| Literature DB >> 27252380 |
Joseph W LaMattina1, Nicholas D Keul1, Pierre Reitzer1, Suraj Kapoor1, Felipe Galzerani2, Daniel J Koch2, Iuri E Gouvea2, William N Lanzilotta3.
Abstract
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, 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 developed and successfully tested a hypothesis that explains the functional differences we observe.Entities:
Keywords: chemical biology; diol dehydratase; enzyme structure; glycerol dehydratase; glycyl radical enzyme; intestinal metabolism; metabolic engineering; radical; radical dehydration
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Year: 2016 PMID: 27252380 PMCID: PMC4957038 DOI: 10.1074/jbc.M116.721142
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157