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Molecule Parameter List for ATP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ATP 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 | 1 | 0 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
| PKA_2003 | 47 | Network | Shared_Object_PKA_2003, PKA, AC, Gs |
| This model consists of receptor-ligand interaction, G-protein activation, Adenylyl cyclase mediated formation of cAMP and activation of PKA in the neuron. Demonstration programs using this model described in Bhalla US. (2004) Biophys J. 87(2):733-44 to generate a dose-response curve using stochastic calculations are available here. | |||
ATP acting as a Molecule in PKA_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| ATP | PKA_2003 Accession No. : 47 | AC Pathway No. : 197 | 5000 | 1000 | Yes | |
| ATP is present in all cells between 2 and 10 mM. See Lehninger. It is assumed buffered since the metabolic activity will take care of its levels. | ||||||
ATP acting as a Substrate for an Enzyme in PKA_2003 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| Gs.AC / cyclase | PKA_2003 Accession No. : 47 | AC Pathway No. : 197 | 20 | 18 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
| See Feinstein et al PNAS 88:10173-10177, Jacobowitz et al JBC 286(6):3829-3832 Smigel, JBC 261(4):1976-1982 (1986) | |||||||
color.