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. 2020 Jun 8;39(14):e104410. doi: 10.15252/embj.2020104410

Figure EV2. Kinetic characterization of CK1α inhibition by MDMX .

Figure EV2

  1. Reaction velocity as a function of β‐catenin peptide substrate and increasing MDMX concentrations at 100 μM ATP and 2 nM CK1α. Data in Fig 1C were fitted to the competitive inhibition model.
  2. Same as (A) but data fitted to the allosteric sigmoidal model.
  3. Reaction velocity as a function of ATP and increasing MDMX concentrations at 800 μM peptide substrate and 2 nM CK1α. Data in Fig 1D were fitted to the mixed inhibition model. The value of the parameter Alpha determines the mechanism of inhibition, and Alpha < 1 indicates that the inhibitor preferentially binds to the enzyme–substrate complex. Equations used for data fitting are shown in the respective graph titles. The results are representative of 3 experiments.