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[11] Pathway No. : 599	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
40	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
41	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
42	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[12] Pathway No. : 605	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
43	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
44	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
45	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[13] Pathway No. : 611	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
46	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
47	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
48	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[14] Pathway No. : 617	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
49	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
50	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
51	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[15] Pathway No. : 623	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
52	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
53	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
54	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[16] Pathway No. : 629	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
55	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
56	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
57	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[17] Pathway No. : 635	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
58	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
59	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
60	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[18] Pathway No. : 641	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
61	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
62	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
63	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[19] Pathway No. : 647	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
64	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
65	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
66	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[20] Pathway No. : 653	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
67	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
68	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
69	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[21] Pathway No. : 659	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
70	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
71	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
72	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[22] Pathway No. : 665	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X
73	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
74	PKC-active / PKC-inact-GAP	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	3.33333	4	4	explicit E-S complex	Substrate GAP Product GAP*
	Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
75	PKC-active / PKC-act-GEF	Ajay_Bhalla_ 2007_ReacDiff1_ 1e-13 Accession No. : 82	kinetics[23] Pathway No. : 671	3.33333	4	4	explicit E-S complex	Substrate inact-GEF Product GEF*
	Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X

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