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Molecule Parameter List for CaMK-thr306

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
CaMK-thr306 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001100

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Osc_Ca_
    IP3metabolism
  • 32Network
    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 is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    CaMK-thr306 acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    CaMK-thr306
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    01000No
    This forms due to basal autophosphorylation, but I think it has to be considered as a pathway even if some CaM is floating around. In either case it will tend to block further binding of CaM, and will not display any enzyme activity. See Hanson and Schulman JBC 267:24 pp17216-17224 1992

    CaMK-thr306 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
    PP1-active  /
    Deph-thr306
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    5.099070.354explicit E-S complexSubstrate
    CaMK-thr306

    Product
    CaMKII
    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.

    CaMK-thr306 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-thr286c
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • CaMKII
    Pathway No. : 159
    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.



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