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Molecule Parameter List for I1*

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
I1* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences2006220

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_traff_
    model1
  • 60Network
    Shared_Object_AMPAR_traff_model1 CaMKII CaM 
    PP1 PP2B PP1_PSD 
    PKA AC AMPAR 
    AMPAR_memb 
    This is the basic model of AMPAR trafficking bistability. It is based on Hayer and Bhalla, PLoS Comput. Biol. 2005. It includes the degradation and turnover of AMPARs. The CaMKII portion of the model is not bistable.

    I1* acting as a Molecule in  
    AMPAR_traff_model1 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    I1*
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1
    Pathway No. : 247
    00.09No
    Dephosph is mainly by PP2B
    I1*
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1_PSD
    Pathway No. : 249
    00.01No
    Dephosph is mainly by PP2B

    I1* acting as a Substrate for an Enzyme in  
    AMPAR_traff_model1 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP2A  /
  • PP2A-dephosph-I1
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1
    Pathway No. : 247
    15.999924.1667explicit E-S complexSubstrate
    I1*

    Product
    I1
        PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6
    2PP2A  /

  • PP2A-dephosph-I1
    _
    PSD
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1
    Pathway No. : 247
    15.999924.1667explicit E-S complexSubstrate
    I1*

    Product
    I1
        PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6
    3CaNAB-Ca4  /
  • dephosph_
    inhib1_noCaM
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP2B
    Pathway No. : 248
    4.970790.0344explicit E-S complexSubstrate
    I1*

    Product
    I1
        The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034
    4CaNAB-Ca4  /
  • dephosph_
    inhib1_noCaM_
    PSD
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP2B
    Pathway No. : 248
    4.970710.0344explicit E-S complexSubstrate
    I1*

    Product
    I1
        The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034
    5CaM_Ca_n-CaNAB  /
    dephosph_inhib1
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP2B
    Pathway No. : 248
    4.970790.344explicit E-S complexSubstrate
    I1*

    Product
    I1
    6CaM_Ca_n-CaNAB  /
  • dephosph_
    inhib1_PSD
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP2B
    Pathway No. : 248
    4.970710.344explicit E-S complexSubstrate
    I1*

    Product
    I1

    I1* acting as a Product of an Enzyme in  
    AMPAR_traff_model1 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PKA-active  /
    PKA-phosph-I1
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PKA
    Pathway No. : 250
    7.5000894explicit E-S complexSubstrate
    I1

    Product
    I1*
        #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta.
    2PKA-active  /
  • PKA-phosph-I1_
    PSD
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PKA
    Pathway No. : 250
    7.5000894explicit E-S complexSubstrate
    I1

    Product
    I1*

    I1* acting as a Substrate in a reaction in  
    AMPAR_traff_model1 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
    1Inact-PP1
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1
    Pathway No. : 247
    499.981
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.0002(uM)-Substrate
    I1*
    PP1-active

    Product
    PP1-I1*
      K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4
    2Inact-PP1
  • AMPAR_traff_
    model1

    Accession No. : 60
  • PP1_PSD
    Pathway No. : 249
    499.98
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.0002(uM)-Substrate
    I1*
    PP1-active_PSD

    Product
    PP1-I1*
      K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4



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