C-Glycoside metabolism in the gut and in nature: Identification, characterization, structural analyses and distribution of C-C bond-cleaving enzymes

Takahiro Mori, Takuto Kumano, Haibing He, Satomi Watanabe, Miki Senda, Toshio Moriya, Naruhiko Adachi, Sanae Hori, Yuzu Terashita, Masato Kawasaki, Yoshiteru Hashimoto, Takayoshi Awakawa, Toshiya Senda (), Ikuro Abe () and Michihiko Kobayashi ()
Additional contact information
Takahiro Mori: Graduate School of Pharmaceutical Sciences, The University of Tokyo
Takuto Kumano: Graduate School of Life and Environmental Sciences, University of Tsukuba
Haibing He: Graduate School of Pharmaceutical Sciences, The University of Tokyo
Satomi Watanabe: Graduate School of Life and Environmental Sciences, University of Tsukuba
Miki Senda: Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Toshio Moriya: Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Naruhiko Adachi: Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Sanae Hori: Graduate School of Life and Environmental Sciences, University of Tsukuba
Yuzu Terashita: Graduate School of Life and Environmental Sciences, University of Tsukuba
Masato Kawasaki: Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Yoshiteru Hashimoto: Graduate School of Life and Environmental Sciences, University of Tsukuba
Takayoshi Awakawa: Graduate School of Pharmaceutical Sciences, The University of Tokyo
Toshiya Senda: Structural Biology Research Center, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK)
Ikuro Abe: Graduate School of Pharmaceutical Sciences, The University of Tokyo
Michihiko Kobayashi: Graduate School of Life and Environmental Sciences, University of Tsukuba

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract C-Glycosides, in which a sugar moiety is linked via a carbon-carbon (C-C) bond to a non-sugar moiety (aglycone), are found in our food and medicine. The C-C bond is cleaved by intestinal microbes and the resulting aglycones exert various bioactivities. Although the enzymes responsible for the reactions have been identified, their catalytic mechanisms and the generality of the reactions in nature remain to be explored. Here, we present the identification and structural basis for the activation of xenobiotic C-glycosides by heterocomplex C-deglycosylation enzymes from intestinal and soil bacteria. They are found to be metal-dependent enzymes exhibiting broad substrate specificity toward C-glycosides. X-ray crystallographic and cryo-electron microscopic analyses, as well as structure-based mutagenesis, reveal the structural details of these enzymes and the detailed catalytic mechanisms of their remarkable C-C bond cleavage reactions. Furthermore, bioinformatic and biochemical analyses suggest that the C-deglycosylation enzymes are widely distributed in the gut, soil, and marine bacteria.

Date: 2021
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-021-26585-1 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26585-1

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-26585-1

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().