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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 occurrences1000212

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
    8-10 fold activation with both CaM bound and CaMKII phosphorylation (phos at thr311) Communi et al; EMBO J 16 (8), pp 1943-1952, 1997

    IP3_3K_CaM* acting as a Product of 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
    80.358
    (uM^-1 s^-1)
    180
    (s^-1)
    Kd(bf) = 2.24(uM)-Substrate
    IP3(145)
    IP3_3K_CaM*

    Product
  • 3kCaM*_ip3_
    cmplx

  • Rates from Km of enzyme Communi et al, EMBO J 16(8)

    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
    49.9998
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.002(uM)-Substrate
    CaM-Ca4
    IP3_3K*

    Product
    IP3_3K_CaM*
      Communi et al, EMBO J 16; 1997 phosphorylated 3kinase has 25 fold greater sensitivity to CaM binding than the non-phosphorylated enzyme (Kd of 2nM)
    23k-CaM*-off
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • IP3-3K
    Pathway No. : 148
    45
    (s^-1)
    0.4148
    (uM^-1 s^-1)
    Kd(cb) = 0.0092(uM)-Substrate
  • 3kCaM*_ip3_
    cmplx


    Product
    IP3_3K_CaM*
    IP4(1345)
  •   Kf = Vmax for enzyme (Communi et al, EMBO J 16(8)) Vmax is such that enzyme activity is 9 fold above basal. Kb derived from Keq value when reaction free energy = -10 kJ/mol



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