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Molecule Parameter List for IP3_3K_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
IP3_3K_CaM participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1002012

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • NonOsc_Ca_
    IP3metabolism
  • 31Network
    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. It is similar to the NonOsc_Ca_IP3metab model (accession 23) except that some enzymes have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. These 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.

    IP3_3K_CaM acting as a Molecule in  
    NonOsc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    IP3_3K_CaM
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • IP3-3K
    Pathway No. : 148
    01000No
    2-2.5 fold increase in enzyme activity due to CaM binding CaM binding involves Trp165 Erneux et al; Biochem 214, 497-501 (1993)

    IP3_3K_CaM acting as a Substrate for an Enzyme in  
    NonOsc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1tot_CaM_CaMKII  /
    CaM-CaMK-phos1
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • CaMKII
    Pathway No. : 145
    1.599980.54explicit E-S complexSubstrate
    IP3_3K_CaM

    Product
    IP3_3K_CaM*
        rates referred from standard CaM-CaMKII phosphorylation rates
    2
  • tot_autonomous_
    CaMKII
      /
    CaMK-phos1
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • CaMKII
    Pathway No. : 145
    2.499950.54explicit E-S complexSubstrate
    IP3_3K_CaM

    Product
    IP3_3K_CaM*
        rates referred from standard CaMKII phosphorylation rates

    IP3_3K_CaM acting as a Substrate in a reaction in  
    NonOsc_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
    3k-CaM-on
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • IP3-3K
    Pathway No. : 148
    18.7497
    (uM^-1 s^-1)
    42.001
    (s^-1)
    Kd(bf) = 2.2401(uM)-Substrate
    IP3(145)
    IP3_3K_CaM

    Product
    3kCaM_ip3_cmplx
    rates from Km for enzyme: Erneux et al, Biochem 214; 1993 Enzyme is 2-2.5 fold more active than ip3-3k, but Km is doubled.

    IP3_3K_CaM acting as a Product in a reaction in  
    NonOsc_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
    13K-bind-CaM
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • IP3-3K
    Pathway No. : 148
    19.2312
    (uM^-1 s^-1)
    1
    (s^-1)
    Kd(bf) = 0.052(uM)-Substrate
    CaM-Ca4
    IP3_3K

    Product
    IP3_3K_CaM
      Communi et al, EMBO J 16; 1997 non-phosphorylated 3kinase with low sensitivity to CaM binding (Kd = 52nM)
    23k-CaM-off
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • IP3-3K
    Pathway No. : 148
    10.5
    (s^-1)
    0.0968
    (uM^-1 s^-1)
    Kd(cb) = 0.0092(uM)-Substrate
    3kCaM_ip3_cmplx

    Product
    IP3_3K_CaM
    IP4(1345)
      Kf = Vmax for enzyme: Erneux et al, Biochem 214; 1993 Enzyme is 2-2.5 fold more active than basal enzyme. Kb derived from equilibrium conditions for dG = -10 kJ/mol



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