Enzymes involved in the degradation of aromatic compounds - mechanism, evolution and regulation

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The myriad of chemical reactions occurring within living systems are catalyzed by enzymes. Most enzymes are proteins which fold into a compact three dimensional structures, creating a unique environment where chemical catalysis can occur. Therefore, the structure of an enzyme has a bearing on function. S. Seah and his students are studying this structure-function relationship in enzymes known as pyruvate aldolases, that evolve independently to catalyze similar reactions. Specifically, his team is determining if these aldolases utilize similar chemical strategies for catalysis. They are also studying how some of these aldolases regulate their catalytic activity and interact with other enzymes in a metabolic pathway to ensure efficiency. The aldolases being studied are from aromatic degradation pathways that are useful for bioremediation of toxic aromatic pollutants, such as Polychlorinated biphenyls. Aldolases are also useful for the synthesis of pharmaceutical compounds. One of the aldolase being studied is from bacteria that cause tuberculosis, and therefore this work may lead o the development of new drugs against this disease. At the broader level, learning the principles of how nature creates new enzymes will allow us to apply this knowledge to design new biological catalysts for application in medicine and industry. The research work will also contribute to the new area of "functional genomics" allowing us to predict with greater accuracy the functions of enzymes based on the sequences of their building blocks (amino acids) or 3D fold. Undergraduate, graduate and postdoctoral trainees participating in this work will learn to solve scientific problems using research tools drawn from molecular biology and biochemistry.