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Molecule Parameter List for CaMKII-thr286*-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-thr286*-CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1101201

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • MAPK_network_
    2003
  • 50Network
    Shared_Object_MAPK_network_2003 PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC 
    This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53

    CaMKII-thr286*-CaM acting as a Molecule in  
    MAPK_network_2003 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMKII-thr286*-CaM
  • MAPK_network_
    2003

    Accession No. : 50
  • CaMKII
    Pathway No. : 216
    01000No
    From Hanson and Schulman, the thr286 is responsible for autonomous activation of CaMKII.

    CaMKII-thr286*-CaM acting as a Summed Molecule in  
    MAPK_network_2003 Network
    Accession NamePathway NameTargetInput
  • MAPK_network_
    2003

    Accession No. : 50
  • CaMKII
    Pathway No. : 216
    tot_CaM_CaMKIICaMKII-CaM
  • CaMKII-thr286*-C
    aM


  • CaMKII-thr286*-CaM acting as a Substrate for an Enzyme in  
    MAPK_network_2003 Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PP1-active  /
    Deph-thr286
  • MAPK_network_
    2003

    Accession No. : 50
  • Shared_Object_
    MAPK_network_
    2003

    Pathway No. : 206
  • 5.099070.354explicit 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-thr286*-CaM acting as a Product of an Enzyme in  
    MAPK_network_2003 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1tot_CaM_CaMKII  /
    CaM_act_286
  • MAPK_network_
    2003

    Accession No. : 50
  • CaMKII
    Pathway No. : 216
    113.6010.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM

  • 2
  • tot_autonomous_
    CaMKII
      /
    auton_286
  • MAPK_network_
    2003

    Accession No. : 50
  • CaMKII
    Pathway No. : 216
    174.9970.54explicit E-S complexSubstrate
    CaMKII-CaM

    Product
  • CaMKII-thr286*-C
    aM


  • CaMKII-thr286*-CaM acting as a Product in a reaction in  
    MAPK_network_2003 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
  • CaMK-thr286-bind
    -CaM
  • MAPK_network_
    2003

    Accession No. : 50
  • CaMKII
    Pathway No. : 216
    1000.2
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.0001(uM)-Substrate
    CaM-Ca4
    CaMKII-thr286

    Product
  • CaMKII-thr286*-C
    aM

  • Affinity is up 1000X. Time to release is about 20 sec, so the kb is OK at 0.1 This makes Kf around 1.6666e-3



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