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Molecule Parameter List for DAG

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
DAG participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000431

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • NonOsc_Ca_
    IP3metabolism
  • 31Network
    MIPP CaMKII CaM 
    PKC IP3-3K CaRegulation 
    Gq PLCbeta 134_dephos 
    145_dephos IP4-system IHP-system 
    1345_dephos 
    This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. It is similar to the NonOsc_Ca_IP3metab model (accession 23) except that some enzymes have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. These 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.

    DAG acting as a Molecule in  
    NonOsc_Ca_IP3metabolism Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    DAG
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    01000No
    Basal levels of Diacylglycerol in model are 5.06 uM. DAG is pretty nasty to estimate. Data sources are many and varied and sometimes difficult to reconcile. Welsh and Cabot 1987 JCB 35:231-245: DAG degradation Bocckino et al JBC 260(26):14201-14207: hepatocytes stim with vasopressin: 190 uM. Bocckino et al 1987 JBC 262(31):15309-15315: DAG rises from 70 to 200 ng/mg wet weight, approx 150 to 450 uM. Prescott and Majerus 1983 JBC 258:764-769: Platelets: 6 uM. Also see Rittenhouse-Simmons 1979 J Clin Invest 63. Sano et al JBC 258(3):2010-2013: Report a nearly 10 fold rise. Habenicht et al 1981 JBC 256(23)12329-12335: 3T3 cells with PDGF stim: 27 uM Cornell and Vance 1987 BBA 919:23-36: 10x rise from 10 to 100 uM

    DAG acting as a Product of an Enzyme in  
    NonOsc_Ca_IP3metabolism Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PLC-Gq  /
    PLC-Gq
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    5754explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3(145)
        from Smrcka et al, 1991 Science 251: 804-807
    2PLC-Ca  /
    PLC-Ca
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    19.8408104explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3(145)
        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. Also Smrcka et al; Science 251, 15.2.1991, pp804-807
    3PLC-Ca-Gq  /
    PLCb-Ca-Gq
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    4.999941604explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3(145)
        Km: Sternweis et al, Phil Trans R Soc Lond 1992 Vmax: Smrcka et al, Science 1991
    4PLC  /
    PLC
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    19.99942.54explicit E-S complexSubstrate
    PIP2

    Product
    DAG
    IP3(145)
        Smrcka et al; Science 251, 15.2.1991, pp804-807

    DAG acting as a Substrate in a reaction in  
    NonOsc_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
    1PKC-act-by-DAG
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PKC
    Pathway No. : 147
    0.008
    (uM^-1 s^-1)
    8.6348
    (s^-1)
    Kd(bf) = 1079.377(uM)-Substrate
    DAG
    PKC-Ca

    Product
    PKC-Ca-DAG
      Ca.PKC interaction with DAG is modeled by this reaction. Kf based on Shinomura et al PNAS 88 5149-5153 1991 and Schaechter and Benowitz 1993 J Neurosci 13(10):4361 and uses the constraining procedure referred to in the general notes for PKC.
    2PKC-n-DAG
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PKC
    Pathway No. : 147
    0.0006
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 166.6667(uM)-Substrate
    DAG
    PKC-cytosolic

    Product
    PKC-DAG
      Binding of PKC to DAG, non-Ca dependent. Kf based on Shinomura et al PNAS 88 5149-5153 1991 Tau estimated as fast and here it is about the same time-course as the formation of DAG so it will not be rate-limiting.
    3Degrade-DAG
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    0.15
    (s^-1)
    0
    (s^-1)
    --Substrate
    DAG

    Product
    PC
      Rate based on basal and activated levels of DAG

    DAG acting as a Product in a reaction in  
    NonOsc_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
    basal
  • NonOsc_Ca_
    IP3metabolism

    Accession No. : 31
  • PLCbeta
    Pathway No. : 151
    0.003
    (s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    PIP2

    Product
    DAG
    IP3(145)
    accounts for other PLC isoforms that contribute to basal levels of IP3



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