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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_
    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.

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

    Accession No. : 64
  • AC
    Pathway No. : 278
    00.09No
    This version is activated by Gs and by a betagamma and phosphorylation.

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

    Accession No. : 64
  • AC
    Pathway No. : 278
    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_strong_coupling Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKC-active  /
    phosph-AC2
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_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-AC2
  • AMPAR_CaMKII_
    strong_coupling

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