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Molecule Parameter List for PKC-DAG | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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-DAG 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 | 0 | 0 | 1 | 1 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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-DAG acting as a Molecule in Ajay_Bhalla_2007_Bistable Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| PKC-DAG | 2007_Bistable Accession No. : 79 | PKC Pathway No. : 364 | 0 | 125.7 | No | |
| CoInit was .0624 | ||||||
PKC-DAG acting as a Substrate in a reaction in Ajay_Bhalla_2007_Bistable 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 |
| PKC-n-DAG-AA | 2007_Bistable Accession No. : 79 | PKC Pathway No. : 364 | 0.018 (uM^-1 s^-1) | 2 (s^-1) | Kd(bf) = 111.113(uM) | - | Substrate AA PKC-DAG Product PKC-DAG-AA |
| Reduced kf to 0.66X to match Shinomura et al data. Initial: kf = 3.3333e-9 New: 2e-9 Newer: 2e-8 kb was 0.2 now 2. | |||||||
PKC-DAG acting as a Product in a reaction in Ajay_Bhalla_2007_Bistable 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 |
| PKC-n-DAG | 2007_Bistable Accession No. : 79 | PKC Pathway No. : 364 | 0.0006 (uM^-1 s^-1) | 0.1 (s^-1) | Kd(bf) = 166.6656(uM) | - | Substrate DAG PKC-cytosolic Product PKC-DAG |
| kf raised 10 X based on Shinomura et al PNAS 88 5149-5153 1991 closer analysis of Shinomura et al: kf now 1e-8 (was 1.66e-8). Further tweak. To get sufficient AA synergy, increase kf to 1.5e-8 26 June 1996: Corrected DAG levels: reduce kf by 15x from 1.5e-8 to 1e-9 | |||||||
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