Date of Award


Document Type

Open Access Dissertation


Chemistry and Biochemistry


College of Arts and Sciences

First Advisor

Maksymilian Chruszcz


Agricultural pests are a worldwide problem and cause billions of dollars in crop loss. In the United States alone, an estimated $40 billion USD is lost per year due to insecticide resistance [1]. Studied here are proteins (potentially new pesticide targets) from the agricultural pests Tetranychus urticae and Aspergillus fumigatus. T. urticae, or twospotted spidermite, is a polyphagous pest, and three proteins from this pest, a cyanase, a glutathione S-transferase and an intradiol ring-cleavage dioxygenase are described [2]. Cyanase is involved in the conversion of bicarbonate and cyanate, a toxic self-defense metabolite produced by plants, into ammonia and carbon dioxide. Glutathione Stransferase conjugates reduced glutathione to xenobiotics for detoxification and have been associated with insecticide resistance [3]. Intradiol ring-cleavage dioxygenase is involved in the breakdown and metabolism of toxic aromatic compounds.

Furthermore, A. fumigatus is a ubiquitous fungus that is not only a problem in agriculture, but also in healthcare. A. fumigatus drug resistance is becoming more prominent which is mainly attributed to the widespread use of fungicides in agriculture [4]. The 2-methylcitrate cycle, which is only present in fungi, is responsible for detoxifying propionyl-CoA, a toxic metabolite produced as the fungus breaks down proteins [5]. The enzyme responsible for this detoxification is 2-methylcitrate synthase (mcsA) and is a potential candidate for the design of new anti-fungals. However, mcsA shares a similar reaction to human citrate synthase (hCS), and both the structure and function of each enzyme is studied in parallel to find mcsA-specific inhibitors.

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