Thursday, October 7, 2021
3:00 – 4:30 p.m. (AST)
On Zoom
Passcode: 446008
Harnessing the Chemistry of Plant Natural Product Biosynthesis
By Sarah E. O’Connor
The Director of the Department of Natural Product Biosynthesis at the Max Planck Institute of Chemical Ecology.
Abstract
Through the concerted action of enzymes that are assembled into metabolic pathways, nature creates enormous chemical complexity from simple starting materials.
This talk will highlight the discovery process for enzymes that catalyze unusual or unprecedented enzymatic transformations, mechanistic and structural characterization of these enzymes, and methods by which these enzymes can be harnessed for metabolic engineering to generate pharmacological important compounds. We study a variety of different plants and molecules: two recent examples are the anti-cancer agent vinblastine, and the insect repellent (and active ingredient of catnip) nepetalactone.
About the speaker
Prof. Dr. Sarah Ellen O’Connor is Director of the Department of Natural Product Biosynthesis at the Max Planck Institute of Chemical Ecology (Jena, Germany). She obtained her Ph.D. in Organic Chemistry from the Massachusetts Institute of Technology in 2001, and was an ACS Irving Sigal post-doctoral fellow at the Department of Biological Chemistry at Harvard Medical School (Boston, USA) from 2001-2003. From 2003-2011 she was Assistant and Associate Professor of Chemistry at the Massachusetts Institute of Technology, from 2011-2019 she was a Project Leader and Professor in the Department of Biological Chemistry at the John Innes Centre, and in 2019 she moved to the Max Planck Institute of Chemical Ecology. She has co-authored over 100 peer-reviewed papers and is the co-inventor of 2 patent applications.
She has mentored 13 Ph.D. students and 26 postdocs. Her major research interest is planted biosynthetic pathways, where her group takes a multi-disciplinary approach to discover new genes responsible biosynthesis of complex natural products. Her group also studies the mechanism, engineering and evolution of these biosynthetic enzymes.
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