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. 2017 Jul 27;292(38):15870–15879. doi: 10.1074/jbc.M117.804625

Table 2.

Comparison of single-turnover parameters of LIG3β and LIG1

Single-turnover parameters were obtained at 150 mm ionic strength. All reactions contained 600 nm adenylylated enzyme and 100 nm nicked DNA substrate in the presence of 20 mm Mg2+ and the absence of ATP.

Kinetic parameter LIG3β LIG1a Relative LIG1/LIG3β
kadenylylation (s−1)b 1.6 ± 0.2 1.3 ± 0.3 0.81
ktransfer (s−1) 0.89 ± 0.03 2.6 ± 0.6 2.9
kseal (s−1) 19 ± 6 12 ± 2 0.63
KMg, transfer (mm) 0.30 ± 0.07 0.15 ± 0.06 0.50
KMg, seal (mm) 18 ± 3 2.6 ± 0.9 0.14

a LIG1 values were previously reported for Δ232 LIG1 under similar experimental conditions (34).

b The microscopic rate constant for enzyme adenylylation was calculated using a kcat value of 0.55 s−1 with the net rate constants equation (Equation 4). The error is represented as S.D. from the mean (n ≥ 3).