Riboflavin (RF) and its active forms, the cofactors flavin mononucleotide (FMN) and flavin
adenine dinucleotide (FAD), have been extensively used in the food, feed and …

The rapid resistance of pathogens to antibiotics has emerged as a major threat to global
health. Identification of new antibiotic targets is thus needed for developing alternative …

Flavin mononucleotide (FMN) is the active form of riboflavin. It has a wide range of
application scenarios in the pharmaceutical and food additives. However, there are …

FAD synthase (FADS, EC 2.7. 7.2) is the last essential enzyme involved in the pathway of
biosynthesis of Flavin cofactors starting from Riboflavin (Rf). Alternative splicing of the …

The increase of bacterial strains resistant to most of the available antibiotics shows a need to
explore novel antibacterial targets to discover antimicrobial drugs. Bifunctional bacterial FAD …

Prokaryotic bifunctional FAD synthetases (FADSs) catalyze the biosynthesis of FMN and
FAD, whereas in eukaryotes two enzymes are required for the same purpose. FMN and FAD …

New treatments for diseases caused by antimicrobial-resistant microorganisms can be
developed by identifying unexplored therapeutic targets and by designing efficient drug …

Listeria monocytogenes is riboflavin auxotrophic, but it has two genes envisaged to
transform riboflavin into FMN and FAD after its uptaked by specialized transporters. One …

The biosynthesis of the flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD),
cofactors used by 2% of proteins, occurs through the sequential action of two ubiquitous …

Riboflavin kinases (RFKs) catalyse the phosphorylation of riboflavin to produce FMN. In
most bacteria this activity is catalysed by the C-terminal module of a bifunctional enzyme …