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Molecule Parameter List for AMP | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| AMP 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 | 0 | 0 | 2 | 0 | 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 | |||
AMP acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| AMP | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 1000 | 1000 | Yes | |
| Assumed buffered to 1 mM. Value is irrelevant to simulation. | ||||||
AMP 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 | |
| 1 | cAMP-PDE / PDE | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 19.8413 | 10 | 4 | explicit E-S complex | Substrate cAMP Product AMP |
| Best rates are from Conti et al Biochem 34 7979-7987 1995. Though these are for the Sertoli cell form, it looks like they carry nicely into alternatively spliced brain form. See Sette et al JBC 269:28 18271-18274 Km ~2 uM, Vmax est ~ 10 umol/min/mg for pure form. Brain protein is 93 kD but this was 67. So k3 ~10, k2 ~40, k1 ~4.2e-6 | ||||||||
| 2 | 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. | ||||||||