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

doi:10.1074/jbc.M113.487447

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 journal › Article › peer-review

9 Scopus citations

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 language	English (US)
Pages (from-to)	26350-26356
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	288
Issue number	37
DOIs	https://doi.org/10.1074/jbc.M113.487447
State	Published - Sep 13 2013

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.487447

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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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AU - Yezdimer, Eric M.

AU - Boehr, David D.

PY - 2013/9/13

Y1 - 2013/9/13

N2 - 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.

AB - 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

Abstract

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