Suzanne Walker is a biochemist who is recognized for her work on the assembly of the bacterial cell wall. She is particularly known for her studies characterizing pathways that build important extracellular glycopolymers, including peptidoglycan and teichoic acids, and for innovative strategies to identify pathway-specific inhibitors. A general interest in glycosyltransferases led her to study the metazoan protein O-GlcNAc transferase, and her lab has done the foundational biochemical work on this enzyme, which is essential for cell proliferation. Walker grew up in Gallup, NM and graduated from the University of Chicago in 1983 with a degree in English. She started graduate school at Columbia University and moved with her family to Princeton University where she completed her Ph.D. in 1992. She joined the faculty at Princeton as an Instructor of Chemistry in 1995 and was promoted to Professor of Chemistry in 2003. The following year she moved to the Department of Microbiology at Harvard Medical School. She is a member of the American Academy of Microbiology, the American Academy of Arts and Sciences, and the National Academy of Sciences.

Research Interests

Suzanne Walker's laboratory is interested in two seemingly disparate problems that involve carbohydrate-processing enzymes. One major thrust of her research involves understanding how the bacterial cell envelope is assembled and how its assembly is coordinated with cell growth and division. All bacteria are surrounded by a peptidoglycan cell wall that is crucial for survival. In Gram-positive bacteria, the cell wall is assembled from two different glycopolymers that are coupled outside the cell. Walker has developed methods to make increasingly complex substrates to characterize enzymes in peptidoglycan and teichoic acid assembly pathways, and has used genetic and genomic approaches to understand how the cell assembles and maintains a functional cell envelope. Her structural studies on a bacterial glycosyltransferase required to make the disaccharide building block of peptidoglycan led her to learn about an unusual metazoan glycosyltransferase that used a common substrate. OGT is the only glycosyltransferase that acts in the nucleus, cytoplasm, and mitochondria in eukaryotes, and it the most conserved glycosyltransferase in humans. It has been linked to nutrient sensing, but has over a thousand substrates so identifying its most important cellular roles has been challenging. The Walker lab has developed cell permeable inhibitors to probe OGT biology, defined the catalytic mechanisms of OGT, and elucidated determinants for substrate recognition to provide a foundation for cellular studies to dissect its functions.

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Primary Section

Section 21: Biochemistry

Secondary Section

Section 14: Chemistry