ArticleMolecular microbiology2010
Identification and characterization of two families of F420 H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 168 citations in OpenAlex.
- Biodegradation of Aflatoxins by Four Novel Environmental Bacterial Isolates: A Comparative Genomic and Molecular Docking-Proof-of-Concept Study.Foods (Basel, Switzerland) · 2026Article
- Enhancing the Substrate Adaptability of Laccase through Ancestral Sequence Reconstruction for Applications in Mycotoxin Detoxification.Journal of agricultural and food chemistry · 2025Article
- Intestinal Microecological Mechanisms of Aflatoxin B1 Degradation by Black Soldier Fly Larvae (Animals : an open access journal from MDPI · 2025Review
- Enzymatic detoxification of major mycotoxins: current status, challenges, and future prospective.Mycotoxin research · 2025Review
- A Review of Research Progress on the Microbial or Enzymatic Degradation and Mechanism of Aflatoxin B1.Journal of microbiology and biotechnology · 2025Review
- Exploring Large Protein Sequence Space through Homology- and Representation-based Hierarchical Clustering.Molecular biology and evolution · 2025Article
- Comparative Genomic and Transcriptomic Analysis Provides New Insights into the Aflatoxin BMicroorganisms · 2025Article
- Degradation and detoxification of aflatoxin B1 by two peroxidase enzymes from Irpex lacteus F17.Bioprocess and biosystems engineering · 2025Article
- Pilot Scale Production of a FBiotechnology journal · 2025Article
- Flavin and deazaflavin biosynthesis in mycobacteria: relevance to physiology, implications for drug discovery, MR-1 antigenicity, and vaccine development.Frontiers in immunology · 2025Review
- Article
- Glucose-6-phosphate dehydrogenase and its 3D structures from crystallography and electron cryo-microscopy.Acta crystallographica. Section F, Structural biology communications · 2024Review
- Aflatoxin Biodetoxification Strategies Based on Postbiotics.Probiotics and antimicrobial proteins · 2024Review
- Aflatoxin B1 Control by VariousToxins · 2024Article
- Identification of a Novel Aflatoxin BToxins · 2024Article
- Bioenzymatic detoxification of mycotoxins.Frontiers in microbiology · 2024Review
- Detoxification of aflatoxin B1 by aFrontiers in microbiology · 2024Article
- Mechanisms by which microbial enzymes degrade four mycotoxins and application in animal production: A review.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2023Review
- Recombinant Oxidase fromToxins · 2023Article
- Isolation and Optimization of Aflatoxin BToxins · 2023Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aflatoxins are polyaromatic mycotoxins that contaminate a range of food crops as a result of fungal growth and contribute to serious health problems in the developing world because of their toxicity and mutagenicity. Although relatively resistant to biotic degradation, aflatoxins can be metabolized by certain species of Actinomycetales. However, the enzymatic basis for their breakdown has not been reported until now. We have identified nine Mycobacterium smegmatis enzymes that utilize the deazaflavin cofactor F(420) H(2) to catalyse the reduction of the α,β-unsaturated ester moiety of aflatoxins, activating the molecules for spontaneous hydrolysis and detoxification. These enzymes belong to two previously uncharacterized F(420) H(2) dependent reductase (FDR-A and -B) families that are distantly related to the flavin mononucleotide (FMN) dependent pyridoxamine 5'-phosphate oxidases (PNPOxs). We have solved crystal structures of an enzyme from each FDR family and show that they, like the PNPOxs, adopt a split barrel protein fold, although the FDRs also possess an extended and highly charged F(420) H(2) binding groove. A general role for these enzymes in xenobiotic metabolism is discussed, including the observation that the nitro-reductase Rv3547 from Mycobacterium tuberculosis that is responsible for the activation of bicyclic nitroimidazole prodrugs belongs to the FDR-A family.
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