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Table 3 DNA cleavage rates (pM min−1) determined for HpMutS2 and mutants

From: Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function

  No nucleotide + ATP + ADP + ATPγS
Single-stranded DNA
 HpMutS2 24.82 ± 1.15 32.08 ± 5.32 28.11 ± 5.15 28.5 ± 3.68
 HpMutS2-G338R 40.19 ± 8.73 40.45 ± 9.52 38.87 ± 8.79 ND
 HpMutS2-E413A 6.50 ± 0.55 7.23 ± 0.65 6.90 ± 1.4 ND
 HpMutS2ΔSmr-D30A 2.12 ± 1.67 ND ND ND
Holliday junction
 HpMutS2 26.49 ± 3.95 37.77 ± 8.59 18.85 ± 1.9 17.44 ± 0.84
 HpMutS2-G338R 41.59 ± 9.53 43.7 ± 11.42 41.6 ± 10.27 ND
 HpMutS2-E413A 4.92 ± 1.25 1.27 ± 1.01 6.77 ± 3.53 ND
 HpMutS2ΔSmr-D30A 3.34 ± 1.67 ND ND ND
  1. Reaction rates were estimated by dividing the total product formed by corresponding incubation time obtained from the linear range of enzymatic activity (Figs. 6a-f). The error values represent standard deviation from two or more different time points. ND, not determined