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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
cAMP-PDE* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1010110

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
PKA_200347Network
Shared_Object_PKA_2003 PKA AC 
Gs 
This model consists of receptor-ligand interaction, G-protein activation, Adenylyl cyclase mediated formation of cAMP and activation of PKA in the neuron. Demonstration programs using this model described in Bhalla US. (2004) Biophys J. 87(2):733-44 to generate a dose-response curve using stochastic calculations are available here.

cAMP-PDE* acting as a Molecule in  
PKA_2003 Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
cAMP-PDE*PKA_2003
Accession No. : 47
AC
Pathway No. : 197
01000No
This form has about 2X activity as plain PDE. See Sette et al (1994 Jul 15) J Biol Chem. 269(28):18271-4

cAMP-PDE* acting as an Enzyme in  
PKA_2003 Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
cAMP-PDE* /
PDE*
PKA_2003
Accession No. : 47
AC
Pathway No. : 197
19.8413204explicit E-S complexSubstrate
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  
PKA_2003 Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
PKA-active  /
phosph-PDE
PKA_2003
Accession No. : 47
  • Shared_Object_
    PKA_2003

    Pathway No. : 195
  • 7.594explicit E-S complexSubstrate
    cAMP-PDE

    Product
    cAMP-PDE*
    See Bramson et al CRC crit rev Biochem 15:2 93-124. The rates there are for peptide substrates and too fast. Scaled down by a factor of 3 as per Cohen et al FEBS Lett 76:182-86 (1977).

    cAMP-PDE* acting as a Substrate in a reaction in  
    PKA_2003 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.
    NameAccession NamePathway NameKfKbKdtauReagents
    dephosph-PDEPKA_2003
    Accession No. : 47
    AC
    Pathway No. : 197
    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
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