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Molecule Parameter List for cAMP-PDE | 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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | AMPAR_CaMKII_
weak_coupling | 65 | Network |
Shared_Object_AMPAR_CaMKII_weak_coupling, CaMKII, CaM,
PP1, PP2B, PP1_PSD,
AMPAR, PKA, AC,
AMPAR_memb, PP1_CaMKII_PSD, CaMKII_PSD | | This is a model of weak coupling between the AMPAR traffikcing bistability, and the CaMKII autophosphorylation bistability. In this model, there are three stable states: Both off, AMPAR on, or both on. The fourth possible state: CaMKII on but AMPAR off, is not truly stable, since over the course of hours the AMPAR also turns on. |
cAMP-PDE acting as a Molecule in AMPAR_CaMKII_weak_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | cAMP-PDE | AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | AC
Pathway No. : 289 | 0.5556 | 0.09 | No | | The levels of the PDE are not known at this time. However, enough kinetic info and info about steady-state levels of cAMP etc are around to make it possible to estimate this. 18 Feb 2005: After some playing with initial conc, it is now back at 0.5 uM. |
cAMP-PDE acting as an Enzyme in AMPAR_CaMKII_weak_coupling Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | cAMP-PDE /
PDE
| AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | AC
Pathway No. : 289 | 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 |
cAMP-PDE acting as a Substrate for an Enzyme in AMPAR_CaMKII_weak_coupling Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PKA-active /
phosph-PDE | AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | PKA
Pathway No. : 288 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate
cAMP-PDE
Product
cAMP-PDE*
| | Same rates as PKA-phosph-I1 |
cAMP-PDE acting as a Product in a reaction in AMPAR_CaMKII_weak_coupling 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-PDE | AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | AC
Pathway No. : 289 | 0.01
(s^-1) | 0
(s^-1) | - | - | Substrate
cAMP-PDE*
Product
cAMP-PDE
| | The rates for this are poorly constrained. In adipocytes (probably a different PDE) the dephosphorylation is complete within 15 min, but there are no intermediate time points so it could be much faster. Identity of phosphatase etc is still unknown. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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