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Molecule Parameter List for Rec-Glu-Gq

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
Rec-Glu-Gq participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000012

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning
  • 78Network
    Shared_Object_Ajay_Bhalla_2004_Feedback_Tuning PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC 
    This model is taken from Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedback model from Figure 8a.

    Rec-Glu-Gq acting as a Molecule in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    Rec-Glu-Gq
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Gq
    Pathway No. : 351
    01.5No

    Rec-Glu-Gq acting as a Substrate in a reaction in  
    Ajay_Bhalla_2004_Feedback_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
    Activate-Gq
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Gq
    Pathway No. : 351
    0.01
    (s^-1)
    0
    (uM^-2 s^-1)
    --Substrate
    Rec-Glu-Gq

    Product
    BetaGamma
    G*GTP
    Rec-Glu
    This is the kcat==k3 stage of the Rec-Glu ezymatic activation of Gq. From Berstein et al actiation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec From Nakamura et al J physiol Lond 474:1 35-41 1994 see time courses. Also (Berstein) 15-40% of gprot is in GTP-bound form on stim.

    Rec-Glu-Gq acting as a Product in a reaction in  
    Ajay_Bhalla_2004_Feedback_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
    1Rec-Glu-bind-Gq
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Gq
    Pathway No. : 351
    0.006
    (uM^-1 s^-1)
    0.0001
    (s^-1)
    Kd(bf) = 0.0167(uM)-Substrate
    G-GDP
    Rec-Glu

    Product
    Rec-Glu-Gq
      This is the k1-k2 equivalent for enzyme complex formation in the binding of Rec-Glu to Gq. See Fay et al Biochem 30 5066-5075 1991. kf = 5e-5 which is nearly the same as calculated by Fay et al. (4.67e-5) kb = .04 June 1996: Closer reading of Fay et al suggests that kb <= 0.0001, so kf = 1e-8 by detailed balance. This reaction appears to be neglible.
    2Glu-bind-Rec-Gq
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Gq
    Pathway No. : 351
    16.8003
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.006(uM)-Substrate
    Glu
    Rec-Gq

    Product
    Rec-Glu-Gq
      From Fay et al kb3 = kb = 1.06e-3 which is rather slow. k+1 = kf = 2.8e7 /M/sec= 4.67e-5/sec use 5e-5. However, the Kd from Martin et al may be more appropriate, as this is Glu not the system from Fay. kf = 2.8e-5, kb = 10 Let us compromise. since we have the Fay model, keep kf = k+1 = 2.8e-5. But kb (k-3) is .01 * k-1 from Fay. Scaling by .01, kb = .01 * 10 = 0.1



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