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Molecule Parameter List for MKP-3

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
MKP-3 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1020110

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning
  • 77Network
    Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning PKC PLA2 
    PLCbeta Ras Gq 
    MAPK EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC MKP3 PKM 
    This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a.

    MKP-3 acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MKP-3
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MKP3
    Pathway No. : 345
    0.021.5No
    MKP-3 dephosphoryates and inactivates MAPK in CA1 with a delay of under 30 min

    MKP-3 acting as an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-3 /
    MKP3-thr-deph
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MKP3
    Pathway No. : 345
    10.000144explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph Km is twice as high to avoid saturation.
    2MKP-3 /
    MKP3-tyr-deph
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MKP3
    Pathway No. : 345
    10.000144explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg Km for MKP3 is set to 267 nM, twice as high as MKP1 version, to lessen substrate saturation.

    MKP-3 acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    MKP3_synthesis  /
    kenz
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MKP3
    Pathway No. : 345
    0.1999980.014explicit E-S complexSubstrate
    MKP3_AA

    Product
    MKP-3

    MKP-3 acting as a Substrate in a reaction in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning 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
    MKP3-turnover
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MKP3
    Pathway No. : 345
    0.0005
    (s^-1)
    0
    (s^-1)
    --Substrate
    MKP-3

    Product
    ubiquitination



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