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A single Q227E mutation introduces ADH activity in an archaeon TyrA p To test if the non-acidic residue of MhTyrA p at the corresponding 222 position (Gln227) is involved in prephenate substrate specificity, site-directed mutagenesis was performed on MhTyrA p to replace Gln227 with acidic Glu and generate the MhTyrA p Q227E mutant

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doi: 10.1016/j.eng.2024.02.002