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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_
    2007_Bistable
  • 79Network
    Shared_Object_Ajay_Bhalla_2007_Bistable PKC PLA2 
    MAPK Ras CaM 
    This is a model of ERKII signaling which is bistable due to feedback. The feedback occurs through ERKII phosphorylation of phospholipase A2 (PLA2), leading to increased production of arachidonic acid (AA), which activates protein kinase C (PKC) which activates c-Raf which is upstream of ERKII.
    The model is a highly simplified variant of more detailed bistable models of MAPK signaling (Bhalla US, Iyengar R. Science. 1999 Jan 15;283(5400):381-7, Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80)

    MKP-1 acting as a Molecule in  
    Ajay_Bhalla_2007_Bistable Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MKP-1
  • Ajay_Bhalla_
    2007_Bistable

    Accession No. : 79
  • Shared_Object_
    Ajay_Bhalla_
    2007_Bistable

    Pathway No. : 363
  • 0.024125.7No
    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_2007_Bistable Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-1 /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_Bistable

    Accession No. : 79
  • Shared_Object_
    Ajay_Bhalla_
    2007_Bistable

    Pathway No. : 363
  • 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_
    2007_Bistable

    Accession No. : 79
  • Shared_Object_
    Ajay_Bhalla_
    2007_Bistable

    Pathway No. : 363
  • 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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