Prenylated FMN: Biosynthesis, purification, and Fdc1 activation.

Clicks: 308
ID: 97245
2019
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Abstract
Prenylated flavin mononucleotide (prFMN) is a recently discovered flavin cofactor produced by the UbiX family of FMN prenyltransferases, and is required for the activity of UbiD-like reversible decarboxylases. The latter enzymes are known to be involved in ubiquinone biosynthesis and biotransformation of lignin, aromatic compounds, and unsaturated aliphatic acids. However, exploration of uncharacterized UbiD proteins for biotechnological applications is hindered by our limited knowledge about the biochemistry of prFMN and prFMN-dependent enzymes. Here, we describe experimental protocols and considerations for the biosynthesis of prFMN in vivo and in vitro, in addition to cofactor extraction and application for activation of UbiD proteins.
Reference Key
khusnutdinova2019prenylatedmethods Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Khusnutdinova, Anna N;Xiao, Johnny;Wang, Po-Hsiang;Batyrova, Khorcheska A;Flick, Robert;Edwards, Elizabeth A;Yakunin, Alexander F;
Journal methods in enzymology
Year 2019
DOI
S0076-6879(19)30102-8
URL
Keywords
Escherichia coli af1214 dimethylallyl phosphate fmn fmn prenyltransferase ubix fdc1 polyphosphate prenol kinase prenylated fmn reversible decarboxylase ubid

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