ArticleScientific reports2015
Structural analysis of fungus-derived FAD glucose dehydrogenase.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 127 citations in OpenAlex.
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- Preliminary Investigation on Salivary Enzymes of Massese Sheep.Animals : an open access journal from MDPI · 2026Article
- Electrochemical tyrosine-click bioconjugation enables multiplexed cytokine sensing and immunoprofiling in native serum.Nature communications · 2026Article
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- Insights into the Lignocellulose-Degrading Enzyme System Based on the Genome Sequence ofInternational journal of molecular sciences · 2025Article
- Electrochemical Small-Angle X-ray Scattering for Potential-Dependent Structural Analysis of Redox Enzymes.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Does Acinetobacter calcoaceticus glucose dehydrogenase produce self-damaging H2O2?Bioscience reports · 2024Article
- Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases.Biotechnology for biofuels and bioproducts · 2024Article
- Exploration and Application of DNA-Binding Proteins to Make a Versatile DNA-Protein Covalent-Linking Patch (D-Pclip): The Case of a Biosensing Element.Journal of the American Chemical Society · 2024Article
- Development of a Versatile Method to Construct Direct Electron Transfer-Type Enzyme Complexes Employing SpyCatcher/SpyTag System.International journal of molecular sciences · 2023Article
- Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.Biomolecules · 2022Review
- Characterization of Fungal FAD-Dependent AA3_2 Glucose Oxidoreductases from Hitherto Unexplored Phylogenetic Clades.Journal of fungi (Basel, Switzerland) · 2021Article
- Crystal structure and functional characterization of an oligosaccharide dehydrogenase from Pycnoporus cinnabarinus provides insights into fungal breakdown of lignocellulose.Biotechnology for biofuels · 2021Article
- Electrochemical quantification of accelerated FADGDH rates in aqueous nanodroplets.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum.Acta crystallographica. Section D, Structural biology · 2021Article
- Orientated Immobilization of FAD-Dependent Glucose Dehydrogenase on Electrode by Carbohydrate-Binding Module Fusion for Efficient Glucose Assay.International journal of molecular sciences · 2021Article
- A Tandem Solar Biofuel Cell: Harnessing Energy from Light and Biofuels.Angewandte Chemie (International ed. in English) · 2021Article
- Early Transcriptome Response ofFrontiers in fungal biology · 2021Article
- TargetingBiology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the first three-dimensional structure of fungus-derived glucose dehydrogenase using flavin adenine dinucleotide (FAD) as the cofactor. This is currently the most advanced and popular enzyme used in glucose sensor strips manufactured for glycemic control by diabetic patients. We prepared recombinant nonglycosylated FAD-dependent glucose dehydrogenase (FADGDH) derived from Aspergillus flavus (AfGDH) and obtained the X-ray structures of the binary complex of enzyme and reduced FAD at a resolution of 1.78 Å and the ternary complex with reduced FAD and D-glucono-1,5-lactone (LGC) at a resolution of 1.57 Å. The overall structure is similar to that of fungal glucose oxidases (GOxs) reported till date. The ternary complex with reduced FAD and LGC revealed the residues recognizing the substrate. His505 and His548 were subjected for site-directed mutagenesis studies, and these two residues were revealed to form the catalytic pair, as those conserved in GOxs. The absence of residues that recognize the sixth hydroxyl group of the glucose of AfGDH, and the presence of significant cavity around the active site may account for this enzyme activity toward xylose. The structural information will contribute to the further engineering of FADGDH for use in more reliable and economical biosensing technology for diabetes management.
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