|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
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 | 0.09 | No | | This form has about 2X activity as plain PDE. See Sette et al JBC 269:28 18271-18274 1994. |
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 | 19.8413 | 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. |
cAMP-PDE* 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 | 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 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-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
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|
