@inbook{335bccda1237469f89436f0870fa81ce,
title = "Prenylated FMN: Biosynthesis, purification, and Fdc1 activation",
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.",
keywords = "AF1214, Dimethylallyl phosphate, Escherichia coli, Fdc1, FMN, FMN prenyltransferase UbiX, Polyphosphate, Prenol kinase, Prenylated FMN, Reversible decarboxylase UbiD",
author = "Khusnutdinova, {Anna N.} and Johnny Xiao and Wang, {Po Hsiang} and Batyrova, {Khorcheska A.} and Robert Flick and Edwards, {Elizabeth A.} and Yakunin, {Alexander F.}",
note = "Publisher Copyright: {\textcopyright} 2019 Elsevier Inc.",
year = "2019",
doi = "10.1016/bs.mie.2019.03.021",
language = "???core.languages.en_GB???",
isbn = "9780128168295",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "469--488",
editor = "Palfey, {Bruce A.}",
booktitle = "Methods in Enzymology",
}