Structural and Functional Characterization of a Gene Cluster Responsible for Deglycosylation of C-glucosyl Flavonoids and Xanthonoids by Deinococcus aerius
Open accessAbstract
Plant C-glycosylated aromatic polyketides are important for plant and animal health. These are specialized metabolites that perform functions both within the plant, and in interaction with soil or intestinal microbes. Despite the importance of these plant compounds, there is still limited knowledge of how they are metabolized. The Gram-positive aerobic soil bacterium Deinococcus aerius strain TR0125 and other Deinococcus species thrive in a wide range of harsh environments. In this work, we identified a C-glycoside deglycosylation gene cluster in the genome of D. aerius. The cluster includes three genes coding for a GMC-type oxidoreductase (DaCGO1) that oxidizes the glucosyl C3 position in aromatic C-glucosyl compounds, which in turn provides the substrate for the C-glycoside deglycosidase (DaCGD; composed of α+β subunits) that cleaves the glucosyl-aglycone C-C bond. Our results from size-exclusion chromatography, single particle cryo-electron microscopy and X-ray crystallography show that DaCGD is an α 2 β 2 heterotetramer, which represents a novel oligomeric state among bacterial CGDs. Importantly, the high-resolution X-ray structure of DaCGD provides valuable insights into the activation of the catalytic hydroxide ion by Lys261. DaCGO1 is specific for the 6-C-glucosyl flavones isovitexin, isoorientin and the 2-C-glucosyl xanthonoid mangiferin, and the subsequent C-C-bond cleavage by DaCGD generated apigenin, luteolin and norathyriol, respectively. Of the substrates tested,…
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The gut microbiota serves a critical role in the deglycosylation and subsequent metabolism of MGF, representing a key determinant of its systemic availability and pharmacological effects.
“The gut microbiota serves a critical role in the deglycosylation and subsequent metabolism of MGF, representing a key determinant of its systemic availability and pharmacological effects (24).”
From Mangiferin in human disease: Multifaceted mechanisms and applications (Review) (2026) · cites this paper as [24]
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- Authors
- Furlanetto, V., Kalyani, D. C., Kostelac, A., Puc, J., Haltrich, D., Hällberg, B. M., & Divne, C.
- Affiliations
- KTH Royal Institute of Technology (SE)
- BOKU University (AT)
- Karolinska Institutet (SE)
- Corresponding author
- Divne, Christina
- ORCID
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2024-05
- Volume
- 436
- Issue
- 9
- Pages
- 168547
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W4392907664
- Cited by
- 9
- References
- 61
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 4
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Molecular Biology (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- KTH Royal Institute of Technology
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Biochemical and biochemical processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Keywords
- enzyme structure, isovitexin, isoorientin, mangiferin, apigenin, luteolin, norathyriol, soil bacteria
- MeSH terms
- Bacterial Proteins, Flavonoids, Genes, Bacterial, Multigene Family, Glycosides, Glycosylation, Models, Molecular, Crystallography, X-Ray, Deinococcus, Xanthones
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