Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius
Crystals, 2019 Flavin dependent monooxygenases catalyze various reactions to play a key role in biological processes, such as catabolism, detoxification, and biosynthesis.
Hyunjin Moon +2 more
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Cofactors and pathogens: Flavin mononucleotide and flavin adenine dinucleotide (FAD) biosynthesis by the FAD synthase from Brucella ovis. [PDF]
IUBMB Life, 2022 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 activities: a riboflavinkinase (RFK) that phosphorylates the riboflavin ...
Moreno A +5 more
europepmc +2 more sources
Unravelling interactions between active site residues and DMAP in the initial steps of prenylated flavin mononucleotide biosynthesis catalyzed by PaUbiX [PDF]
, 2022 Background Prenylated flavin mononucleotide (prFMN) is a recently discovered, heavily modified flavin compound. It is the only known cofactor that enables enzymatic 1,3-dipolar cycloaddition reactions. It is produced by enzymes from the UbiX family, from
Szymon, Zaczek +1 more
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QM/MM Modeling of the Flavin Functionalization in the RutA Monooxygenase
Molecules, 2023 Oxygenase activity of the flavin-dependent enzyme RutA is commonly associated with the formation of flavin-oxygen adducts in the enzyme active site. We report the results of quantum mechanics/molecular mechanics (QM/MM) modeling of possible reaction ...
Bella Grigorenko +2 more
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FEBS Open Bio, 2021 In this study, we investigated the stereospecificity of hydride transfer from NADH to flavin mononucleotide (FMN) in reactions catalyzed by the FMN‐dependent NADH‐indigo reductase expressed by thermophilic Bacillus smithii.
Kazunari Yoneda +3 more
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Exploring the functional residues in a flavin-binding fluorescent protein using deep mutational scanning. [PDF]
PLoS ONE, 2014 Flavin mononucleotide (FMN)-based fluorescent proteins are versatile reporters that can monitor various cellular processes in both aerobic and anaerobic conditions.
HyeonSeok Shin +6 more
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Frontiers in Molecular Biosciences, 2023 Enzymes catalysing sequential reactions have developed different mechanisms to control the transport and flux of reactants and intermediates along metabolic pathways, which usually involve direct transfer of metabolites from an enzyme to the next one in ...
Maribel Rivero +15 more
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Generation of the Camptothecin Scaffold by a Flavin-Catalyzed Photooxidative Skeletal Reorganization. [PDF]
Angew Chem Int Ed EnglThe biosynthetic pathway of the anticancer drug precursor camptothecin involves an enigmatic skeletal reorganization from a 6/5/6 tetrahydro‐β‐carboline to a 6/6/5 pyrroloquinoline ring system. Here, we show that this transformation can be achieved by photooxidation with flavin cofactors, such as flavin mononucleotide (FMN) as catalysts.
Liu S +6 more
europepmc +3 more sources
Production of riboflavin and related cofactors by biotechnological processes
Microbial Cell Factories, 2020 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 pharmaceutical industries.
Shuang Liu +3 more
doaj +1 more source
Chemosensors, 2023 Flavin mononucleotides (FMNs) and flavin adenine nucleotide (FAD) play vital roles in the electron-transfer processes in diverse enzymatic reactions.
Yawen Liu +5 more
doaj +1 more source