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Molecule Parameter List for AC2* | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| AC2* 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 |
model0 | 59 | Network | Shared_Object_AMPAR_traff_model0, CaMKII, CaM, PP1, PP2B, PP1_PSD, PKA, AC, AMPAR, AMPAR_memb |
| This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno ver reactions for AMPAR. | |||
AC2* acting as a Molecule in AMPAR_traff_model0 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| AC2* | model0 Accession No. : 59 | AC Pathway No. : 241 | 0 | 0.09 | No | |
| This version is activated by Gs and by a betagamma and phosphorylation. | ||||||
AC2* acting as an Enzyme in AMPAR_traff_model0 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| AC2* / kenz | model0 Accession No. : 59 | AC Pathway No. : 241 | 300.002 | 2 | 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 18 Feb: Raised Km to 300 based on BRENDA data. Unlikely to make much difference, given the vast amount of ATP. | |||||||
AC2* acting as a Product of an Enzyme in AMPAR_traff_model0 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PKC-active / phosph-AC2 | model0 Accession No. : 59 | AMPAR_traff_ model0 Pathway No. : 234 | 33.3337 | 4 | 4 | explicit E-S complex | Substrate AC2 Product AC2* |
| Phorbol esters have little effect on AC1 or on the Gs-stimulation of AC2. So in this model we are only dealing with the increase in basal activation of AC2 induced by PKC k1 = 1.66e-6 k2 = 16 k3 =4 | |||||||
AC2* acting as a Substrate in a reaction in AMPAR_traff_model0 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-AC2 | model0 Accession No. : 59 | AC Pathway No. : 241 | 0.1 (s^-1) | 0 (s^-1) | - | - | Substrate AC2* Product AC2 |
| Random rate. | |||||||
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