C. Dale Poulter

University of Utah

Primary Section: 14, Chemistry
Secondary Section: 21, Biochemistry
Membership Type: Member (elected 2009)

Research Interests

As a chemist working at the boundary between chemistry and biology, I have studied the biosynthesis of isoprenoid compounds, a family of molecules that are essential for life in all organisms. My laboratory has identified and cloned the genes for enzymes that catalyze key reactions for construction the carbon skeletons of isoprenoid molecules and established mechanisms for the enzyme-catalyzed reactions. We discovered that these reactions share a common mechanistic motif based on electrophilic alkylations of nucleophilic groups and that the enzymes, which catalyze these reactions, share a common structural motif, the isoprenoid fold. More recently, we found that relatively modest structural changes in the enzymes can change the carbon skeletons of the products produced and that minor alterations in the catalytic machinery of only two isoprenoid synthase enzymes give a family of proteins that synthesize the 7 of the 8 fundamental isoprenoid carbon skeletons found in nature. I am trying to decipher how the structural changes lead to changes in the products formed as a basis for understanding how new biosynthetic reactions and pathways might have evolved.

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