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Molecule Parameter List for ATP

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
ATP participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1002000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_traff_
    model0
  • 59Network
    Shared_Object_AMPAR_traff_model0 CaMKII CaM 
    PP1 PP2B PP1_PSD 
    PKA AC AMPAR 
    AMPAR_memb 
    This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno ver reactions for AMPAR.

    ATP acting as a Molecule in  
    AMPAR_traff_model0 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    ATP
  • AMPAR_traff_
    model0

    Accession No. : 59
  • AC
    Pathway No. : 241
    20000.09Yes
    ATP is present in all cells between 2 and 10 mM. See Lehninger

    ATP acting as a Substrate for an Enzyme in  
    AMPAR_traff_model0 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1AC1-CaM  /
    kenz
  • AMPAR_traff_
    model0

    Accession No. : 59
  • AC
    Pathway No. : 241
    299.9984.54Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    ATP

    Product
    cAMP
        17 Feb 2005 Halved Vmax as the amount of enzyme has been doubled to get an integer value in the spine. 18 Feb 2005. Updated Km from BRENDA: EC No 4.6.1.1 Rat Km: 0.95 mM Turnover 12/sec. Human Km: 0.3 mM 12 umol/min/mg for mammalia, turnover is 12/sec See PMID 8663304 by Dessauer and Gilman JBC 271 1996 Unfortunately turnover range is from 34 down to 0.1 in different studies, according to BRENDA.
    2AC2*  /
    kenz
  • AMPAR_traff_
    model0

    Accession No. : 59
  • AC
    Pathway No. : 241
    300.00224Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    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 18 Feb: Raised Km to 300 based on BRENDA data. Unlikely to make much difference, given the vast amount of ATP.



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