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. Author manuscript; available in PMC: 2017 Oct 1.
Published in final edited form as: Bioorg Med Chem. 2016 Jul 29;24(19):4536–4543. doi: 10.1016/j.bmc.2016.07.055

Table 2.

Comparison of kinetic values of wild-type and mutants of B. anthracis DHOases.

Enzyme Substrate KM (µM) kcat (s−1) Kcat/KM (M−1s−1)
WT-DHOase Ca-asp 112 ± 24 2.1 ± 0.1 1.9 × 104
WT-DHOase DHO 114 ± 16 1.9 ± 0.1 1.7 × 104
R63A-DHOase Ca-asp na na na
R63A-DHOase DHO na na na
N93A-DHOase Ca-asp 1183 ± 251 1.4 ± 0.1 1.2 × 103
N93A-DHOase DHO na na na
D304A-DHOase Ca-asp na na na
D304A-DHOase DHO na na na

na : no activity (not measurable)