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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



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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