Prenylated FMN: Biosynthesis, purification, and Fdc1 activation

Anna N. Khusnutdinova, Johnny Xiao, Po Hsiang Wang, Khorcheska A. Batyrova, Robert Flick, Elizabeth A. Edwards, Alexander F. Yakunin

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

2 Scopus citations

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.

Original languageEnglish
Title of host publicationMethods in Enzymology
EditorsBruce A. Palfey
PublisherAcademic Press Inc.
Pages469-488
Number of pages20
ISBN (Print)9780128168295
DOIs
StatePublished - 2019

Publication series

NameMethods in Enzymology
Volume620
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • AF1214
  • Dimethylallyl phosphate
  • Escherichia coli
  • Fdc1
  • FMN
  • FMN prenyltransferase UbiX
  • Polyphosphate
  • Prenol kinase
  • Prenylated FMN
  • Reversible decarboxylase UbiD

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