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Molecule Parameter List for PKC-DAG-AA* | 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 | |
PKC-DAG-AA* acting as a Molecule in MAPK-bistability-fig1c Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | PKC-DAG-AA* | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 0 | 1000 | No | | Membrane translocated form of PKC-DAG-AA complex. |
PKC-DAG-AA* acting as a Summed Molecule in MAPK-bistability-fig1c Network
| Accession Name | Pathway Name | Target | Input | MAPK-bistability
-fig1c
Accession No. : 35 | Shared_Object_
MAPK-bistability
-fig1c
Pathway No. : 179 | PKC-active | PKC-DAG-AA*
PKC-Ca-memb*
PKC-Ca-AA*
PKC-DAG-memb*
PKC-basal*
PKC-AA*
| | This is the total active PKC. It is the sum of the respective activities of PKC-basal* PKC-Ca-memb* PKC-DAG-memb* PKC-Ca-AA* PKC-DAG-AA* PKC-AA* I treat PKC here in a two-state manner: Either it is in an active state (any one of the above list) or it is inactive. No matter what combination of stimuli activate the PKC, I treat it as having the same activity. The scaling comes in through the relative amounts of PKC which bind to the respecive stimuli. The justification for this is the mode of action of PKC, which like most Ser/Thr kinases has a kinase domain normally bound to and blocked by a regulatory domain. I assume that all the activators simply free up the kinase domain. A more general model would incorporate a different enzyme activity for each combination of activating inputs, as well as for each substrate. The current model seems to be a decent and much simpler approximation for the available data. One caveat of this way of representing PKC is that the summation procedure assumes that PKC does not saturate with its substrates. If this assumption fails, then the contributing PKC complexes would experience changes in availability which would affect their balance. Given the relatively low percentage of PKC usually activated, and its high throughput as an enzyme, this is a safe assumption under physiological conditions. |
PKC-DAG-AA* acting as a Product in a reaction in MAPK-bistability-fig1c 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-act-by-DAG-A
A | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 2
(s^-1) | 0.2
(s^-1) | Keq = 0.1(uM) | 0.455sec | Substrate
PKC-DAG-AA
Product
PKC-DAG-AA*
| | Membrane translocation step for PKC-DAG-AA complex. Rates from matching concentration-effect data in our two main references: Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and Shinomura et al 1988 PNAS 88: 5149-5153 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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