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

Margot J. Zaccardi, Eric M. Yezdimer, David D. Boehr

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)26350-26356
Number of pages7
JournalJournal of Biological Chemistry
Volume288
Issue number37
DOIs
StatePublished - Sep 13 2013

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Indole-3-Glycerol-Phosphate Synthase
Catalysis
Dehydration
Catalytic Domain
Acids
Enzyme Inhibitors
Enzymes
Bacteria
Anti-Bacterial Agents

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

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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.",
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Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis. / Zaccardi, Margot J.; Yezdimer, Eric M.; Boehr, David D.

In: Journal of Biological Chemistry, Vol. 288, No. 37, 13.09.2013, p. 26350-26356.

Research output: Contribution to journalArticle

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