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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PKA-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 | 0 | 1 | 0 | 0 | 1 | 2 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
| cAMP_pathway | 25 | Network | Shared_Object_cAMP_pathway, PKA, AC, Gs |
| This is a model of the canonical cAMP signaling pathway: Ligand->Receptor->G-protein->Cyclase->cAMP->PKA. It also includes phosphodiesterases to balance out cAMP formation.Bhalla US Methods Enzymol. 2002;345:3-23 | |||
PKA-active acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| PKA-active | cAMP_pathway Accession No. : 25 | cAMP_pathway Pathway No. : 134 | 0 | 1000 | No | |
PKA-active acting as an Enzyme in cAMP_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PKA-active / phosph-PDE | cAMP_pathway Accession No. : 25 | cAMP_pathway Pathway No. : 134 | 7.5 | 9 | 4 | explicit E-S complex | Substrate cAMP-PDE Product cAMP-PDE* |
| See Bramson et al CRC crit rev Biochem 15:2 93-124. The rates there are for peptide substrates and too fast. Scaled down by a factor of 3 as per Cohen et al FEBS Lett 76:182-86 (1977). | |||||||
PKA-active acting as a Substrate in a reaction in cAMP_pathway 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 | cAMP_pathway Accession No. : 25 | PKA Pathway No. : 135 | 60 (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. | |||||||
PKA-active acting as a Product in a reaction in cAMP_pathway 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 | cAMP_pathway Accession No. : 25 | PKA Pathway No. : 135 | 60 (s^-1) | 18 (uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | Substrate cAMP4.R2C2 Product PKA-active cAMP4.R2C |
| This has to be fast, as the activation of PKA by cAMP is also fast. kf was 10 | ||||||||
| 2 | Release-C2 | cAMP_pathway Accession No. : 25 | PKA Pathway No. : 135 | 60 (s^-1) | 18 (uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | Substrate cAMP4.R2C Product PKA-active cAMP4.R2 |
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