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Molecule Parameter List for IP2_3pase1

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
IP2_3pase1 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1010000

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.

    IP2_3pase1 acting as a Molecule in  
    NonOsc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    IP2_3pase1
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • 134_dephos
    Pathway No. : 152
    0.00381000No
    from Caldwell et al, JBC 266(27); 1991: 18378-86 Enzyme is a homodimer with two catalytic subunits. Conc of enzyme increased 2 times from 1.9 nM to account for two monomeric subunit pools

    IP2_3pase1 acting as an Enzyme in  
    NonOsc_Ca_IP3metabolism Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    IP2_3pase1 /
    ip2_3pase1
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • 134_dephos
    Pathway No. : 152
    0.799992117.334explicit E-S complexSubstrate
    IP2(13)

    Product
    IP1(1)
    from Caldwell et al, JBC 266; 1991 enzyme activity was assayed for the monomeric form of the enzyme



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