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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 | 5 | 0 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
2003 | 50 | Network | Shared_Object_MAPK_network_2003, PKC, PLA2, PLCbeta, Gq, MAPK, Ras, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC |
| This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 | |||
ATP acting as a Molecule in MAPK_network_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| ATP | 2003 Accession No. : 50 | AC Pathway No. : 221 | 5000 | 1000 | Yes | |
| ATP is present in all cells between 2 and 10 mM. See Lehninger. | ||||||
ATP acting as a Substrate for an Enzyme in MAPK_network_2003 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | AC1-CaM / kenz | 2003 Accession No. : 50 | AC Pathway No. : 221 | 20 | 18 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
| 2 | AC2* / kenz | 2003 Accession No. : 50 | AC Pathway No. : 221 | 20.1149 | 7 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
| Reduced Km to match expt data for basal activation of AC2 by PKC. Now k1 = 2.9e-6, k2 = 72, k3 = 18 | ||||||||
| 3 | AC2-Gs / kenz | 2003 Accession No. : 50 | AC Pathway No. : 221 | 20 | 18 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
| 4 | AC1-Gs / kenz | 2003 Accession No. : 50 | AC Pathway No. : 221 | 20 | 18 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
| 5 | AC2*-Gs / kenz | 2003 Accession No. : 50 | AC Pathway No. : 221 | 60 | 54 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate ATP Product cAMP |
color.