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Molecule Parameter List for PKC-active | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Statistics | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PKC-active participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction |
| No. of occurrences | 1 | 1 | 3 | 0 | 0 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
2007_PKM | 80 | Network | Shared_Object_Ajay_Bhalla_2007_PKM, PKC, MAPK, Ras, CaM, PKM |
| This is a non-bistable model of ERKII signaling that also incorporates PKM synthesis triggered by Ca influx. It is a simplified variant of the model of Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. | |||
PKC-active acting as a Molecule in Ajay_Bhalla_2007_PKM Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| PKC-active | 2007_PKM Accession No. : 80 | Ajay_Bhalla_ 2007_PKM Pathway No. : 369 | 0 | 1.5 | No |
PKC-active acting as a Summed Molecule in Ajay_Bhalla_2007_PKM Network
| Accession Name | Pathway Name | Target | Input |
2007_PKM Accession No. : 80 | Ajay_Bhalla_ 2007_PKM Pathway No. : 369 | PKC-active | PKC-Ca-memb* PKC-DAG-memb* PKM-zeta |
PKC-active acting as an Enzyme in Ajay_Bhalla_2007_PKM 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_PKM Accession No. : 80 | Ajay_Bhalla_ 2007_PKM Pathway No. : 369 | 20.0001 | 4 | 4 | explicit E-S complex | Substrate craf-1 Product craf-1* |
| Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC | ||||||||
| 2 | PKC-active / PKC-inact-GAP | 2007_PKM Accession No. : 80 | Ajay_Bhalla_ 2007_PKM Pathway No. : 369 | 3.33331 | 4 | 4 | explicit E-S complex | Substrate GAP Product GAP* |
| Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review. | ||||||||
| 3 | PKC-active / PKC-act-GEF | 2007_PKM Accession No. : 80 | Ajay_Bhalla_ 2007_PKM Pathway No. : 369 | 3.33331 | 4 | 4 | explicit E-S complex | Substrate inact-GEF Product GEF* |
| Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X | ||||||||
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