Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis

Abstract

Background: Bacteria require the enzyme indole-3-glycerol phosphate synthase for the production of Trp. Results: Glu-51 and Lys-53 are identified as the base and acid acting in the dehydration step of enzyme catalysis. Conclusion: Ring closure and dehydration steps are catalyzed by distinct active-site surfaces. Significance: Enzyme inhibitors targeted against these active-site surfaces may serve as novel antibiotics. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.