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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 occurrences1011001

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_CaMKII_
    strong_coupling
  • 64Network
    Shared_Object_AMPAR_CaMKII_strong_coupling CaMKII CaM 
    PP1 AMPAR_memb PP2B 
    PKA AC PP1_PSD 
    AMPAR 
    This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on.

    cAMP-PDE acting as a Molecule in  
    AMPAR_CaMKII_strong_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    cAMP-PDE
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • AC
    Pathway No. : 278
    0.55560.09No
    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_CaMKII_strong_coupling Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    cAMP-PDE /
    PDE
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • AC
    Pathway No. : 278
    19.8411104explicit E-S complexSubstrate
    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_CaMKII_strong_coupling Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKA-active  /
    phosph-PDE
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 7.5000894explicit E-S complexSubstrate
    cAMP-PDE

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

    cAMP-PDE acting as a Product in a reaction in  
    AMPAR_CaMKII_strong_coupling 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-PDE
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • AC
    Pathway No. : 278
    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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