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Molecule Parameter List for Rec-Glu

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 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
  • Osc_Ca_
    IP3metabolism
  • 32Network
    MIPP CaMKII CaM 
    PKC IP3-3K Gq 
    PLCbeta 134_dephos 145_dephos 
    IP4-system IHP-system 1345_dephos 
    CaRegulation Othmer-Tang-model 
    This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The 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.

    Rec-Glu acting as a Molecule in  
    Osc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    Rec-Glu
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • Gq
    Pathway No. : 163
    01000No
    Glu-Receptor complex.

    Rec-Glu acting as a Substrate in a reaction in  
    Osc_Ca_IP3metabolism 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
    Rec-Glu-bind-Gq
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • Gq
    Pathway No. : 163
    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. Closer reading of Fay et al suggests that kb <= 0.0001, so kf = 1e-8 by detailed balance. This reaction appears to be neglible.

    Rec-Glu acting as a Product in a reaction in  
    Osc_Ca_IP3metabolism 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
    1
  • RecLigandBinding
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • Gq
    Pathway No. : 163
    16.8
    (uM^-1 s^-1)
    10
    (s^-1)
    Kd(bf) = 0.5952(uM)-Substrate
    Glu
    mGluR

    Product
    Rec-Glu
      From Martin et al FEBS Lett 316:2 191-196 1993 we have Kd = 600 nM Assuming kb = 10/sec, we get kf = 10/(0.6 uM * 6e5) = 2.8e-5 1/sec/# The off time for Glu seems pretty slow: Nicoletti et al 1986 PNAS 83:1931-1935 and Schoepp and Johnson 1989 J Neurochem 53 1865-1870 indicate it is at least 30 sec. Here we are a little faster because this is only a small part of the off rate, the rest coming from the Rec-Gq complex.
    2Activate-Gq
  • Osc_Ca_
    IP3metabolism

    Accession No. : 32
  • Gq
    Pathway No. : 163
    0.01
    (s^-1)
    0
    (uM^-2 s^-1)
    --Substrate
    Rec-Glu-Gq

    Product
    BetaGamma
    G*GTP
    Rec-Glu
      This reaction is the critical one for activation of Gq. It probably encapsulates multiple steps. In this approximation the receptor-ligand- Gprotein complex splits up into GTP.Galpha, rec.ligand complex, and Gbetagamma. There is a hidden step of exchange of GDP for GTP. The reaction does not take these into account since it is assumed that both GTP and GDP levels are tightly regulated by metabolic control. 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.



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