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Changing The Substrate Specificity Of Arogenate Dehydratases (Adts) From Arabidopsis Thaliana., Megan Es Smith-Uffen

Electronic Thesis and Dissertation Repository

Phenylalanine (Phe), an essential aromatic amino acid, serves as a precursor for protein synthesis and a variety of secondary metabolites in plants. Two pathways are known for Phe biosynthesis. In the first, prephenate dehydratases (PDTs) convert prephenate to phenylpyruvate, which is transaminated to Phe. In the second, prephenate is transaminated to arogenate, which is converted to Phe by arogenate dehydratases (ADTs). ADTs and PDTs are structurally very similar, as are their substrates. Six ADTs (ADT1-ADT6) have been identified in Arabidopsis thaliana. ADT1 and ADT2 can recognize both prephenate and arogenate as substrates whereas ADT3-ADT6 are solely arogenate-accepting. Twenty ADT domain-swapping …