Journal
CELL CHEMICAL BIOLOGY
Volume 25, Issue 5, Pages 560-+Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2018.02.007
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Funding
- NSERC Industrial Biocatalysis Strategic Network grant
- Genome Canada (Government of Canada through Genome Canada)
- Genome Canada (Ontario Genomics Institute) [2009-OGI-ABC-1405]
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Prenylated flavin mononucleotide (prFMN) is a recently discovered cofactor required by the UbiD family of reversible decarboxylases involved in ubiquinone biosynthesis, biological decomposition of lignin, and biotransformation of aromatic compounds. This cofactor is synthesized by UbiX-like prenyltransferases catalyzing the transfer of the dimethylallyl moiety of dimethylallyl-monophosphate (DMAP) to FMN. The origin of DMAP for prFMN biosynthesis and the biochemical properties of free prFMN are unknown. We show that in Escherichia coli cells, DMAP can be produced by phosphorylating prenol using ThiM or dephosphorylating DMAPP using Nudix hydrolases. We produced 14 active prenyltransferases whose properties enabled the purification and characterization of protein-free forms of prFMN. In vitro assays revealed that the UbiD-like ferulate decarboxylase (Fdc1) can be activated by free prFMN(iminium) or C2'-hydroxylated prFMN(iminium) under both oxidized and reduced conditions. These insights into the biosynthesis and properties of prFMN will facilitate further elucidation of the biochemical diversity of reversible UbiD (de) carboxylases.
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