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Molecule Parameter List for cAMP-PDE* | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| cAMP-PDE* 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 | 1 | 1 | 0 |
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 | |||
cAMP-PDE* acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| cAMP-PDE* | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 0 | 1000 | No | |
| This form has about 2X activity as plain PDE. See Sette et al JBC 269:28 18271-18274 1994. | ||||||
cAMP-PDE* 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 |
| cAMP-PDE* / PDE* | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 19.8413 | 20 | 4 | explicit E-S complex | Substrate cAMP Product AMP |
| This form has about twice the activity of the unphosphorylated form. See Sette et al JBC 269:28 18271-18274 1994. We'll ignore cGMP effects for now. | |||||||
cAMP-PDE* acting as a Product of 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). | |||||||
cAMP-PDE* 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 |
| dephosph-PDE | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 0.1 (s^-1) | 0 (s^-1) | - | - | Substrate cAMP-PDE* Product cAMP-PDE |
| The rates for this are poorly constrained. In adipocytes (probably a different PDE) the dephosphorylation is complete within 15 min, but there are no intermediate time points so it could be much faster. Identity of phosphatase etc is still unknown. | |||||||