Liu, Hung-Wen

Hung-Wen (Ben) Liu

College of Pharmacy, Department of Chemistry

George H. Hitchings Regents Chair in Drug Design

Phone: 512-232-7811

Office Location
PHR 3.206B

Postal Address
The University of Texas at Austin
Phar-Med Chem
PO Box F
Austin, TX 78713

My group is currently working on three general areas with the focus aimed at the elucidation of the mechanisms of novel enzymatic reactions and the design of methods to control and/or regulate their functions. Most of the biological systems under investigation are target candidates for therapeutic drugs.

Enzyme Mechanism and Inhibitor Design: We study the mechanisms of enzymes involved in diverse biological processes including the formation of bacterial cell wall, biosynthesis of and resistance to antibiotics, and biosynthesis and metabolism of lipids.

Metabolic Pathway Engineering: Through selective disruption and/or substitution of sugar biosynthetic genes in the microorganisms that produce bioactive glycosylated secondary metabolites, we are exploring the feasibility of engineering nature�s biosynthetic machinery for the production of novel compounds carrying designed sugar appendages.

Protein Function Regulation: We study poly(ADP-ribose) polymerase, an enzyme that recognizes damaged DNA and turns on the repairing machinery through polyADP-ribosylation of itself and other nuclear proteins. This posttranslational modification is also essential to other crucial cellular events including apoptosis.

Mechanistic Studies of an Enzymatic Unprecedented 1,2-Phosphono Migration Reaction (2013) Nature 496, 114-118.

A Combined EPR-Kinetic Isotope Effect Study of Radical-Mediated Dehydrogenation of an Alcohol by the Radical SAM Enzyme DesII: Evidence for General Base Catalysis (2013) Proc. Nat. Acad. Sci. USA 110, 2088-2093.

In vitro Characterization of LmbR and LmbN: Construction of the Octose 8-Phosphate Intermediate in Lincomycin A Biosynthesis (2012) J. Am. Chem. Soc. 134, 17432-17435.

Evidence for Radical-Mediated Catalyzed by HppE – A Study Using Cyclopropyl and Methylenecyclopropyl Substrate Analogues (2012) J. Am. Chem. Soc. 134, 116171-16174.

An Enzyme-Catalyzed [4+2] Cycloaddition is a Key Step in the Biosynthesis of Spinosyn A (2011) Nature 473, 109-112.

Graduate Students:

  • Chen, Jung-Kuei

Post Doc Students:

  • Borisova, Svetlana
  • Lepore, Bryan
  • Ogasawara, Yasushi
  • Pu, Xiaotao