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. 2021 Dec 22;9(3):e00009-21. doi: 10.1128/Spectrum.00009-21

TABLE 2.

Apparent steady-state kinetic parameters for MsEPSPS enzymes

MsEPSPS enzymea Km (μM) kcat (s−1) kcat/Km (M−1s−1)
WT 88 ± 11 0.5530 ± 0.0185 6.28 E+03 ± 813
D61W 1,014 ± 975 0.1075 ± 0.0608 1.06 E02 ± 118
R134A 3,676 ± 1,007 0.1843 ± 0.0330 5.01 E01 ± 16
E321N 3,081 ± 808 0.4378 ± 0.0469 1.42 E02 ± 40
a

Recombinant EPSPS enzymes from M. smegmatis: WT and point mutants. S3P was used at saturating concentrations (see Table S1 in the supplemental material) and PEP as a variable substrate in the enzymatic assay. All reactions were performed in duplicate.