Flavin mononucleotide synthase

Flavin mononucleotide synthase is not a standard or canonical name for any known protein or therapeutic target. The correct term for the enzyme that catalyzes the conversion of flavin mononucleotide (FMN) to flavin adenine dinucleotide (FAD) is FAD synthase or FMN adenylyltransferase, encoded by the gene FLAD1 in humans[2][5]. This enzyme plays a crucial role in cellular metabolism by producing FAD, an essential cofactor for numerous redox enzymes. In mammals and yeast, two separate enzymes—riboflavin kinase and FMN adenylyltransferase—sequentially convert riboflavin to FMN and then to FAD. In most prokaryotes, these activities are combined into a single bifunctional protein called FADS[5]. There are no approved drugs directly targeting this enzyme, nor is it considered a direct therapeutic target at present. The submitted name "Flavin mononucleotide synthase" appears incorrect because it does not correspond to an established molecular entity; rather, it likely refers mistakenly either to riboflavin kinase ("flavin mononucleotide synthetASE") or more accurately to "FAD synthASE" ("flavin adenine dinucleotide synthetASE"), which uses FMN as substrate[2][5].

Other names

FAD synthaseFMN adenylyltransferaseFAD synthetaseFLAD1 (gene encoding human enzyme)ATP:FMN adenylyltransferaseRiboflavin kinase/FMNAT (in prokaryotes, as bifunctional enzyme)