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Molecule Parameter List for PKC-active

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
PKC-active participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1130000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2007_PKM
  • 80Network
    Shared_Object_Ajay_Bhalla_2007_PKM PKC MAPK 
    Ras CaM PKM 
    This is a non-bistable model of ERKII signaling that also incorporates PKM synthesis triggered by Ca influx. It is a simplified variant of the model of Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80.

    PKC-active acting as a Molecule in  
    Ajay_Bhalla_2007_PKM Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PKC-active
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 01.5No

    PKC-active acting as a Summed Molecule in  
    Ajay_Bhalla_2007_PKM Network
    Accession NamePathway NameTargetInput
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • PKC-activePKC-Ca-memb*
    PKC-DAG-memb*
    PKM-zeta

    PKC-active acting as an Enzyme in  
    Ajay_Bhalla_2007_PKM Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PKC-active /
    PKC-act-raf
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 20.000144explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    2PKC-active /
    PKC-inact-GAP
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 3.3333144explicit E-S complexSubstrate
    GAP

    Product
    GAP*
        Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review.
    3PKC-active /
    PKC-act-GEF
  • Ajay_Bhalla_
    2007_PKM

    Accession No. : 80
  • Shared_Object_
    Ajay_Bhalla_
    2007_PKM

    Pathway No. : 369
  • 3.3333144explicit E-S complexSubstrate
    inact-GEF

    Product
    GEF*
        Rate consts from PKC-act-raf. This reaction activates GEF. It can lead to at least 2X stim of ras, and a 2X stim of MAPK over and above that obtained via direct phosph of c-raf. Note that it is a push-pull reaction, and there is also a contribution through the phosphorylation and inactivation of GAPs. The original PKC-act-raf rate consts are too fast. We lower K1 by 10 X



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