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Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis*

Identifieur interne : 000346 ( Main/Exploration ); précédent : 000345; suivant : 000347

Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis*

Auteurs : Margot J. Zaccardi [États-Unis] ; Eric M. Yezdimer [États-Unis] ; David D. Boehr [États-Unis]

Source :

RBID : PMC:3772182

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.


Url:
DOI: 10.1074/jbc.M113.487447
PubMed: 23900843
PubMed Central: 3772182


Affiliations:


Links toward previous steps (curation, corpus...)


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Bacteria require the enzyme indole-3-glycerol phosphate synthase for the production of Trp.</p>
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<bold>Results:</bold>
Glu-51 and Lys-53 are identified as the base and acid acting in the dehydration step of enzyme catalysis.</p>
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<bold>Conclusion:</bold>
Ring closure and dehydration steps are catalyzed by distinct active-site surfaces.</p>
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Enzyme inhibitors targeted against these active-site surfaces may serve as novel antibiotics.</p>
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