Dr. Nicole A. Horenstein

Associate Professor

Nicole A. Horenstein

University of Florida
Department of Chemistry
PO Box 117200
Gainesville, FL 32611-7200 USA
352-392-9859 (voice)
352-846-2095 (fax)
email: horen@chem.ufl.edu
office: LEI 402

 

  • EDUCATION

    • B.S., State University of New York, College of Environmental Science and Forestry, 1983
    • M.S., Michigan State University, 1986
    • Ph.D., Columbia University, 1988
    • Postdoctoral Associate, University of California-Berkeley, 1988-1989
    • Postdoctoral Associate, Albert Einstein College of Medicine, 1989-1993

  • Positions and Honors

    • NSF CAREER Award, 1995-2000
    • U. Florida Teaching Incentive Program Award, 1998

    • Pegram Award, Columbia University, 1988   

  • Research Interests

    • Enzyme mechanisms and kinetics
    • protein structure & function
    • biosynthesis
    • synthesis of biologically active molecules

    We integrate tools in organic synthesis, enzymology, molecular biology, and computational methods to unravel complex biomolecular interactions and events. One of our interest areas is carbohydrate chemistry and biochemistry. For example we have applied kinetic isotope effects to understand glycosyltransferase mechanisms. Another project area is focused on study of the biosynthesis of azasugars. These compounds are well known glycosidase inhibitors that feature a nitrogen atom in the ring, rather than oxygen. We have identified part of the biosynthetic path and are working on identifying the other enzymes. We are studying the kinetic and chemical mechanisms of an interesting transaminase in this pathway.  In a related project we have used the three-gene signature for azasugar biosynthesis to locate biosynthetic machinery in other species and are pursuing structure determinations of these glycosidase inhibitors.  In another project area, we chemically synthesize new probes and use computational methods including molecular dynamics to define structural, functional, and selectivity features of ligand binding domains within the nicotinic acetylcholine receptor.