ArticleInternational journal of molecular sciences2012
Bacterial over-expression and purification of the 3'phosphoadenosine 5'phosphosulfate (PAPS) reductase domain of human FAD synthase: functional characterization and homology modeling.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 25 citations in OpenAlex.
- Metabolism of FAD, FMN and riboflavin (vitamin B2) in the human parasitic blood fluke Schistosoma mansoni.BMC infectious diseases · 2024Article
- Metabolism of FAD, FMN and riboflavin (vitamin B2) in the human parasitic blood flukebioRxiv : the preprint server for biology · 2024Article
- New insights into the nutritional genomics of adult-onset riboflavin-responsive diseases.Nutrition & metabolism · 2023Review
- Purification of Recombinant Human 6His-FAD Synthase (Isoform 2) and Quantitation of FAD/Protein Monomer Ratio by UV-Vis Spectra.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Alteration of Flavin Cofactor Homeostasis in Human Neuromuscular Pathologies.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Continuous and Discontinuous Approaches to Study FAD Synthesis and Degradation Catalyzed by Purified Recombinant FAD Synthase or Cellular Fractions.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Development of Novel Experimental Models to Study Flavoproteome Alterations in Human Neuromuscular Diseases: The Effect of Rf Therapy.International journal of molecular sciences · 2020Review
- Riboflavin Deficiency-Implications for General Human Health and Inborn Errors of Metabolism.International journal of molecular sciences · 2020Review
- Insights into the FMNAT Active Site of FAD Synthase: Aromaticity is Essential for Flavin Binding and Catalysis.International journal of molecular sciences · 2020Article
- Mutation of Aspartate 238 in FAD Synthase Isoform 6 Increases the Specific Activity by Weakening the FAD Binding.International journal of molecular sciences · 2019Article
- A Novel Truncating FLAD1 Variant, Causing Multiple Acyl-CoA Dehydrogenase Deficiency (MADD) in an 8-Year-Old Boy.JIMD reports · 2019Article
- Bacterial Production, Characterization and Protein Modeling of a Novel Monofuctional Isoform of FAD Synthase in Humans: An Emergency Protein?Molecules (Basel, Switzerland) · 2018Article
- Riboflavin transport and metabolism in humans.Journal of inherited metabolic disease · 2016Review
- Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency.American journal of human genetics · 2016Article
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5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
FAD synthase (FADS, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor, FAD. Human FADS is organized in two domains: -the 3'phosphoadenosine 5'phosphosulfate (PAPS) reductase domain, similar to yeast Fad1p, at the C-terminus, and -the resembling molybdopterin-binding domain at the N-terminus. To understand whether the PAPS reductase domain of hFADS is sufficient to catalyze FAD synthesis, per se, and to investigate the role of the molybdopterin-binding domain, a soluble "truncated" form of hFADS lacking the N-terminal domain (Δ(1-328)-hFADS) has been over-produced and purified to homogeneity as a recombinant His-tagged protein. The recombinant Δ(1-328)-hFADS binds one mole of FAD product very tightly as the wild-type enzyme. Under turnover conditions, it catalyzes FAD assembly from ATP and FMN and, at a much lower rate, FAD pyrophosphorolytic hydrolysis. The Δ(1-328)-hFADS enzyme shows a slight, but not significant, change of K(m) values (0.24 and 6.23 µM for FMN and ATP, respectively) and of k(cat) (4.2 × 10-2 s-1) compared to wild-type protein in the forward direction. These results demonstrate that the molybdopterin-binding domain is not strictly required for catalysis. Its regulatory role is discussed in light of changes in divalent cations sensitivity of the Δ(1-328)-hFADS versus wild-type protein.
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