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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 occurrences1010111

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning
  • 77Network
    Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning PKC PLA2 
    PLCbeta Ras Gq 
    MAPK EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC MKP3 PKM 
    This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a.

    Ca.PLC_g* acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    Ca.PLC_g*
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • PLC_g
    Pathway No. : 338
    01.5No

    Ca.PLC_g* acting as an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    Ca.PLC_g* /
    PIP2_hydrolysis
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • PLC_g
    Pathway No. : 338
    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.

    Ca.PLC_g* acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    L.EGFR  /
    phosph_PLC_g
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • EGFR
    Pathway No. : 336
    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 Substrate in a reaction in  
    Ajay_Bhalla_2004_PKM_MKP3_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
    dephosph_PLC_g
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • PLC_g
    Pathway No. : 338
    0.05
    (s^-1)
    0
    (s^-1)
    --Substrate
    Ca.PLC_g*

    Product
    Ca.PLC_g

    Ca.PLC_g* acting as a Product in a reaction in  
    Ajay_Bhalla_2004_PKM_MKP3_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
    Ca_act_PLC_g*
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • PLC_g
    Pathway No. : 338
    11.9997
    (uM^-1 s^-1)
    10
    (s^-1)
    Kd(bf) = 0.8334(uM)-Substrate
    Ca
    PLC_G*

    Product
    Ca.PLC_g*
    Again, we refer to Homma et al and Wahl et al, for preference using Wahl. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. Did some curve comparisons, and instead of 316 nM giving a kf of 5.27e-5, we will use 8e-5 for kf. 16 Sep 97. As we are now phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 to match the curves.



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