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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q1A666_9FIRM Q1A666_9FIRM] | | [https://www.uniprot.org/uniprot/Q1A666_9FIRM Q1A666_9FIRM] |
| <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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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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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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
