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Molecule Parameter List for craf-1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Statistics | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| craf-1 participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction |
| No. of occurrences | 25 | 0 | 0 | 25 | 25 | 25 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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 | |||
craf-1 acting as a Molecule in Ajay_bhalla_2007_ReacDiff1_1e-12 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 377 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 384 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 390 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 396 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 403 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 409 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 415 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 421 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 402 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 432 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 438 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 444 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 450 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 456 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 462 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 468 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 474 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 480 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 486 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 492 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 498 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 504 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 510 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 516 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
| craf-1 | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | MAPK Pathway No. : 522 | 0.5 | 1.5 | No | |
| Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006 | ||||||
craf-1 acting as a Substrate for an Enzyme in Ajay_bhalla_2007_ReacDiff1_1e-12 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Pathway No. : 375 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics Pathway No. : 382 | 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 | ||||||||
| 3 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[1] Pathway No. : 388 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[2] Pathway No. : 394 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[3] Pathway No. : 400 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[4] Pathway No. : 407 | 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 | ||||||||
| 7 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[5] Pathway No. : 413 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[6] Pathway No. : 417 | 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 | ||||||||
| 9 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[7] Pathway No. : 425 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[8] Pathway No. : 430 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[9] Pathway No. : 436 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[10] Pathway No. : 442 | 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 | ||||||||
| 13 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[11] Pathway No. : 448 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[12] Pathway No. : 454 | 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 | ||||||||
| 15 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[13] Pathway No. : 460 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[14] Pathway No. : 466 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[15] Pathway No. : 472 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[16] Pathway No. : 478 | 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 | ||||||||
| 19 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[17] Pathway No. : 484 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[18] Pathway No. : 490 | 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 | ||||||||
| 21 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[19] Pathway No. : 496 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[20] Pathway No. : 502 | 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-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[21] Pathway No. : 508 | 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 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[22] Pathway No. : 514 | 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 | ||||||||
| 25 | PKC-active / PKC-act-raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[23] Pathway No. : 520 | 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 | ||||||||
craf-1 acting as a Product of an Enzyme in Ajay_bhalla_2007_ReacDiff1_1e-12 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Pathway No. : 375 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 2 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics Pathway No. : 382 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 3 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[1] Pathway No. : 388 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 4 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[2] Pathway No. : 394 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 5 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[3] Pathway No. : 400 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 6 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[4] Pathway No. : 407 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 7 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[5] Pathway No. : 413 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 8 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[6] Pathway No. : 417 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 9 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[7] Pathway No. : 425 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 10 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[8] Pathway No. : 430 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 11 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[9] Pathway No. : 436 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 12 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[10] Pathway No. : 442 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 13 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[11] Pathway No. : 448 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 14 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[12] Pathway No. : 454 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 15 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[13] Pathway No. : 460 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 16 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[14] Pathway No. : 466 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 17 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[15] Pathway No. : 472 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 18 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[16] Pathway No. : 478 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 19 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[17] Pathway No. : 484 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 20 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[18] Pathway No. : 490 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 21 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[19] Pathway No. : 496 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 22 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[20] Pathway No. : 502 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 23 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[21] Pathway No. : 508 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 24 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[22] Pathway No. : 514 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
| 25 | PPhosphatase2A / craf-deph | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[23] Pathway No. : 520 | 15.6567 | 6 | 4 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | ||||||||
craf-1 acting as a Substrate in a reaction in Ajay_bhalla_2007_ReacDiff1_1e-12 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 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | Ajay_bhalla_ 2007_ReacDiff1_ 1e-12 Pathway No. : 375 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 2 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics Pathway No. : 382 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 3 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[1] Pathway No. : 388 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 4 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[2] Pathway No. : 394 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 5 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[3] Pathway No. : 400 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 6 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[4] Pathway No. : 407 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 7 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[5] Pathway No. : 413 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 8 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[6] Pathway No. : 417 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 9 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[7] Pathway No. : 425 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 10 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[8] Pathway No. : 430 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 11 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[9] Pathway No. : 436 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 12 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[10] Pathway No. : 442 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 13 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[11] Pathway No. : 448 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 14 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[12] Pathway No. : 454 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 15 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[13] Pathway No. : 460 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 16 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[14] Pathway No. : 466 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 17 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[15] Pathway No. : 472 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 18 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[16] Pathway No. : 478 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 19 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[17] Pathway No. : 484 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 20 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[18] Pathway No. : 490 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 21 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[19] Pathway No. : 496 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 22 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[20] Pathway No. : 502 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 23 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[21] Pathway No. : 508 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 24 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[22] Pathway No. : 514 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
| 25 | -raf | 2007_ReacDiff1_ 1e-12 Accession No. : 81 | kinetics[23] Pathway No. : 520 | 0 (uM^-1 s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras craf-1 Product Raf-GTP-Ras |
| 18 May 2003. This reaction is here to provide basal activity for MAPK as well as the potential for direct EGF stimulus without PKC activation. Based on model from FB/fb28c.g: the model used for MKP-1 turnover. The rates there were constrained by basal activity values. | ||||||||
color.