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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 | Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning | 77 | Network | Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning, PKC, PLA2, PLCbeta, Ras, Gq, MAPK, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC, MKP3, PKM | This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a. |
cAMP-PDE acting as a Molecule in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | cAMP-PDE | Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77 | AC Pathway No. : 344 | 0.45 | 1.5 | 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. |
cAMP-PDE acting as an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | cAMP-PDE / PDE
| Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77 | AC Pathway No. : 344 | 19.8413 | 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 Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
cAMP-PDE acting as a Product in a reaction in Ajay_Bhalla_2004_PKM_MKP3_Tuning 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 | Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77 | AC Pathway No. : 344 | 0.1 (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. |
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