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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 occurrences2002602

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • AMPAR_CaMKII_
    strong_coupling
  • 64Network
    Shared_Object_AMPAR_CaMKII_strong_coupling CaMKII CaM 
    PP1 AMPAR_memb PP2B 
    PKA AC PP1_PSD 
    AMPAR 
    This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on.

    I1 acting as a Molecule in  
    AMPAR_CaMKII_strong_coupling Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PP1
    Pathway No. : 274
    1.80.09No
    I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-compet, so it just turns the enz off without interacting with the binding site. Cohen et al ann rev bioch refer to results where conc is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM.
    I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PP1_PSD
    Pathway No. : 279
    80.01No
    I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-compet, so it just turns the enz off without interacting with the binding site. Cohen et al ann rev bioch refer to results where conc is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM.

    I1 acting as a Substrate for an Enzyme in  
    AMPAR_CaMKII_strong_coupling Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PKA-active  /
    PKA-phosph-I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 7.5000894explicit E-S complexSubstrate
    I1

    Product
    I1*

    I1 acting as a Product of an Enzyme in  
    AMPAR_CaMKII_strong_coupling Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP2A  /
  • PP2A-dephosph-I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 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_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 4.970790.344explicit E-S complexSubstrate
    I1*

    Product
    I1
    6CaM_Ca_n-CaNAB  /
  • dephosph_
    inhib1_PSD
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • Shared_Object_
    AMPAR_CaMKII_
    strong_coupling

    Pathway No. : 271
  • 4.970710.344explicit E-S complexSubstrate
    I1*

    Product
    I1

    I1 acting as a Product in a reaction in  
    AMPAR_CaMKII_strong_coupling 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
    1dissoc-PP1-I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PP1
    Pathway No. : 274
    1
    (s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    PP1-I1

    Product
    I1
    PP1-active
      Let us assume that the equil in this case is very far over to the right. This is probably safe.
    2dissoc-PP1-I1
  • AMPAR_CaMKII_
    strong_coupling

    Accession No. : 64
  • PP1_PSD
    Pathway No. : 279
    1
    (s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    PP1-I1

    Product
    I1
    PP1-active_PSD
      Let us assume that the equil in this case is very far over to the right. This is probably safe.



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