Oct 31, 2013

Truncated FAD synthetase for direct biocatalytic conversion of riboflavin and analogs to their corresponding flavin mononucleotides

Protein Engineering, Design & Selection : PEDS
Samantha M IamurriStefan Lutz

Abstract

The preparation of flavin mononucleotide (FMN) and FMN analogs from their corresponding riboflavin precursors is traditionally performed in a two-step procedure. After initial enzymatic conversion of riboflavin to flavin adenine dinucleotide (FAD) by a bifunctional FAD synthetase, the adenyl moiety of FAD is hydrolyzed with snake venom phosphodiesterase to yield FMN. To simplify the protocol, we have engineered the FAD synthetase from Corynebacterium ammoniagenes by deleting its N-terminal adenylation domain. The newly created biocatalyst is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogs to their corresponding FMN cofactors at preparative-scale.

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Mentioned in this Paper

Bacterial Proteins
Corynebacterium
Proteins, Recombinant DNA
Flavin Mononucleotide
Analog
Protein Phosphorylation
FLAD1 gene
Riboflavin
Analogs & derivatives
Flavins

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