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Science and Mathematics

Chemistry Colloquium: Vincenzo Venditti

April 9, 2024 at 4:00pm5:00pm EDT

Center for Science and Technology (CST), 1-132

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The Department of Chemistry in the College of Arts and Sciences is pleased to welcome Dr. Vincenzo Venditti, an associate professor at Iowa State University.

Title: Conformational disorder in regulation of enzymatic catalysis


Enzymes are remarkable nanomachines that play a myriad of essential functions in cellular metabolism. Modulation of enzyme structure and flexibility by cofactor/substrate binding provides an important source of regulation of enzyme function, yet our understanding of the fundamental mechanisms by which concerted protein motion facilitates enzymatic activity is still largely incomplete. Indeed, while several studies have appeared in the past two decades describing how conformational dynamics mediate the biological function of small proteins, our understanding of how the coupling among multiple conformational equilibria determines the activity of large multidomain systems continues to lag. The overall goal of our research is using and developing integrated approaches combining NMR with complementary biophysical and biochemical tools to reveal how modulation of local disorder upon cofactor/substrate binding affects concerted motions and regulates the activity of high molecular weight enzymes that are essential for human and bacterial metabolism. This combination of tools sensitive to protein motion brings a newly detailed picture of high molecular weight enzyme function. The enzymes characterized in my lab are Enzyme I (EI) of the bacterial phosphotransferase system (PTS), and the AlkB family of nucleic acid demethylases. EI is a 128 kDa multi-domain oligomeric enzyme that is a master regulator of bacterial metabolism and an ideal target for the development of broad-spectrum antibiotics. The AlkB demethylases are involved in epigenetic regulation of gene expression and are pharmaceutical targets in anticancer research. Together these distinct classes of enzymes show how the relationship between local disorder and concerted domain motions can be probed by this combination of tools and demonstrate how essential these mechanisms are across diverse enzyme classes.

This event was published on March 25, 2024.

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