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Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria
by
Yang, Pengjie
, Zhang, Peng
, Hong, Sen
, Yang, Gaohua
, Sun, Yuwei
, Gu, Yang
, Wang, Yong
, Jiang, Weihong
in
38
/ 631/326/325/1506
/ 631/45/173
/ 631/45/535/1266
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Catabolism
/ Clostridiales - enzymology
/ Clostridiales - genetics
/ Crystal structure
/ Crystallography, X-Ray
/ Flavones
/ Flavones - metabolism
/ Flavonoids
/ Flavonols
/ Flavonols - metabolism
/ Gastrointestinal Microbiome - physiology
/ Genetic analysis
/ Homology
/ Humanities and Social Sciences
/ Hydrogenation
/ Medicinal plants
/ Metabolism
/ Microorganisms
/ Molecular modelling
/ Molecular structure
/ multidisciplinary
/ Nutrition
/ Oxidoreductases - genetics
/ Oxidoreductases - isolation & purification
/ Oxidoreductases - metabolism
/ Oxidoreductases - ultrastructure
/ Phylogeny
/ Polyphenols
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Reductase
/ Reductases
/ Science
/ Science (multidisciplinary)
/ Structural analysis
2021
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Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria
by
Yang, Pengjie
, Zhang, Peng
, Hong, Sen
, Yang, Gaohua
, Sun, Yuwei
, Gu, Yang
, Wang, Yong
, Jiang, Weihong
in
38
/ 631/326/325/1506
/ 631/45/173
/ 631/45/535/1266
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Catabolism
/ Clostridiales - enzymology
/ Clostridiales - genetics
/ Crystal structure
/ Crystallography, X-Ray
/ Flavones
/ Flavones - metabolism
/ Flavonoids
/ Flavonols
/ Flavonols - metabolism
/ Gastrointestinal Microbiome - physiology
/ Genetic analysis
/ Homology
/ Humanities and Social Sciences
/ Hydrogenation
/ Medicinal plants
/ Metabolism
/ Microorganisms
/ Molecular modelling
/ Molecular structure
/ multidisciplinary
/ Nutrition
/ Oxidoreductases - genetics
/ Oxidoreductases - isolation & purification
/ Oxidoreductases - metabolism
/ Oxidoreductases - ultrastructure
/ Phylogeny
/ Polyphenols
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Reductase
/ Reductases
/ Science
/ Science (multidisciplinary)
/ Structural analysis
2021
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Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria
by
Yang, Pengjie
, Zhang, Peng
, Hong, Sen
, Yang, Gaohua
, Sun, Yuwei
, Gu, Yang
, Wang, Yong
, Jiang, Weihong
in
38
/ 631/326/325/1506
/ 631/45/173
/ 631/45/535/1266
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Catabolism
/ Clostridiales - enzymology
/ Clostridiales - genetics
/ Crystal structure
/ Crystallography, X-Ray
/ Flavones
/ Flavones - metabolism
/ Flavonoids
/ Flavonols
/ Flavonols - metabolism
/ Gastrointestinal Microbiome - physiology
/ Genetic analysis
/ Homology
/ Humanities and Social Sciences
/ Hydrogenation
/ Medicinal plants
/ Metabolism
/ Microorganisms
/ Molecular modelling
/ Molecular structure
/ multidisciplinary
/ Nutrition
/ Oxidoreductases - genetics
/ Oxidoreductases - isolation & purification
/ Oxidoreductases - metabolism
/ Oxidoreductases - ultrastructure
/ Phylogeny
/ Polyphenols
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Reductase
/ Reductases
/ Science
/ Science (multidisciplinary)
/ Structural analysis
2021
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Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria
Journal Article
Discovery of an ene-reductase for initiating flavone and flavonol catabolism in gut bacteria
2021
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Overview
Gut microbial transformations of flavonoids, an enormous class of polyphenolic compounds abundant in plant-based diets, are closely associated with human health. However, the enzymes that initiate the gut microbial metabolism of flavones and flavonols, the two most abundant groups of flavonoids, as well as their underlying molecular mechanisms of action remain unclear. Here, we discovered a flavone reductase (FLR) from the gut bacterium,
Flavonifractor plautii
ATCC 49531 (originally assigned as
Clostridium orbiscindens
DSM 6740), which specifically catalyses the hydrogenation of the C2–C3 double bond of flavones/flavonols and initiates their metabolism as a key step. Crystal structure analysis revealed the molecular basis for the distinct catalytic property of FLR. Notably, FLR and its widespread homologues represent a class of ene-reductases that has not been previously identified. Genetic and biochemical analyses further indicated the importance of FLR in gut microbial consumption of dietary and medicinal flavonoids, providing broader insight into gut microbial xenobiotic transformations and possible guidance for personalized nutrition and medicine.
Flavonoids are abundant polyphenols in plants but it is not well understood how their metabolism is initiated by microbes in the human gut. Here, the authors identify and characterise an ene-reductase from the gut bacterium,
Flavonifractor plautii
ATCC 49531 that catalyses the hydrogenation of the C2–C3 double bond of flavones and flavonols and present its crystal structure.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Bacteria
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Bacterial Proteins - ultrastructure
/ Flavones
/ Gastrointestinal Microbiome - physiology
/ Homology
/ Humanities and Social Sciences
/ Oxidoreductases - isolation & purification
/ Oxidoreductases - metabolism
/ Oxidoreductases - ultrastructure
/ Recombinant Proteins - genetics
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Recombinant Proteins - ultrastructure
/ Science
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