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Molecule Parameter List for CaMKII-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
CaMKII-CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1102101

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_Tuning
  • 76Network
    PKC Shared_Object_Ajay_Bhalla_2004_PKM_tuning PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC PKM 
    This model is taken from the Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the reference feedforward model from Figure 8a.

    CaMKII-CaM acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMKII-CaM
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • CaMKII
    Pathway No. : 322
    01.5No

    CaMKII-CaM acting as a Summed Molecule in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    Accession NamePathway NameTargetInput
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • CaMKII
    Pathway No. : 322
    tot_CaM_CaMKIICaMKII-CaM
  • CaMKII-thr286*-C
    aM


  • CaMKII-CaM acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1tot_CaM_CaMKII  /
    CaM_act_286
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • CaMKII
    Pathway No. : 322
    113.6010.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM

  •    
    2
  • tot_autonomous_
    CaMKII
      /
    auton_286
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • CaMKII
    Pathway No. : 322
    1750.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM

  •    

    CaMKII-CaM acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PP1-active  /
    Deph-thr286
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_tuning

    Pathway No. : 312
  • 5.099110.354explicit E-S complexSubstrate
  • CaMKII-thr286*-C
    aM


    Product
    CaMKII-CaM
  • The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35

    CaMKII-CaM acting as a Product in a reaction in  
    Ajay_Bhalla_2004_PKM_Tuning 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
    CaMKII-bind-CaM
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • CaMKII
    Pathway No. : 322
    49.9995
    (uM^-1 s^-1)
    5
    (s^-1)
    Kd(bf) = 0.1(uM)-Substrate
    CaM-Ca4
    CaMKII

    Product
    CaMKII-CaM
    This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol.



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