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Molecule Parameter List for AMP

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
AMP participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000400

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_CaMKII_
    weak_coupling
  • 65Network
    Shared_Object_AMPAR_CaMKII_weak_coupling CaMKII CaM 
    PP1 PP2B PP1_PSD 
    AMPAR PKA AC 
    AMPAR_memb PP1_CaMKII_PSD CaMKII_PSD 
    This is a model of weak coupling between the AMPAR traffikcing bistability, and the CaMKII autophosphorylation bistability. In this model, there are three stable states: Both off, AMPAR on, or both on. The fourth possible state: CaMKII on but AMPAR off, is not truly stable, since over the course of hours the AMPAR also turns on.

    AMP acting as a Molecule in  
    AMPAR_CaMKII_weak_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    AMP
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    00.09No

    AMP acting as a Product of an Enzyme in  
    AMPAR_CaMKII_weak_coupling Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1cAMP-PDE  /
    PDE
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    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
    2cAMP-PDE*  /
    PDE*
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    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.
    3PDE1  /
    PDE1
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    39.69991.6674.0012explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        Rate is 1/6 of the CaM stim form. We'll just reduce all lf k1, k2, k3 so that the Vmax goes down 1/6.
    4CaM.PDE1  /
    CaM.PDE1
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    39.6831104explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        Max activity ~10umol/min/mg in presence of lots of CaM. Affinity is low, 40 uM. k3 = 10, k2 = 40, k1 = (50/40) / 6e5.



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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