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Molecule Parameter List for MAPK-tyr

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-tyr participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1002200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning
  • 78Network
    Shared_Object_Ajay_Bhalla_2004_Feedback_Tuning PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC 
    This model is taken from Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedback model from Figure 8a.

    MAPK-tyr acting as a Molecule in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPK-tyr
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • MAPK
    Pathway No. : 352
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.

    MAPK-tyr acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • MAPK
    Pathway No. : 352
    0.04629630.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    2MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Shared_Object_
    Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Pathway No. : 347
  • 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

    MAPK-tyr acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_Feedback_Tuning Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • MAPK
    Pathway No. : 352
    0.04629630.34explicit 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
    2MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Accession No. : 78
  • Shared_Object_
    Ajay_Bhalla_
    2004_Feedback_
    Tuning

    Pathway No. : 347
  • 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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