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Molecule Parameter List for cAMP

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
cAMP participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1004540

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.

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

    Accession No. : 76
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_tuning

    Pathway No. : 312
  • 01.5No
    The conc of this has been a problem. Schaecter and Benowitz use 50 uM, but Shinomura et al have < 5. So I have altered the cAMP-dependent rates in the PKA model to reflect this.

    cAMP 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
    1cAMP-PDE  /
    PDE
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    19.8413104explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        Best rates are from Conti et al Biochem 34 7979-7987 1995. Though these are for the Sertoli cell form, it looks like they carry nicely into alternatively spliced brain form. See Sette et al JBC 269:28 18271-18274 Km ~2 uM, Vmax est ~ 10 umol/min/mg for pure form. Brain protein is 93 kD but this was 67. So k3 ~10, k2 ~40, k1 ~4.2e-6
    2cAMP-PDE*  /
    PDE*
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    19.8413204explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        This form has about twice the activity of the unphosphorylated form. See Sette et al JBC 269:28 18271-18274 1994. We'll ignore cGMP effects for now.
    3PDE1  /
    PDE1
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    39.70061.6674.0012explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        Rate is 1/6 of the CaM stim form. We'll just reduce all lf k1, k2, k3 so that the Vmax goes down 1/6.
    4CaM.PDE1  /
    CaM.PDE1
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    39.6825104explicit E-S complexSubstrate
    cAMP

    Product
    AMP
        Max activity ~10umol/min/mg in presence of lots of CaM. Affinity is low, 40 uM. k3 = 10, k2 = 40, k1 = (50/40) / 6e5.

    cAMP acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1AC1-CaM  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    20184explicit E-S complexSubstrate
    ATP

    Product
    cAMP
       
    2AC2*  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    20.115374explicit E-S complexSubstrate
    ATP

    Product
    cAMP
        Reduced Km to match expt data for basal activation of AC2 by PKC. Now k1 = 2.9e-6, k2 = 72, k3 = 18
    3AC2-Gs  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    20184explicit E-S complexSubstrate
    ATP

    Product
    cAMP
       
    4AC1-Gs  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    20184explicit E-S complexSubstrate
    ATP

    Product
    cAMP
       
    5AC2*-Gs  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • AC
    Pathway No. : 327
    60544explicit E-S complexSubstrate
    ATP

    Product
    cAMP
       

    cAMP acting as a Substrate 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
    1
  • cAMP-bind-site-B
    1
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PKA
    Pathway No. : 326
    54
    (uM^-1 s^-1)
    33
    (s^-1)
    Kd(bf) = 0.6111(uM)-Substrate
    R2C2
    cAMP

    Product
    R2C2-cAMP
      Hasler et al FASEB J 6:2734-2741 1992 say Kd =1e-7M for type II, 5.6e-8 M for type I. Take mean which comes to 2e-13 #/cell Smith et al PNAS USA 78:3 1591-1595 1981 have better data. First kf/kb=2.1e7/M = 3.5e-5 (#/cell). Ogreid and Doskeland Febs Lett 129:2 287-292 1981 have figs suggesting time course of complete assoc is < 1 min.
    2
  • cAMP-bind-site-B
    2
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PKA
    Pathway No. : 326
    54
    (uM^-1 s^-1)
    33
    (s^-1)
    Kd(bf) = 0.6111(uM)-Substrate
    R2C2-cAMP
    cAMP

    Product
    R2C2-cAMP2
      For now let us set this to the same Km (1e-7M) as site B. This gives kf/kb = .7e-7M * 1e6 / (6e5^2) : 1/(6e5^2) = 2e-13:2.77e-12 Smith et al have better values. They say that this is cooperative, so the consts are now kf/kb =8.3e-4
    3
  • cAMP-bind-site-A
    1
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PKA
    Pathway No. : 326
    74.9997
    (uM^-1 s^-1)
    110
    (s^-1)
    Kd(bf) = 1.4667(uM)-Substrate
    R2C2-cAMP2
    cAMP

    Product
    R2C2-cAMP3
    4
  • cAMP-bind-site-A
    2
  • Ajay_Bhalla_
    2004_PKM_Tuning

    Accession No. : 76
  • PKA
    Pathway No. : 326
    74.9997
    (uM^-1 s^-1)
    32.5
    (s^-1)
    Kd(bf) = 0.4333(uM)-Substrate
    R2C2-cAMP3
    cAMP

    Product
    R2C2-cAMP4



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