Table 2.

Kinetic parameters of WT Clr4 and the K455R/K472R mutant obtained by steady-state methylation experiments conducted at variable AdoMet concentrations using the H3K9me1 peptide substrate. All data are given as mean ± SEM. The data and fits are shown in Figure 6. Note that the mutant data were fitted to the Michaelis–Menten model corresponding to an n-value of 1. Reaction conditions were c_enzyme = 0.9 µM, c_peptide = 4.58 µM, c_AdoMet = 0–50 µM. K_m refers to AdoMet binding at the specified peptide concentration. v_max values are given relative to WT activity.

Substrate	Clr4 WT			Clr4 K455R/K472R
	Km (µM)	rel. vmax	N	Km (µM)	rel. vmax	n
AdoMet	11.4 ± 1.5	1.0 ± 0.01	1.87 ± 0.19	13.6 ± 1.0	0.71 ± 0.08	1