Prenylated FMN: Biosynthesis, purification, and Fdc1 activation.
Methods Enzymol
; 620: 469-488, 2019.
Article
em En
| MEDLINE
| ID: mdl-31072498
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.
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Base de dados:
MEDLINE
Assunto principal:
Carboxiliases
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Escherichia coli
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Ensaios Enzimáticos
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Mononucleotídeo de Flavina
Idioma:
En
Revista:
Methods Enzymol
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Canadá