ArticleFrontiers in chemistry2015
Remaining challenges in cellular flavin cofactor homeostasis and flavoprotein biogenesis.
Article in Frontiers in chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Triokinase/FMN Cyclase: A Bifunctional Enzyme Linking Metabolism, Stress Responses and Disease.Biology · 2026Review
- A familial case of FLAD1 protein deficiency associated with impaired adrenal steroidogenesis.JCI insight · 2026Article
- Tissue-Specific Transcriptomic Profiling of Vitamin-Dependent Mitochondrial Pathways in Female Buffalo.Cell biochemistry and biophysics · 2026Article
- Cyclic-FMN Is a Detectable, Putative Intermediate of FAD Metabolism.Biomolecules · 2026Article
- Rescuing Ischemic Brain Injury by Rewiring Mitochondrial Electron Flow.bioRxiv : the preprint server for biology · 2025Article
- Revitalising Riboflavin: Unveiling Its Timeless Significance in Human Physiology and Health.Foods (Basel, Switzerland) · 2024Review
- Pharmacophore Virtual Screening Identifies Riboflavin as an Inhibitor of the Schistosome Cathepsin B1 Protease with Antiparasitic Activity.ACS omega · 2024Article
- Mini-encyclopedia of mitochondria-relevant nutraceuticals protecting health in primary and secondary care-clinically relevant 3PM innovation.The EPMA journal · 2024Article
- Cryptochromes in mammals: a magnetoreception misconception?Frontiers in physiology · 2023Review
- Riboflavin kinase and pyridoxine 5'-phosphate oxidase complex formation envisages transient interactions for FMN cofactor delivery.Frontiers in molecular biosciences · 2023Article
- Advances in Human Mitochondria-Based Therapies.International journal of molecular sciences · 2022Review
- Article
- The Nutraceutical Alliin From Garlic Is a Novel Substrate of the Essential Amino Acid Transporter LAT1 (SLC7A5).Frontiers in pharmacology · 2022Article
- The structural and functional roles of the flavin cofactor FAD in mammalian cryptochromes.Frontiers in molecular biosciences · 2022Review
- Enhanced small green fluorescent proteins as a multisensing platform for biosensor development.Frontiers in bioengineering and biotechnology · 2022Article
- Regulation of Heme Synthesis by Mitochondrial Homeostasis Proteins.Frontiers in cell and developmental biology · 2022Review
- Nutrients to Improve Mitochondrial Function to Reduce Brain Energy Deficit and Oxidative Stress in Migraine.Nutrients · 2021Review
- Molecular mechanism of interactions between ACAD9 and binding partners in mitochondrial respiratory complex I assembly.iScience · 2021Article
- Subcellular Localization of Fad1p inLife (Basel, Switzerland) · 2021Article
- Alteration of Flavin Cofactor Homeostasis in Human Neuromuscular Pathologies.Methods in molecular biology (Clifton, N.J.) · 2021Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The primary role of the water-soluble vitamin B2 (riboflavin) in cell biology is connected with its conversion into FMN and FAD, the cofactors of a large number of dehydrogenases, oxidases and reductases involved in a broad spectrum of biological activities, among which energetic metabolism and chromatin remodeling. Subcellular localisation of FAD synthase (EC 2.7.7.2, FADS), the second enzyme in the FAD forming pathway, is addressed here in HepG2 cells by confocal microscopy, in the frame of its relationships with kinetics of FAD synthesis and delivery to client apo-flavoproteins. FAD synthesis catalyzed by recombinant isoform 2 of FADS occurs via an ordered bi-bi mechanism in which ATP binds prior to FMN, and pyrophosphate is released before FAD. Spectrophotometric continuous assays of the reconstitution rate of apo-D-aminoacid oxidase with its cofactor, allowed us to propose that besides its FAD synthesizing activity, hFADS is able to operate as a FAD "chaperone." The physical interaction between FAD forming enzyme and its clients was further confirmed by dot blot and immunoprecipitation experiments carried out testing as a client either a nuclear lysine-specific demethylase 1 (LSD1) or a mitochondrial dimethylglycine dehydrogenase (Me2GlyDH, EC 1.5.8.4). Both enzymes carry out similar reactions of oxidative demethylation, in which tetrahydrofolate is converted into 5,10-methylene-tetrahydrofolate. A direct transfer of the cofactor from hFADS2 to apo-dimethyl glycine dehydrogenase was also demonstrated. Thus, FAD synthesis and delivery to these enzymes are crucial processes for bioenergetics and nutri-epigenetics of liver cells.
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