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Molecule Parameter List for PP1-active

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
PP1-active participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1050000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • NonOsc_Ca_
    IP3metabolism
  • 23Network
    MIPP CaMKII CaM 
    PKC IP3-3K CaRegulation 
    Gq PLCbeta 134_dephos 
    145_dephos IP4-system IHP-system 
    1345_dephos 
    This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. The calcium response is non-oscillatory. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

    PP1-active acting as a Molecule in  
    NonOsc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PP1-active
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    1.81000No
    Cohen et al Meth Enz 159 390-408 is main source of info concentration of enzyme = 1.8 uM

    PP1-active acting as an Enzyme in  
    NonOsc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP1-active /
    Deph-thr286
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    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. This gives the final Km of 5.1, and Vmax of 0.35/sec.
    2PP1-active /
    Deph-thr305
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    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.
    3PP1-active /
    Deph-thr306
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    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.
    4PP1-active /
    Deph-thr286c
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    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.
    5PP1-active /
    Deph_thr286b
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 23
  • CaMKII
    Pathway No. : 106
    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.



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