W. Todd Lowther, PhD, Wake Forest School of Medicine

W. Todd Lowther, PhD

The Lowther lab is focused on several ongoing projects to understand the molecular basis for enzyme catalysis and substrate/inhibitor/ligand specificity. In these endeavors a variety of molecular biology, biochemical and X-ray crystallographic methods are utilized. Current projects in the lab include: (1) an analysis of the molecular basis for the repair or retro-reduction of hyperoxidized peroxiredoxins by an enzyme called surfiredoxin, (2) the characterization of enzymes involved in glyoxylate metabolism and kidney stone formation, (3) the study of the thioesterase domain of human fatty acid synthase and its inhibition by the anti-cancer compound Orlistat, and (4) the study of methionine sulfoxide reductases.



  1. Lin Z, Johnson LC, Weissbach H, Brot N, Lively MO, and Lowther WT. Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function. PNAS 104(23): 9597-9602 (2007).
  2. Klomsiri C, Nelson KJ, Bechtold E, Soito L, Johnson LC, Lowther WT, Ryu S, King SB, Furdui CM and Poole LB. Use of dimedone-based chemical probes for sulfenic acid detection; evaluation of conditions affecting probe incorporation into redox sensitive proteins. Methods. Enzymol. 473: 77-94. (2010).