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Molecule Parameter List for PIP2

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
PIP2 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1004000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_Tuning
  • 76Network
    PKC Shared_Object_Ajay_Bhalla_2004_PKM_tuning PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC PKM 
    This model is taken from the Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the reference feedforward model from Figure 8a.

    PIP2 acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PIP2
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_tuning

    Pathway No. : 312
  • 101.5Yes

    PIP2 acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PLC-Ca  /
    PLC-Ca
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLCbeta
    Pathway No. : 315
    19.8413104explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3
        From Sternweis et al Phil Trans R Soc Lond 1992, also matched by Homma et al. k1 = 1.5e-5, now 4.2e-6 k2 = 70/sec; now 40/sec k3 = 17.5/sec; now 10/sec Note that the wording in Sternweis et al is ambiguous re the Km.
    2PLC-Ca-Gq  /
    PLCb-Ca-Gq
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLCbeta
    Pathway No. : 315
    5.00003484explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3
        From Sternweis et al, Phil Trans R Soc Lond 1992, and the values from other refs eg Homma et al JBC 263(14) pp6592 1988 match. k1 = 5e-5/sec k2 = 240/sec; now 120/sec k3 = 60/sec; now 30/sec Note that the wording in Sternweis et al is ambiguous wr. to the Km for Gq vs non-Gq states of PLC. K1 is still a bit too low. Raise to 7e-5 9 Jun 1996: k1 was 0.0002, changed to 5e-5
    3Ca.PLC_g  /
    PIP2_hydrolysis
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLC_g
    Pathway No. : 321
    97.2222144explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3
        Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that the Ca_stim and phosph form has 7X higher affinity for substrate than control. This is close to Wahl's figure 7, which I am using as reference.
    4Ca.PLC_g*  /
    PIP2_hydrolysis
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLC_g
    Pathway No. : 321
    19.7917574explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3
        Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that this has 7X higher affinity for substrate than control.



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