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The Levinson Emerging Scholars Program

Catherine Louw - Biology and Biochemisty

Catherine LouwCatherine Louw’s interest in performing scientific research was inspired by a summer session at the Seattle Biomedical Research Institute. This experience soon led her to embark on her laboratory experience in the Baker lab, after being intrigued by the idea of computational protein design. Catherine began working with graduate student Justin Siegel on a novel project, aiming to enhance the efficiency of a computationally designed enzyme that could one day be used in a pathway for carbon dioxide fixation. She has developed a high-throughput screening protocol to grow and assay potential hits in a fraction of the time that it would normally take. Catherine is currently a senior at UW, pursuing a dual degree in Biology and Biochemistry. After graduating she hopes to attend medical school to become a doctor in family medicine were she plans to utilize her experiences with research methodologies in order to better understand and incorporate new medical discoveries into her practice.

Mentor: David Baker, Biochemistry

Project Title: Enhancement of a Computationally Designed Enzyme: A Contribution to the End of Global Warming

Abstract: Global warming is a pressing issue worldwide and finding new ways to control excess carbon dioxide is becoming increasingly important. This study aims to develop a novel biological system which converts carbon dioxide into small sugars. To create this system, a new metabolic pathway is being constructed which employs six naturally-occurring enzymes and one computationally-designed enzyme called Formolase. Formolase is derived from a naturally-occurring enzyme, Benzaldehyde Lyase, which ligates two benzaldehyde molecules together, while the desired reaction of Formolase is to ligate three formaldehyde molecules together to create dihydroxyacetone. A computer program called Rosetta was used to create Formolase, identifying four mutations to make within the active site in order to drastically alter substrate specificity. The enzyme would now catalyze the polymerization of formaldehyde over that of benzaldehyde, and when tested, these mutations altered specificity as predicted. In order to further understand this change in specificity, I determined the contribution of each mutated residue to the activity on formaldehyde. This study illuminated the key mutations necessary to maintain desired activity, as well as mutations which could be changed in the future to improve the activity of the enzyme. Although Formolase demonstrates enhanced activity on formaldehyde, the activity must be increased further before it can be used in the metabolic pathway. Therefore, I am now working on mutating additional residues in order to enhance activity. We also plan to alter the structure of the protein by adding new loops and tails to form more contacts with the formaldehyde ligand, which we hypothesize, will further improve our enzyme. Once sufficiently active, Formolase will complete the novel metabolic pathway and provide an alternative method for converting carbon dioxide into a more useful material. In this way, global warming can be controlled and the amount of carbon dioxide in the atmosphere decreased.