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Table 1 Kinetic parameters for ATPase activities of 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

  K m (μM) V max (μM min−1) k cat (min−1)
HpMutS2 412.1 ± 83.43 1.88 ± 0.13 41.77 ± 2.88
HpMutS2-G338R 939.3 ± 489.2 0.64 ± 0.15 14.22 ± 3.33
HpMutS2-E413A 373.2 ± 188.6 0.19 ± 0.03 4.22 ± 0.66
  1. The kinetic parameters for HpMutS2, HpMutS2-G338R, and HpMutS2-E413A were determined by varying the substrate concentration and performing Michaelis-Menten analysis. The error values represent standard deviation from at least two different experiments