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Molecule Parameter List for Gs.AC | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Gs.AC 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 | 0 | 1 |
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 | |||
Gs.AC acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| Gs.AC | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 0 | 1000 | No | |
| This is the active form of the cyclase. | ||||||
Gs.AC 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 |
| Gs.AC / cyclase | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 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) | |||||||
Gs.AC 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 |
| Gs-bind-AC | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 499.998 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.002(uM) | - | Substrate AC GTP.Ga Product Gs.AC |
| Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer Jacobowitz thesis (Mount Sinai 1995) data indicates it is more like 2 nM. | |||||||