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Molecule Parameter List for PP-IP5

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
PP-IP5 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001211

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.

    PP-IP5 acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PP-IP5
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    21000No
    Diphosphoinositol pentakisphosphate Conc from Huang et al, Biochem 37; 1998

    PP-IP5 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
    DIPP1  /
    dipp_ip7
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    0.3400065.14explicit E-S complexSubstrate
    PP-IP5

    Product
    IP6
    from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of recombinant human protein which is 20-50 fold greater than activity of the purified rat enzyme

    PP-IP5 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
    1IP6_K2  /
    ip6_k2
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    2.999991.6334explicit E-S complexSubstrate
    IP6

    Product
    PP-IP5
        from Saiardi et al, Curr Biol 9; 1999
    2DIPP1  /
    dipp_ip8
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    0.03400350.61654explicit E-S complexSubstrate
    bisPP-IP4

    Product
    PP-IP5
        from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of human recombinant protein, which is 20-50 fold greater than activity of the purified rat enzyme

    PP-IP5 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
    PP-IP5cmplx-on
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    0.0027
    (uM^-2 s^-1)
    2.5
    (s^-1)
    --Substrate
    ATP
    PP-IP5
    PP-IP5-K

    Product
  • PP-IP5-K-complex
  • from Huang et al, Biochem 37; 1998 Kf calculated using Km for PP-InsP5 and ATP, and Vmax of forward and backward reactions. Kb = Vmax of backward reaction

    PP-IP5 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
    IP6cmplx-off
  • Osc_Ca_
    IP3metabolism

    Accession No. : 24
  • IHP-system
    Pathway No. : 130
    1.26
    (s^-1)
    0.0012
    (uM^-2 s^-1)
    --Substrate
    IP6-K-complex

    Product
    ADP
    IP6-K
    PP-IP5
    from Voglmaier et al, PNAS 93; 1996 Kf = Vmax of forward reaction Kb calculated from Km for InsP6 and ATP, and Vmax of forward and backward reactions