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Molecule Parameter List for AC2*

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
AC2* 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
  • 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.

    AC2* acting as a Molecule in  
    AMPAR_CaMKII_weak_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    AC2*
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    00.09No
    This version is activated by Gs and by a betagamma and phosphorylation.

    AC2* acting as an Enzyme in  
    AMPAR_CaMKII_weak_coupling Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    AC2* /
    kenz
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    300.00224Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    ATP

    Product
    cAMP
    Reduced Km to match expt data for basal activation of AC2 by PKC. Now k1 = 2.9e-6, k2 = 72, k3 = 18 18 Feb: Raised Km to 300 based on BRENDA data. Unlikely to make much difference, given the vast amount of ATP.

    AC2* 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
    PKC-active  /
    phosph-AC2
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • Shared_Object_
    AMPAR_CaMKII_
    weak_coupling

    Pathway No. : 281
  • 33.333744explicit E-S complexSubstrate
    AC2

    Product
    AC2*
    Phorbol esters have little effect on AC1 or on the Gs-stimulation of AC2. So in this model we are only dealing with the increase in basal activation of AC2 induced by PKC k1 = 1.66e-6 k2 = 16 k3 =4

    AC2* acting as a Substrate in a reaction in  
    AMPAR_CaMKII_weak_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-AC2
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    0.1
    (s^-1)
    0
    (s^-1)
    --Substrate
    AC2*

    Product
    AC2
    Random rate.



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