Biosynthesis and Activity of Prenylated FMN Cofactors.
Cell Chem Biol
; 25(5): 560-570.e6, 2018 05 17.
Article
em En
| MEDLINE
| ID: mdl-29551348
ABSTRACT
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 prFMNiminium or C2'-hydroxylated prFMNiminium 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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Base de dados:
MEDLINE
Assunto principal:
Escherichia coli
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Vias Biossintéticas
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Mononucleotídeo de Flavina
Idioma:
En
Revista:
Cell Chem Biol
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Canadá