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Molecule Parameter List for MKP-2

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-2 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
  • mkp1_feedback_
    effects
    		• 4Network
    Shared_Object_mkp1_feedback_effects,  Sos,  PKC,  
    MAPK,  PLA2,  Ras,  
    PDGFR 
    This is a network involving the MAPK-PKC feedback loop with input from the PDGFR in the synapse. The distinctive feature of this model is that it includes MKP-1 induction by MAPK, and the consequent inhibitory regulation of MAPK and the feedback loop. Lots of interesting dynamics arise from this. This link provides supplementary material for the paper Bhalla US et al. Science (2002) 297(5583):1018-23. In the form of several example simulations and demos for the figures in the paper.

    MKP-2 acting as a Molecule in      mkp1_feedback_effects Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    MKP-2
  • mkp1_feedback_
    effects
    Accession No. : 4
  • Shared_Object_
    mkp1_feedback_
    effects
    Pathway No. : 32
    		• 0.0021000No
    MKP2 is modeled to act as a relatively steady, unregulated phosphatase for controlling MAPK activity. From Brondello JM, Brunet A, Pouyssegur J, McKenzie FR (1997) J Biol Chem. 272(2):1368-1376, the blockage of MKP-1 induction increases MAPK activity by no more than 2x. So this phosphatase will play the steady role and the fully stimulated MKP-1 can come up to the level of this steady level. From Chu Y, Solski PA, Khosravi-Far R, Der CJ, Kelly K (1996) J Biol Chem. 271(11):6497-6501 it looks like both MKP-1 and MKP-2 have similar activities in dephosphorylating ERK2. So I use the same enzymatic rates for both.

    MKP-2 acting as an Enzyme in      mkp1_feedback_effects Network
     Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-2 /
    MKP2-tyr-deph
  • mkp1_feedback_
    effects
    Accession No. : 4
  • Shared_Object_
    mkp1_feedback_
    effects
    Pathway No. : 32
    		• 0.066666714explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        22 Apr 2001: Based on MKP1 parameters. The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. The only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. The rates are treated as the same as for MKP-1, based on Chu Y, Solski PA, Khosravi-Far R, Der CJ, Kelly K. (1996) J Biol Chem. 271(11):6497-6501.
    2MKP-2 /
    MKP2-thr-deph
  • mkp1_feedback_
    effects
    Accession No. : 4
  • Shared_Object_
    mkp1_feedback_
    effects
    Pathway No. : 32
    		• 0.066666714explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP2-tyr-deph


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