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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 occurrences1003110

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
CaMKII_200349Network
Shared_Object_CaMKII_2003 CaMKII CaM 
PP1 PP2B 
Model of regulation of CaMKII by Calcium, including parallel excitatory input from CaM and inhibitory input from PP1 as regulated by Calcineurin and PKA. Cell type: neuronal.
Bhalla US. Biophys J. 2004 Aug;87(2):733-44.

I1* acting as a Molecule in  
CaMKII_2003 Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
I1*CaMKII_2003
Accession No. : 49
PP1
Pathway No. : 204
0.0011000No
Dephosph is mainly by PP2B

I1* acting as a Substrate for an Enzyme in  
CaMKII_2003 Network
 Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
1CaM(Ca)n-CaNAB  /
dephosph_inhib1
CaMKII_2003
Accession No. : 49
  • Shared_Object_
    CaMKII_2003

    Pathway No. : 201
  • 4.970760.344explicit E-S complexSubstrate
    I1*

    Product
    I1
    2PP2A  /
  • PP2A-dephosph-I1
  • CaMKII_2003
    Accession No. : 49
  • Shared_Object_
    CaMKII_2003

    Pathway No. : 201
  • 7.8282864.16667explicit 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
  • CaMKII_2003
    Accession No. : 49
  • Shared_Object_
    CaMKII_2003

    Pathway No. : 201
  • 4.970760.0344explicit 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

    I1* acting as a Product of an Enzyme in  
    CaMKII_2003 Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKA-active  /
    PKA-phosph-I1
    CaMKII_2003
    Accession No. : 49
  • Shared_Object_
    CaMKII_2003

    Pathway No. : 201
  • 7.594explicit 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.

    I1* acting as a Substrate in a reaction in  
    CaMKII_2003 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
    Inact-PP1CaMKII_2003
    Accession No. : 49
    PP1
    Pathway No. : 204
    499.98
    (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



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