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Molecule Parameter List for AC1-CaM

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
AC1-CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1010001

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.

    AC1-CaM acting as a Molecule in  
    AMPAR_CaMKII_weak_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    AC1-CaM
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    00.09No
    This version of cyclase is Calmodulin activated. Gs stims it but betagamma inhibits.

    AC1-CaM acting as an Enzyme in  
    AMPAR_CaMKII_weak_coupling Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    AC1-CaM /
    kenz
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    299.9984.54Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    ATP

    Product
    cAMP
    17 Feb 2005 Halved Vmax as the amount of enzyme has been doubled to get an integer value in the spine. 18 Feb 2005. Updated Km from BRENDA: EC No 4.6.1.1 Rat Km: 0.95 mM Turnover 12/sec. Human Km: 0.3 mM 12 umol/min/mg for mammalia, turnover is 12/sec See PMID 8663304 by Dessauer and Gilman JBC 271 1996 Unfortunately turnover range is from 34 down to 0.1 in different studies, according to BRENDA.

    AC1-CaM acting as a Product 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
    CaM-bind-AC1
  • AMPAR_CaMKII_
    weak_coupling

    Accession No. : 65
  • AC
    Pathway No. : 289
    49.9997
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 0.02(uM)-Substrate
    AC1
    CaM-Ca4

    Product
    AC1-CaM
    Half-max at 20 nM CaM (Tang et al JBC 266:13 8595-8603 1991 kb/kf = 20 nM = 12000 #/cell so kf = kb/12000 = kb * 8.333e-5



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