NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

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
  • MAPK-bistability
    -fig1c
    		• 35Network
    Shared_Object_MAPK-bistability-fig1c,  Sos,  PKC,  
    MAPK,  PLA2,  Ras,  
    PDGFR 
    Model for figure 1c in Bhalla US et al. Science (2002) 297(5583):1018-23.
    The demo for this figure is available here. This synaptic signaling model is without the MKP-1 feedback, so it is bistable and remains so over long periods.

    MKP-2 acting as a Molecule in      MAPK-bistability-fig1c Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    MKP-2
  • MAPK-bistability
    -fig1c
    Accession No. : 35
  • Shared_Object_
    MAPK-bistability
    -fig1c
    Pathway No. : 179
    		• 0.00241000No
    MKP2 is modeled to act as a relatively steady, unregulated phosphatase for controlling MAPK activity. From Brondello et al JBC 272(2):1368-1376 (1997), 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 et al 1995 JBC 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. 31 Jan 2002: For the purposes of making a bistable model without the complications of MKP-1 induction, I simply set the initial conc of MKP-2 up by 0.0004 uM which was the starting level of MKP-1.

    MKP-2 acting as an Enzyme in      MAPK-bistability-fig1c Network
     Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-2 /
    MKP2-tyr-deph
  • MAPK-bistability
    -fig1c
    Accession No. : 35
  • Shared_Object_
    MAPK-bistability
    -fig1c
    Pathway No. : 179
    		• 0.066666714explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        22 Apr 2001: Based on MKP1 parms. 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 et al 1995 JBC 271(11):6497-6501
    2MKP-2 /
    MKP2-thr-deph
  • MAPK-bistability
    -fig1c
    Accession No. : 35
  • Shared_Object_
    MAPK-bistability
    -fig1c
    Pathway No. : 179
    		• 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
    This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.