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. Author manuscript; available in PMC: 2022 Aug 24.
Published in final edited form as: Biochemistry. 2021 Aug 6;60(33):2524–2536. doi: 10.1021/acs.biochem.1c00384

Figure 3. A positive charge at the −1 substrate position is important for KDAC8 activity.

Figure 3.

(A) Peptides derived from FRKacRW, where R(−1) was substituted, were reacted with KDAC8. Average specific activity was normalized such that the activity of KDAC8 with FRKacRW was represented as 1. Error bars represent standard deviations (n≥4), and p-values are shown for statistically significant differences between activity with FRKacRW and activity with each other substrate. (B) Results of MD analysis identifying interactions between specific residues of KDAC8 and derivative peptide substrates reacted in panel A. x(−1) refers to the substrate residue in the −1 position for each peptide. Shading corresponds to the percent of time a particular interaction was observed during MD simulations.