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The Q227E mutant displayed substantial ADH activity compared to the Wt enzyme with a K m for arogenate of 3.3 mM, similar to that of Q227E for prephenate (2.7 mM, Figure 4C, Table 1) though still 10-fold higher than that of the Wt enzyme for prephenate (Figure 4D, Table 1) and other previously characterized TyrA a enzymes (Bonvin et al., −1 s −1 , Figure 3)