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Molecule Parameter List for CaMKII-thr286

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 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1103111

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-thr286 acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMKII-thr286
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    01000No
    The threonine-286 phosphorylated form of CaMKII. It is likely to be a short-lived intermediate, since it will be phosphorylated further as soon as the CAM falls off.

    CaMKII-thr286 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-thr286 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
    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
    3PP1-active  /
    Deph_thr286b
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    5.099070.354explicit E-S complexSubstrate
    CaMKII-thr286

    Product
    CaMKII
        Rates 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-thr286 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
    PP1-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.

    CaMKII-thr286 acting as a Substrate in a reaction in  
    Osc_Ca_IP3metabolism 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
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    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 over the unphosphorylated CaMKII, which makes the Kd of 0.1 nM. See Hanson et al 1994 Neuron 12:943-956. Time to release is about 20 sec, so the kb is OK at 0.1/sec. as tested by a few runs.

    CaMKII-thr286 acting as a Product in a reaction in  
    Osc_Ca_IP3metabolism 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
    basal-activity
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • CaMKII
    Pathway No. : 121
    0.003
    (s^-1)
    0
    (s^-1)
    --Substrate
    CaMKII

    Product
    CaMKII-thr286
    This reaction represents one of the unknowns in CaMK-II biochemistry: what maintains the basal level of phosphorylation on thr 286 ? See Hanson and Schulman Ann Rev Biochem 1992 61:559-601, specially pg 580, for review. I have not been able to find any compelling mechanism in the literature, but fortunately the level of basal activity is well documented. Lisman et al propose that the levels of PP1 are very low in the postsynaptic density, and PP2A is excluded from the PSD, and this would lead to autophosphorylation at a sustained level.



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