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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 | Ajay_Bhalla_
2007_Bistable | 79 | Network |
Shared_Object_Ajay_Bhalla_2007_Bistable, PKC, PLA2,
MAPK, Ras, CaM | This is a model of ERKII signaling which is bistable due to feedback. The feedback occurs through ERKII phosphorylation of phospholipase A2 (PLA2), leading to increased production of arachidonic acid (AA), which activates protein kinase C (PKC) which activates c-Raf which is upstream of ERKII.
The model is a highly simplified variant of more detailed bistable models of MAPK signaling (Bhalla US, Iyengar R. Science. 1999 Jan 15;283(5400):381-7, Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80) |
PKC-active acting as a Molecule in Ajay_Bhalla_2007_Bistable Network
PKC-active acting as a Summed Molecule in Ajay_Bhalla_2007_Bistable Network
PKC-active acting as an Enzyme in Ajay_Bhalla_2007_Bistable Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PKC-active /
PKC-act-raf
| Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 66.6671 | 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
| Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 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
| Ajay_Bhalla_
2007_Bistable
Accession No. : 79 | Shared_Object_
Ajay_Bhalla_
2007_Bistable
Pathway No. : 363 | 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 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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