Table 1.

Summary of kinetic data and substrate specificity constants, single-turnover assays, and thermodynamic constants from EMSAs

Activity assays included 150 nm enzyme, 100 nm DNA, and 15 μm AdoMet. Reactions were conducted in triplicate and reached completion in 20 min at room temperature. Binding studies included 5 nm DNA and 60 μm sinefungin. Binding experiments were performed at 4 °C for 30 min in methylation reaction buffer. Bold type indicates a lack of the C-terminal segment.

Enzyme	Double-stranded DNA			Single-stranded DNA
	kmethylation	Kd	kmethylation/Kd	kmethylation	Kd	kmethylation/Kd
	min−1	nm	nm min−1	min−1	nm	nm min−1
CcrM (C. crescentus)	2.61 ± 0.21	70.8 ± 7.2	0.037 ± 0.005	3.33 ± 0.30	39.2 ± 4.5	0.085 ± 0.012
CcrM C. crescentus truncation	No activity	No activity	No activity	No activity	No activity	No activity
CcrM C. crescentus W332A	No activity	No activity	No activity	No activity	No activity	No activity
CcrM A. tumefaciens	0.50 ± 0.05	89.0 ± 3.1	0.006 ± 0.001	0.73 ± 0.07	34.2 ± 5.0	0.021 ± 0.004
CcrM B. abortus	0.42 ± 0.03	41.5 ± 7.4	0.010 ± 0.002	0.46 ± 0.06	77.1 ± 14.6	0.006 ± 0.001
M.HinfI	1.27 ± 0.10			0.060 ± 0.003
M.HinfI truncation	No activity	>1 μm	No activity	0.39 ± 0.03
M.HhaII	2.30 ± 0.21	31.5 ± 3.0	0.073 ± 0.010	>300 times slower
DpnA	0.020 ± 0.001			0.051 ± 0.004