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Molecule Parameter List for CaMKII***

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*** participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1102200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Osc_Ca_
    IP3metabolism
  • 24Network
    MIPP CaMKII CaM 
    PKC IP3-3K Gq 
    PLCbeta 134_dephos 145_dephos 
    IP4-system IHP-system 1345_dephos 
    CaRegulation Othmer-Tang-model 
    This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It differs from the NonOsc_Ca_IP3metabolism network in the CaRegulation module and in InsP3 receptor kinetics. Details of InsP3 receptor kinetics have been adapted from the Othmer-Tang model for oscillatory Ca dynamics. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    CaMKII*** acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMKII***
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    01000No
    From Hanson and Schulman, the CaMKII does a lot of autophosphorylation just after the CaM is released. This prevents further CaM binding and renders the enzyme quite independent of Ca.

    CaMKII*** acting as a Summed Molecule in  
    Osc_Ca_IP3metabolism Network
    Accession NamePathway NameTargetInput
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    tot_autonomous_CaMKIICaMKII-thr286
    CaMKII***
    This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII***

    CaMKII*** acting as a Substrate for an Enzyme in  
    Osc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP1-active  /
    Deph-thr305
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    5.099070.354explicit E-S complexSubstrate
    CaMKII***

    Product
    CaMKII-thr286
        Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. 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. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    2PP1-active  /
    Deph-thr286c
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    5.099070.354explicit E-S complexSubstrate
    CaMKII***

    Product
    CaMK-thr306
        Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. 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. This gives the final Km of 5.1, and Vmax of 0.35/sec.

    CaMKII*** acting as a Product of an Enzyme in  
    Osc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1tot_CaM_CaMKII  /
    CaM_act_305
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    0.0000027056364explicit E-S complexSubstrate
    CaMKII-thr286

    Product
    CaMKII***
        Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    2
  • tot_autonomous_
    CaMKII
      /
    auton_305
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    0.0000041666764explicit E-S complexSubstrate
    CaMKII-thr286

    Product
    CaMKII***
        See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation



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