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Understanding these options allows researchers to select the approach best suited to their specific goals and circumstances

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)

24 PanS.LvZ.WangR.ShuH.YuanS.YuY.et al (2022)

Lai HW, See CY, Chen JY, Wu VC

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