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Changing The Substrate Specificity Of Arogenate Dehydratases (Adts) From Arabidopsis Thaliana., Megan Es Smith-Uffen
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 …
Evolutionary And In Silico Analysis Of The Antiviral Trim22 Gene, Jenna Kelly
Evolutionary And In Silico Analysis Of The Antiviral Trim22 Gene, Jenna Kelly
Electronic Thesis and Dissertation Repository
Tripartite motif protein 22 (TRIM22) is an evolutionarily ancient interferon-induced protein that been shown to potently inhibit human immunodeficiency virus (HIV), hepatitis B virus (HBV), and influenza A virus (IAV) replication. Altered TRIM22 expression levels have also been linked to autoimmune disease, cancer, and cellular proliferation. Despite its important role in a number of biological processes, the factors that influence TRIM22 expression and/or antiviral activity remain largely unknown. To identify key functional sites in TRIM22, we performed extensive evolutionary and in silico analyses on the TRIM22 coding region. These tools allowed us to pinpoint multiple sites in TRIM22 that have …