The Dimer-of-Trimers Assembly Prevents Catalysis at the Transferase Site of Prokaryotic FAD Synthase.
Sign Up to like & getrecommendations! Published in 2018 at "Biophysical journal"
DOI: 10.1016/j.bpj.2018.08.011
Abstract: Flavin mononucleotide (FMN) and flavin-adenine dinucleotide (FAD) are essential flavoprotein cofactors. A riboflavin kinase (RFK) activity catalyzes riboflavin phosphorylation to FMN, which can then be transformed into FAD by an FMN:adenylyltransferase (FMNAT) activity. Two enzymes… read more here.
Keywords: dimer; catalysis; dimer trimers; fad synthase ... See more keywords
Retrograde response to mitochondrial dysfunctions associated to LOF variations in FLAD1 exon 2: unraveling the importance of RFVT2
Sign Up to like & getrecommendations! Published in 2022 at "Free Radical Research"
DOI: 10.1080/10715762.2022.2146501
Abstract: Abstract Flavin adenine dinucleotide (FAD) synthase (EC 2.7.7.2), encoded by human flavin adenine dinucleotide synthetase 1 (FLAD1), catalyzes the last step of the pathway converting riboflavin (Rf) into FAD. FLAD1 variations were identified as a… read more here.
Keywords: fad synthase; retrograde; rfvt2; synthase deficiency ... See more keywords