1,2-Propanediol Dehydration in Roseburia inulinivorans: Structural Basis for Substrate and Enantiomer Selectivity
Journal Article
·
· Journal of Biological Chemistry
- Univ. of Georgia, Athens, GA (United States)
- Braskem S.A., São Paulo, SP (Brazil)
Glycyl radical enzymes (GREs) represent a diverse superfamily of enzymes that utilize a radical mechanism to catalyze difficult, but often essential, chemical reactions. Here, 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.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1324768
- Journal Information:
- Journal of Biological Chemistry, Journal Name: Journal of Biological Chemistry Journal Issue: 30 Vol. 291; ISSN 0021-9258
- Publisher:
- American Society for Biochemistry and Molecular BiologyCopyright Statement
- Country of Publication:
- United States
- Language:
- ENGLISH
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