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Molecule Parameter List for PKC-Ca | 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-Ca acting as a Molecule in MAPK-bistability-fig1c Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | PKC-Ca | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 0 | 1000 | No | | This intermediate is strongly indicated by the synergistic activation of PKC by combinations of DAG and Ca, as well as AA and Ca. PKC by definition also has a direct Ca-activation, to which this also contributes. |
PKC-Ca acting as a Substrate 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 | | 1 | PKC-act-by-DAG | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 0.008
(uM^-1 s^-1) | 8.6348
(s^-1) | Kd(bf) = 1079.377(uM) | - | Substrate
DAG
PKC-Ca
Product
PKC-Ca-DAG
| | | Ca.PKC interaction with DAG is modeled by this reaction. Kf based on Shinomura et al PNAS 88 5149-5153 1991 and Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and uses the constraining procedure referred to in the general notes for PKC. | | 2 | PKC-Ca-to-memb | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 1.2705
(s^-1) | 3.5026
(s^-1) | Keq = 2.7569(uM) | 0.21sec | Substrate
PKC-Ca
Product
PKC-Ca-memb*
| | | Membrane translocation is a standard step in PKC activation. It also turns out to be necessary to replicate the curves from Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and Shonomura et al 1991 PNAS 88:5149-5153. These rates are constrained by matching the curves in the above papers and by fixing a rather fast (sub-second) tau for PKC activation. | | 3 | PKC-act-by-Ca-AA | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 0.0012
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 83.3333(uM) | - | Substrate
AA
PKC-Ca
Product
PKC-Ca-AA*
| | | Ca-dependent AA activation of PKC. Note that this step combines the AA activation and also the membrane translocation. From Schaechter and Benowitz 1993 J Neurosci 13(10):4361 |
PKC-Ca 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-Ca | MAPK-bistability
-fig1c
Accession No. : 35 | PKC
Pathway No. : 181 | 0.6
(uM^-1 s^-1) | 0.5
(s^-1) | Kd(bf) = 0.8333(uM) | - | Substrate
Ca
PKC-cytosolic
Product
PKC-Ca
| | This Kd is a straightforward result from the Schaechter and Benowitz 1993 J Neurosci 13(10):4361 curves. The time-course is based on the known rapid activation of PKC and also the fact that Ca association with proteins is typically quite fast. My guess is that this tau of 2 sec is quite conservative and the actualy rate may be much faster. The parameter is quite insensitive for most stimuli. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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