Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis*
Identifieur interne : 000429 ( Ncbi/Checkpoint ); précédent : 000428; suivant : 000430Functional 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 :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2013.
Abstract
Url:
DOI: 10.1074/jbc.M113.487447
PubMed: 23900843
PubMed Central: 3772182
Affiliations:
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<author><name sortKey="Boehr, David D" sort="Boehr, David D" uniqKey="Boehr D" first="David D." last="Boehr">David D. Boehr</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis<xref ref-type="fn" rid="FN1">*</xref>
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<affiliation wicri:level="2"><nlm:aff id="aff1">From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Pennsylvanie</region>
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<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Pennsylvanie</region>
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<author><name sortKey="Boehr, David D" sort="Boehr, David D" uniqKey="Boehr D" first="David D." last="Boehr">David D. Boehr</name>
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<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
Bacteria require the enzyme indole-3-glycerol phosphate synthase for the production of Trp.</p>
<p><bold>Results:</bold>
Glu-51 and Lys-53 are identified as the base and acid acting in the dehydration step of enzyme catalysis.</p>
<p><bold>Conclusion:</bold>
Ring closure and dehydration steps are catalyzed by distinct active-site surfaces.</p>
<p><bold>Significance:</bold>
Enzyme inhibitors targeted against these active-site surfaces may serve as novel antibiotics.</p>
</div>
</front>
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<name sortKey="Boehr, David D" sort="Boehr, David D" uniqKey="Boehr D" first="David D." last="Boehr">David D. Boehr</name>
<name sortKey="Yezdimer, Eric M" sort="Yezdimer, Eric M" uniqKey="Yezdimer E" first="Eric M." last="Yezdimer">Eric M. Yezdimer</name>
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