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Further kinetic analyses showed that Wt MhTyrA p had a K m of 378 M 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., 2010)

While these increases typically resolved or stabilized, they represent a unique variable for researchers to monitor