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. Author manuscript; available in PMC: 2020 May 2.
Published in final edited form as: Chembiochem. 2019 Mar 14;20(9):1133–1138. doi: 10.1002/cbic.201800756

Figure 3.

Figure 3.

Catalytic efficiencies of the wild type and mutant KDM4A enzymes. (A) Schematic showing coupled fluorescence assay. Formaldehyde generated during demethylation of H3K9me3 peptide is oxidized to formic acid by FDH which in turn reduces NAD+ to NADH. (B) Michaelis-Menten plots for KDM4A, and its alanine and glycine mutants at N198 and S288 with increasing concentration of cofactor 2KG. (C) Steady-state kinetic parameters of the enzymes obtained from plots shown in B.