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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 |
model1 | 60 | Network | Shared_Object_AMPAR_traff_model1, CaMKII, CaM, PP1, PP2B, PP1_PSD, PKA, AC, AMPAR, AMPAR_memb |
| This is the basic model of AMPAR trafficking bistability. It is based on Hayer and Bhalla, PLoS Comput. Biol. 2005. It includes the degradation and turnover of AMPARs. The CaMKII portion of the model is not bistable. | |||
AC2* acting as a Molecule in AMPAR_traff_model1 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| AC2* | model1 Accession No. : 60 | AC Pathway No. : 251 | 0 | 0.09 | No | |
| This version is activated by Gs and by a betagamma and phosphorylation. | ||||||
AC2* acting as an Enzyme in AMPAR_traff_model1 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| AC2* / kenz | model1 Accession No. : 60 | AC Pathway No. : 251 | 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_model1 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PKC-active / phosph-AC2 | model1 Accession No. : 60 | AMPAR_traff_ model1 Pathway No. : 244 | 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_model1 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 | model1 Accession No. : 60 | AC Pathway No. : 251 | 0.1 (s^-1) | 0 (s^-1) | - | - | Substrate AC2* Product AC2 |
| Random rate. | |||||||
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