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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
CaMKII_model363Network
Shared_Object_CaMKII_model3 CaMKII CaM 
PP1 PP2B PP1_PSD 
AC PKA 
This is the complete model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 includes PKA regulatory input. This has little effect on the deterministic calculations, but the PKA pathway introduces a lot of noise which causes a difference in stochastic runs.

cAMP-PDE* acting as a Molecule in  
CaMKII_model3 Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
cAMP-PDE*CaMKII_model3
Accession No. : 63
AC
Pathway No. : 269
00.09No
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  
CaMKII_model3 Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
cAMP-PDE* /
PDE*
CaMKII_model3
Accession No. : 63
AC
Pathway No. : 269
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  
CaMKII_model3 Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
PKA-active  /
phosph-PDE
CaMKII_model3
Accession No. : 63
  • Shared_Object_
    CaMKII_model3

    Pathway No. : 263
  • 7.5000894explicit E-S complexSubstrate
    cAMP-PDE

    Product
    cAMP-PDE*
    Same rates as PKA-phosph-I1

    cAMP-PDE* acting as a Substrate in a reaction in  
    CaMKII_model3 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-PDECaMKII_model3
    Accession No. : 63
    AC
    Pathway No. : 269
    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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