. 2014 Mar 31;53(15):2525–2532. doi: 10.1021/bi5002294

Table 1. DNA Binding and 5mC Excision Activities for DMEΔNΔIDR1 Point Mutants^a.

	K_d (μM)	relative affinity	k_st (×10^–5 s^–1)	relative to WT
WT	8.3 ± 1.2	1.0	18.1 ± 1.2	1.0
Q777A	8.1 ± 1.1	1.0	7.6 ± 0.4	0.4
N778A	18.9 ± 3.4	0.4	2.7 ± 0.6	0.1
M1238A	8.5 ± 1.0	1.0	0.02 ± 0.01	0.001
K1286Q	8.2 ± 1.8	1.0	<0.01^b	0.0005
D1304N	0.6 ± 0.1	14	<0.01^b	0.0005

Dissociation constants (K_d) and single-turnover rate constants for 5mC (k_st) excision were measured at 25 °C, pH 8.5, and 170 mM ionic strength using a 25mer DNA duplex containing 5mC and end-labeled with fluorescein. Enzyme concentration was saturating (10 μM) in activity assays. Values are reported as averages ± SD from at least three experiments. Relative binding affinities calculated as (K_d WT)/(K_d Mutant); Relative to WT rates calculated as (k_st Mutant)/(k_st WT).

Activity is below limit of detection.

Table 1. DNA Binding and 5mC Excision Activities for DMEΔNΔIDR1 Point Mutantsa.

Table 1. DNA Binding and 5mC Excision Activities for DMEΔNΔIDR1 Point Mutants^a.