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Molecule Parameter List for MKP-1

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-1 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1020000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning
  • 78Network
    Shared_Object_Ajay_Bhalla_2004_Feedback_Tuning PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC 
    This model is taken from Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedback model from Figure 8a.

    MKP-1 acting as a Molecule in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MKP-1
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Shared_Object_
    Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Pathway No. : 347
  • 0.0241.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.

    MKP-1 acting as an Enzyme in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-1 /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Shared_Object_
    Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Pathway No. : 347
  • 0.13333144explicit 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
    2MKP-1 /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Shared_Object_
    Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Pathway No. : 347
  • 0.13333144explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph



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