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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 |
Accession and Pathway Details | |
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 | Shared_Object_
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
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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