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Molecule Parameter List for MAPK

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
MAPK participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • MAPK_MKP1_
    oscillation
    		• 9Network
    Shared_Object_MAPK_MKP1_oscillation,  PKC,  MAPK,  
    PLA2,  Ras 
    This model relates to figure 5 in Bhalla US, Iyengar R. Chaos (2001) 11(1):221-226. It includes the model used for figures 2-4 and also has MKP-1 induction by MAPK activity in the synapse. PP2A is set to 0.16 uM and MKP synthesis is varied from 5x to 40 x basal to get a range of interesting behaviours.

    MAPK acting as a Molecule in      MAPK_MKP1_oscillation Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    MAPK
  • MAPK_MKP1_
    oscillation
    Accession No. : 9
    		• MAPK
    Pathway No. : 61    		0.361000No
    conc is from Sanghera et al JBC 265 pp 52 (1990) A second calculation gives 3.1 uM, from same paper. They est MAPK is 1e-4x total protein, and protein is 15% of cell wt, so MAPK is 1.5e-5g/ml = 0.36uM. which is closer to our first estimate. Lets use this.

    MAPK acting as a Substrate for an Enzyme in      MAPK_MKP1_oscillation Network
    Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    MAPKK*  /
    MAPKKtyr
  • MAPK_MKP1_
    oscillation
    Accession No. : 9
    		• MAPK
    Pathway No. : 61    		0.04629630.154explicit E-S complexSubstrate
    MAPK

    Product
    MAPK-tyr
    The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5

    MAPK acting as a Product of an Enzyme in      MAPK_MKP1_oscillation Network
     Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-1**  /
    MKP1*-tyr-deph
  • MAPK_MKP1_
    oscillation
    Accession No. : 9
    		• MAPK
    Pathway No. : 61    		0.066666714Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S    		Substrate
    MAPK-tyr

    Product
    MAPK
        3 Feb 2000. Same rates as MKP-1.
    2MKP-1  /
    MKP1-tyr-deph
  • MAPK_MKP1_
    oscillation
    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation
    Pathway No. : 59
    		• 0.066666714Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S    		Substrate
    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


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