. 2014 Oct 20;111(44):15717–15722. doi: 10.1073/pnas.1404915111

Table 1.

Kinetic parameters for the wild-type, M145A, and F128A BmEH toward the substrate rac-PGE or -NGE

Enzyme	rac-PGE			rac-NGE
Enzyme	k_cat, s⁻¹	K_M, mM	k_cat/K_M, s⁻¹⋅mM⁻¹	k_cat, s⁻¹	K_M, mM	k_cat/K_M, s⁻¹⋅mM⁻¹
Wild type	>400^*	>50^†	N.A.	0.60 ± 0.06	1.3 ± 0.3	0.45 ± 0.12
M145A	>9.5^*	>50^†	N.A.	19.0 ± 2.7	1.5 ± 0.5	12 ± 5
F128A	4.4 ± 0.2	12 ± 1	0.37 ± 0.05	34.1 ± 0 0.4	0.75 ± 0.24	45 ± 15

The PGE and NGE concentrations were varied in the ranges of 3–50 and 0.3–10 mM, respectively. N.A., not available.

Calculated based on the highest rate detected.

^{^†}

No saturation was observed. The K_M values were beyond the concentration range of substrate. The concentration of PGE for activity determination was limited by its low solubility.