1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY.

Joseph W LaMattina, Nicholas D Keul, Pierre Reitzer, Suraj Kapoor, Felipe Galzerani, Daniel J Koch, Iuri E Gouvea, William N Lanzilotta

The Journal of biological chemistry 2016 Jul 22

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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, 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. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

Citation

Joseph W LaMattina, Nicholas D Keul, Pierre Reitzer, Suraj Kapoor, Felipe Galzerani, Daniel J Koch, Iuri E Gouvea, William N Lanzilotta. 1,2-Propanediol Dehydration in Roseburia inulinivorans: STRUCTURAL BASIS FOR SUBSTRATE AND ENANTIOMER SELECTIVITY. The Journal of biological chemistry. 2016 Jul 22;291(30):15515-26