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Molecule Parameter List for PKA-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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | | CaMKII_model3 | 63 | Network |
Shared_Object_CaMKII_model3, CaMKII, CaM,
PP1, PP2B, PP1_PSD,
AC, PKA | | This is the complete model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 includes PKA regulatory input. This has little effect on the deterministic calculations, but the PKA pathway introduces a lot of noise which causes a difference in stochastic runs. |
PKA-active acting as a Molecule in CaMKII_model3 Network
PKA-active acting as an Enzyme in CaMKII_model3 Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PKA-active /
PKA-phosph-I1
| CaMKII_model3
Accession No. : 63 | Shared_Object_
CaMKII_model3
Pathway No. : 263 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate
I1
Product
I1*
| | | #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta. | | 2 | PKA-active /
PKA-phosph-I1_
PSD
| CaMKII_model3
Accession No. : 63 | Shared_Object_
CaMKII_model3
Pathway No. : 263 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate
I1
Product
I1*
| | 3 | PKA-active /
phosph-PDE
| CaMKII_model3
Accession No. : 63 | Shared_Object_
CaMKII_model3
Pathway No. : 263 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate
cAMP-PDE
Product
cAMP-PDE*
| | | Same rates as PKA-phosph-I1 |
PKA-active acting as a Substrate in a reaction in CaMKII_model3 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 | | inhib-PKA | CaMKII_model3
Accession No. : 63 | PKA
Pathway No. : 270 | 59.9994
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0167(uM) | - | Substrate
PKA-active
PKA-inhibitor
Product
inhibited-PKA
| | This has to be set to zero for matching the expts in vitro. In vivo we need to consider the inhibition though. kf = 1e-5 kb = 1 |
PKA-active acting as a Product in a reaction in CaMKII_model3 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 | Release-C1 | CaMKII_model3
Accession No. : 63 | PKA
Pathway No. : 270 | 60
(s^-1) | 17.9998
(uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | Substrate
R2C2-cAMP4
Product
PKA-active
R2C-cAMP4
| | | This has to be fast, as the activation of PKA by cAMP is also fast. kf was 10 | | 2 | Release-C2 | CaMKII_model3
Accession No. : 63 | PKA
Pathway No. : 270 | 60
(s^-1) | 17.9998
(uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | Substrate
R2C-cAMP4
Product
PKA-active
R2-cAMP4
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| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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