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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 | 1 | 0 | 0 | 1 | 1 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
| 3d_fold_model | 8 | Network | Shared_Object_3d_fold_model, PKC, MAPK, PLA2, Ras |
| This model is an annotated version of the synaptic signaling network. The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated Bhalla US, Ram PT, Iyengar R. Science. 2002 Aug 9;297(5583):1018-23. | |||
craf-1 acting as a Molecule in 3d_fold_model Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| craf-1 | 3d_fold_model Accession No. : 8 | MAPK Pathway No. : 56 | 0.2 | 1000 | 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 | ||||||
craf-1 acting as a Substrate for an Enzyme in 3d_fold_model Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PKC-active / PKC-act-raf | 3d_fold_model Accession No. : 8 | 3d_fold_model Pathway No. : 54 | 66.6667 | 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 3d_fold_model Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PPhosphatase2A / craf-deph | 3d_fold_model Accession No. : 8 | 3d_fold_model Pathway No. : 54 | 15.6566 | 6 | 4.16667 | explicit E-S complex | Substrate craf-1* Product craf-1 |
| See parent PPhosphatase2A for parms | |||||||
color.