NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

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_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.

    I1 acting as a Molecule in  
    AMPAR_traff_model0 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    I1
  • AMPAR_traff_
    model0

    Accession No. : 59
  • PP1
    Pathway No. : 237
    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_traff_
    model0

    Accession No. : 59
  • PP1_PSD
    Pathway No. : 239
    40.01No
    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_traff_model0 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PKA-active  /
    PKA-phosph-I1
  • AMPAR_traff_
    model0

    Accession No. : 59
  • PKA
    Pathway No. : 240
    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_
    model0

    Accession No. : 59
  • PKA
    Pathway No. : 240
    7.5000894explicit E-S complexSubstrate
    I1

    Product
    I1*

    I1 acting as a Product of an Enzyme in  
    AMPAR_traff_model0 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP2A  /
  • PP2A-dephosph-I1
  • AMPAR_traff_
    model0

    Accession No. : 59
  • PP1
    Pathway No. : 237
    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_
    model0

    Accession No. : 59
  • PP1
    Pathway No. : 237
    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_
    model0

    Accession No. : 59
  • PP2B
    Pathway No. : 238
    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_
    model0

    Accession No. : 59
  • PP2B
    Pathway No. : 238
    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_
    model0

    Accession No. : 59
  • PP2B
    Pathway No. : 238
    4.970790.344explicit E-S complexSubstrate
    I1*

    Product
    I1
    6CaM_Ca_n-CaNAB  /
  • dephosph_
    inhib1_PSD
  • AMPAR_traff_
    model0

    Accession No. : 59
  • PP2B
    Pathway No. : 238
    4.970710.344explicit E-S complexSubstrate
    I1*

    Product
    I1

    I1 acting as a Product in a reaction in  
    AMPAR_traff_model0 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_traff_
    model0

    Accession No. : 59
  • PP1
    Pathway No. : 237
    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_traff_
    model0

    Accession No. : 59
  • PP1_PSD
    Pathway No. : 239
    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.



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
    This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.