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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
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BMC Microbiology

ISSN: 1471-2180

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