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Further kinetic analyses showed that Wt MhTyrA p had a K m of 378 μM and turnover rate ( k cat ) of 2.4 s −1 using prephenate substrate and NADP + cofactor (Figure 4, Table 1), which are comparable to previously characterized microbial TyrA p enzymes (Bonvin et al., p Wt (Figure 4, Table 1) precluded it from kinetic analysis using arogenate