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Molecule Parameter List for Ca.PLC_g

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
Ca.PLC_g participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1011002

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.

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

    Accession No. : 76
  • PLC_g
    Pathway No. : 321
    01.5No

    Ca.PLC_g acting as an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    Ca.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.

    Ca.PLC_g 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
    L.EGFR  /
    phosph_PLC_g
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • EGFR
    Pathway No. : 319
    0.3333370.24explicit E-S complexSubstrate
    Ca.PLC_g

    Product
    Ca.PLC_g*
    Hsu et al JBC 266:1 603-608 1991 Km = 385 +- 100 uM, Vm = 5.1 +-1 pmol/min/ug for PLC-771. Other sites have similar range, but are not stim as much by EGF. k1 = 2.8e-2/385/6e5 = 1.2e-10. Phenomenally slow. But Sherrill and Kyte say turnover # for angiotensin II is 5/min for cell extt, and 2/min for placental. Also see Okada et al for Shc rates which are much faster.

    Ca.PLC_g acting as a Product in a reaction in  
    Ajay_Bhalla_2004_PKM_Tuning 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
    1Ca_act_PLC_g
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLC_g
    Pathway No. : 321
    180
    (uM^-1 s^-1)
    10
    (s^-1)
    Kd(bf) = 0.0556(uM)-Substrate
    Ca
    PLC_g

    Product
    Ca.PLC_g
      Nice curves from Homma et al JBC 263:14 6592-6598 1988 Fig 5c. The activity falls above 10 uM, but that is too high to reach physiologically anyway, so we'll ignore the higher pts and match the lower ones only. Half-max at 1 uM. But Wahl et al JBC 267:15 10447-10456 1992 have half-max at 56 nM which is what I'll use.
    2dephosph_PLC_g
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PLC_g
    Pathway No. : 321
    0.05
    (s^-1)
    0
    (s^-1)
    --Substrate
    Ca.PLC_g*

    Product
    Ca.PLC_g



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