5i2a

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Current revision (12:33, 6 March 2024) (edit) (undo)
 
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q1A666_9FIRM Q1A666_9FIRM]
[https://www.uniprot.org/uniprot/Q1A666_9FIRM Q1A666_9FIRM]
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical reactions. In this work, we present the first biochemical and structural data for a GRE-type diol dehydratase from the organism Roseburia inulinivorans (RiDD). Despite high sequence (48% identity) and structural similarity to the GRE-type glycerol dehydratase from Clostridium butyricum (CbGD), we demonstrate that the RiDD is in fact a diol dehydratase. In addition, the RiDD will utilize both (S)-1,2-propanediol and (R)-1,2-propanediol as a substrate, with an observed preference for the (S) enantiomer. Based on the new structural information we develop and successfully test a hypothesis that explains the functional differences we observe.
 
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1,2-propanediol Dehydration in Roseburia inulinivorans; Structural Basis for Substrate and Enantiomer Selectivity.,LaMattina JW, Keul ND, Reitzer P, Kapoor S, Galzerani F, Koch DJ, Gouvea IE, Lanzilotta WN J Biol Chem. 2016 Jun 1. pii: jbc.M116.721142. PMID:27252380<ref>PMID:27252380</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 5i2a" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
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Current revision

1,2-propanediol Dehydration in Roseburia inulinivorans; Structural Basis for Substrate and Enantiomer Selectivity

PDB ID 5i2a

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