Enzymatic reductive dehalogenation controls the biosynthesis of marine bacterial pyrroles

TitleEnzymatic reductive dehalogenation controls the biosynthesis of marine bacterial pyrroles
Publication TypeJournal Article
Year of Publication2016
AuthorsA. Gamal E, Agarwal V., Rahman I., Moore BS
JournalJournal of the American Chemical Society
Volume138
Pagination13167-13170
Date Published2016/10
Type of ArticleArticle
ISBN Number0002-7863
Accession NumberWOS:000385469600018
Keywordsacid; ahpd; mechanism; microbial dehalogenation; mycobacterium-tuberculosis
Abstract

Enzymes capable of performing dehalogenating reactions have attracted tremendous contemporary attention due to their potential application in the bioremediation of anthropogenic polyhalogenated persistent organic pollutants. Nature, in particular the marine environment, is also a prolific source of polyhalogenated organic natural products. The study of the biosynthesis of these natural products has furnished a diverse array of halogenation biocatalysts, but thus far no examples of dehalogenating enzymes have been reported from a secondary metabolic pathway. Here we show that the penultimate step in the biosynthesis of the highly brominated marine bacterial product pentabromopseudilin is catalyzed by an unusual debrominase Bmp8 that utilizes a redox thiol mechanism to remove the C-2 bromine atom of 2,3,4,5-tetrabromopyrrole to facilitate oxidative coupling to 2,4-dibromophenol. To the best of our knowledge, Bmp8 is first example of a dehalogenating enzyme from the established genetic and biochemical context of a natural product biosynthetic pathway.

DOI10.1021/jacs.6b08512
Short TitleJ. Am. Chem. Soc.
Student Publication: 
No
Research Topics: 
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