Enzymatic β-elimination in natural product O- and C-glycoside deglycosylation

Johannes Bitter, Martin Pfeiffer, Annika J. E. Borg, Kirill Kuhlmann, Tea Pavkov-Keller, Pedro A. Sánchez-Murcia and Bernd Nidetzky ()
Additional contact information
Johannes Bitter: Graz University of Technology, NAWI Graz
Martin Pfeiffer: Graz University of Technology, NAWI Graz
Annika J. E. Borg: Graz University of Technology, NAWI Graz
Kirill Kuhlmann: University of Graz, NAWI Graz
Tea Pavkov-Keller: University of Graz, NAWI Graz
Pedro A. Sánchez-Murcia: Medical University of Graz
Bernd Nidetzky: Graz University of Technology, NAWI Graz

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract Biological degradation of natural product glycosides involves, alongside hydrolysis, β-elimination for glycosidic bond cleavage. Here, we discover an O-glycoside β-eliminase (OGE) from Agrobacterium tumefaciens that converts the C3-oxidized O-β-d-glucoside of phloretin (a plant-derived flavonoid) into the aglycone and the 2-hydroxy-3-keto-glycal elimination product. While unrelated in sequence, OGE is structurally homologous to, and shows effectively the same Mn2+ active site as, the C-glycoside deglycosylating enzyme (CGE) from a human intestinal bacterium implicated in β-elimination of 3-keto C-β-d-glucosides. We show that CGE catalyzes β-elimination of 3-keto O- and C-β-d-glucosides while OGE is specific for the O-glycoside substrate. Substrate comparisons and mutagenesis for CGE uncover positioning of aglycone for protonic assistance by the enzyme as critically important for C-glycoside cleavage. Collectively, our study suggests convergent evolution of active site for β-elimination of 3-keto O-β-d-glucosides. C-Glycoside cleavage is a specialized feature of this active site which is elicited by substrate through finely tuned enzyme-aglycone interactions.

Date: 2023
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-42750-0 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:14:y:2023:i:1:d:10.1038_s41467-023-42750-0

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

DOI: 10.1038/s41467-023-42750-0

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 ().