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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_traff_
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. |
cAMP-PDE acting as a Molecule in AMPAR_traff_model1 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | cAMP-PDE | AMPAR_traff_
model1
Accession No. : 60 | AC
Pathway No. : 251 | 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_traff_model1 Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | cAMP-PDE /
PDE
| AMPAR_traff_
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 |
cAMP-PDE acting as a Substrate for an Enzyme in AMPAR_traff_model1 Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PKA-active /
phosph-PDE | AMPAR_traff_
model1
Accession No. : 60 | PKA
Pathway No. : 250 | 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_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-PDE | AMPAR_traff_
model1
Accession No. : 60 | AC
Pathway No. : 251 | 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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