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. Author manuscript; available in PMC: 2020 May 1.
Published in final edited form as: Chem Biol Drug Des. 2019 Jan 30;93(5):865–873. doi: 10.1111/cbdd.13476

Figure 2: Michaelis-Menten data points fitted to the mixed inhibition rate equation and Double reciprocal plots.

Figure 2:

To determine the mode of inhibition in respect to AcCoA and H4-20 peptide, H4K12CoA was added to the reaction mixture at 0 nM, 20 nM, and 100 nM. A) Conditions to determine HAT1 kinetics in respect to AcCoA included 100 µM H4-20 peptide, 5 nM HAT1, and 0-10 µM AcCoA, with a reaction time of 9 min. B) Conditions to determine HAT1 kinetics in respect to H4-20 peptide included 3 µM AcCoA, 20 nM HAT1, and 0-100 µM AcCoA, with a reaction time of 9 min. Double reciprocal plots of H4K12CoA with respect to AcCoA (C) and H4-20 (D).