User:David Vocadlo

I received my BSc degree in combined Chemistry and Biochemistry from the University of British Columbia (UBC, Vancouver, British Columbia, Canada). After considering a career in architecture I found experimental design and the construction of hypotheses to be more engaging. To pursue my particular interest in the remarkable catalytic proficiency of enzymes I joined the laboratory of Stephen Withers at UBC to pursue my PhD studies in Bioorganic Chemistry. While there I synthesized both substrates and inhibitors of retaining glycoside hydrolases and clarified the catalytic mechanism of hen egg white lysozyme (HEWL) [1], a member of GH22. My interests gradually turned to integrating knowledge of the mechanisms of glycan processing enzymes with their functions in cellular systems. To pursue this interest and exploit knowledge of the biochemistry of glycoside hydrolases and transferases to design chemical tools for use in studying glycans in cellular systems, I moved to the University of California at Berkeley (Berkeley, California, USA) to work with Carolyn Bertozzi. While there I developed chemical probes to perform functional proteomics of glycosylation within cellular systems. In 2004 I returned to Canada and joined Simon Fraser University (Burnaby, British Columbia, Canada) where I am now a Canada Research Chair in Chemical Glycobiology and professor in the Departments of Chemistry and Molecular Biology and Biochemistry. My current interests centre of developing and validating chemical tools that can be used to probe and perturb carbohydrates in cellular and organismal models. One particular interest in the laboratory is to improve our understanding of the physiological and pathophysiological roles of an intracellular form of protein glycosylation known as O-GlcNAc.

Please see my Simon Fraser University page for more details on my research interests.

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1. Vocadlo DJ, Davies GJ, Laine R, and Withers SG. (2001). Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature. 2001;412(6849):835-8. DOI:10.1038/35090602 |