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Molecule Parameter List for AMP | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| AMP 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 | 0 | 4 | 0 | 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. | |||
AMP acting as a Molecule in AMPAR_traff_model1 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| AMP | model1 Accession No. : 60 | AC Pathway No. : 251 | 0 | 0.09 | No | |
AMP 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 | |
| 1 | cAMP-PDE / PDE | model1 Accession No. : 60 | AC Pathway No. : 251 | 19.8411 | 10 | 4 | explicit E-S complex | Substrate cAMP Product AMP |
| Best rates are from Conti et al Biochem 34 7979-7987 1995. Though these are for the Sertoli cell form, it looks like they carry nicely into alternatively spliced brain form. See Sette et al JBC 269:28 18271-18274 Km ~2 uM, Vmax est ~ 10 umol/min/mg for pure form. Brain protein is 93 kD but this was 67. So k3 ~10, k2 ~40, k1 ~4.2e-6 | ||||||||
| 2 | cAMP-PDE* / PDE* | model1 Accession No. : 60 | AC Pathway No. : 251 | 19.8413 | 20 | 4 | explicit E-S complex | Substrate cAMP Product AMP |
| This form has about twice the activity of the unphosphorylated form. See Sette et al JBC 269:28 18271-18274 1994. We'll ignore cGMP effects for now. | ||||||||
| 3 | PDE1 / PDE1 | model1 Accession No. : 60 | AC Pathway No. : 251 | 39.6999 | 1.667 | 4.0012 | explicit E-S complex | Substrate cAMP Product AMP |
| Rate is 1/6 of the CaM stim form. We'll just reduce all lf k1, k2, k3 so that the Vmax goes down 1/6. | ||||||||
| 4 | CaM.PDE1 / CaM.PDE1 | model1 Accession No. : 60 | AC Pathway No. : 251 | 39.6831 | 10 | 4 | explicit E-S complex | Substrate cAMP Product AMP |
| Max activity ~10umol/min/mg in presence of lots of CaM. Affinity is low, 40 uM. k3 = 10, k2 = 40, k1 = (50/40) / 6e5. | ||||||||
color.