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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 occurrences1001100

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • MAPK_network_
    2003
  • 50Network
    Shared_Object_MAPK_network_2003 PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC 
    This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53

    MAPK acting as a Molecule in  
    MAPK_network_2003 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPK
  • MAPK_network_
    2003

    Accession No. : 50
  • MAPK
    Pathway No. : 211
    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_network_2003 Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    MAPKK*  /
    MAPKKtyr
  • MAPK_network_
    2003

    Accession No. : 50
  • MAPK
    Pathway No. : 211
    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_network_2003 Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    MKP-1  /
    MKP1-tyr-deph
  • MAPK_network_
    2003

    Accession No. : 50
  • Shared_Object_
    MAPK_network_
    2003

    Pathway No. : 206
  • 0.066666714explicit 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



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