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Molecule Parameter List for 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
CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000120

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_traff_
    model0
  • 59Network
    Shared_Object_AMPAR_traff_model0 CaMKII CaM 
    PP1 PP2B PP1_PSD 
    PKA AC AMPAR 
    AMPAR_memb 
    This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno ver reactions for AMPAR.

    CaM acting as a Molecule in  
    AMPAR_traff_model0 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaM
  • AMPAR_traff_
    model0

    Accession No. : 59
  • CaM
    Pathway No. : 236
    26.33330.09No
    There is a LOT of this in the cell: upto 1% of total protein mass. (Alberts et al) Say 25 uM. Meyer et al Science 256 1199-1202 1992 refer to studies saying it is comparable to CaMK levels.

    CaM acting as a Product of an Enzyme in  
    AMPAR_traff_model0 Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKC-active  /
  • PKC-phosph-ng-Ca
    M
  • AMPAR_traff_
    model0

    Accession No. : 59
  • Shared_Object_
    AMPAR_traff_
    model0

    Pathway No. : 234
  • 28.59560.354explicit E-S complexSubstrate
    neurogranin-CaM

    Product
    CaM
    neurogranin*
    Rates are 60% those of PKC-phosph-neurogranin. See Huang et al ABB 305:2 570-580 1993

    CaM acting as a Substrate in a reaction in  
    AMPAR_traff_model0 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
    1CaM-TR2-bind-Ca
  • AMPAR_traff_
    model0

    Accession No. : 59
  • CaM
    Pathway No. : 236
    71.999
    (uM^-2 s^-1)
    72
    (s^-1)
    Kd(af) = 1(uM)-Substrate
    Ca
    Ca
    CaM

    Product
    CaM-TR2-Ca2
      Lets use the fast rate consts here. Since the rates are so different, I am not sure whether the order is relevant. These correspond to the TR2C fragment. We use the Martin et al rates here, plus the Drabicowski binding consts. All are scaled by 3X to cell temp. kf = 2e-10 kb = 72 Stemmer & Klee: K1=.9, K2=1.1. Assume 1.0uM for both. kb/kf=3.6e11. If kb=72, kf = 2e-10 (Exactly the same !)....
    2
  • neurogranin-bind
    -CaM
  • AMPAR_traff_
    model0

    Accession No. : 59
  • CaM
    Pathway No. : 236
    0.3
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 3.3333(uM)-Substrate
    CaM
    neurogranin

    Product
    neurogranin-CaM
      Surprisingly, no direct info on rates from neurogranin at this time. These rates are based on GAP-43 binding studies. As GAP-43 and neurogranin share near identity in the CaM/PKC binding regions, and also similarity in phosph and dephosph rates, I am borrowing GAP-43 kinetic info. See Alexander et al JBC 262:13 6108-6113 1987



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