Accession Name | Accession No. | Accession Type | Pathway Link |
Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 | 81 | Network | Shared_Object_Ajay_bhalla_2007_ReacDiff1_1e-12, 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, 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, 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-12_Fig4A which was used for the model to replicate Figure 4A from the paper.
This stimulus file pkm_mapk22_diff_1e-12_Fig4G which was used for the model to replicate Figure 4G from the paper |
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 377 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 384 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 390 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 396 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 403 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 409 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 415 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 421 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 402 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 432 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 438 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 444 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 450 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 456 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 462 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 468 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 474 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 480 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 486 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 492 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 498 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 504 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 510 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 516 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK-tyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 522 | 0 | 1.5 | No |
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
1 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 377 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
2 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | Shared_Object_ Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Pathway No. : 375 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
3 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 384 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
4 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics Pathway No. : 382 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
5 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 390 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
6 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[1] Pathway No. : 388 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
7 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 396 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
8 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[2] Pathway No. : 394 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
9 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 403 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
10 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[3] Pathway No. : 400 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
11 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 409 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
12 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[4] Pathway No. : 407 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
13 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 415 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
14 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[5] Pathway No. : 413 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
15 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 421 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
16 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[6] Pathway No. : 417 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
17 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 402 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
18 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[7] Pathway No. : 425 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
19 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 432 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
20 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[8] Pathway No. : 430 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
21 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 438 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
22 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[9] Pathway No. : 436 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
23 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 444 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
24 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[10] Pathway No. : 442 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
25 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 450 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
26 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[11] Pathway No. : 448 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
27 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 456 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
28 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[12] Pathway No. : 454 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
29 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 462 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
30 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[13] Pathway No. : 460 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
31 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 468 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
32 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[14] Pathway No. : 466 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
33 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 474 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
34 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[15] Pathway No. : 472 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
35 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 480 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
36 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[16] Pathway No. : 478 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
37 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 486 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
38 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[17] Pathway No. : 484 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
39 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 492 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
40 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[18] Pathway No. : 490 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
41 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 498 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
42 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[19] Pathway No. : 496 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
43 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 504 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
44 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[20] Pathway No. : 502 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
45 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 510 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
46 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[21] Pathway No. : 508 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
47 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 516 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
48 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[22] Pathway No. : 514 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
49 | MAPKK* / MAPKKthr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 522 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK*
|
| Rate consts same as for MAPKKtyr. |
50 | MKP-1 / MKP1-tyr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[23] Pathway No. : 520 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK-tyr
Product MAPK
|
| The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
1 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 377 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
2 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | Shared_Object_ Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Pathway No. : 375 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
3 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 384 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
4 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics Pathway No. : 382 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
5 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 390 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
6 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[1] Pathway No. : 388 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
7 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 396 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
8 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[2] Pathway No. : 394 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
9 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 403 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
10 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[3] Pathway No. : 400 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
11 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 409 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
12 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[4] Pathway No. : 407 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
13 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 415 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
14 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[5] Pathway No. : 413 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
15 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 421 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
16 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[6] Pathway No. : 417 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
17 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 402 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
18 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[7] Pathway No. : 425 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
19 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 432 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
20 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[8] Pathway No. : 430 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
21 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 438 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
22 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[9] Pathway No. : 436 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
23 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 444 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
24 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[10] Pathway No. : 442 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
25 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 450 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
26 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[11] Pathway No. : 448 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
27 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 456 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
28 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[12] Pathway No. : 454 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
29 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 462 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
30 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[13] Pathway No. : 460 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
31 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 468 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
32 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[14] Pathway No. : 466 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
33 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 474 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
34 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[15] Pathway No. : 472 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
35 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 480 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
36 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[16] Pathway No. : 478 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
37 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 486 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
38 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[17] Pathway No. : 484 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
39 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 492 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
40 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[18] Pathway No. : 490 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
41 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 498 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
42 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[19] Pathway No. : 496 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
43 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 504 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
44 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[20] Pathway No. : 502 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
45 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 510 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
46 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[21] Pathway No. : 508 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
47 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 516 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
48 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[22] Pathway No. : 514 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |
49 | MAPKK* / MAPKKtyr | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 522 | 0.0462964 | 0.3 | 4 | explicit E-S complex | Substrate MAPK
Product MAPK-tyr
|
| The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 |
50 | MKP-1 / MKP1-thr-deph | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[23] Pathway No. : 520 | 7.00003 | 4 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
|
| See MKP1-tyr-deph |