Discovery and mechanism of intestinal bacteria in enzymatic cleavage of C-C glycosidic bonds

Appl Microbiol Biotechnol. 2020 Mar;104(5):1883-1890. doi: 10.1007/s00253-019-10333-z. Epub 2020 Jan 13.

Abstract

C-Glycosides, a special type of glycoside, are frequently distributed in many kinds of medicinal plants, such as puerarin and mangiferin, showing various and significant bioactivities. C-Glycosides are usually characterized by the C-C bond that forms between the anomeric carbon of sugar moieties and the carbon atom of aglycon, which is usually resistant against acidic hydrolysis and enzymatic treatments. Interestingly, C-glycosides could be cleaved by several intestinal bacteria, but whether the enzymatic cleavage of C-C glycosidic bond is reduction or hydrolysis has been controversial; furthermore, whether existence of a "C-glycosidase" directly catalyzing the cleavage is not clear. Here we review research advances about the discovery and mechanism of intestinal bacteria in enzymatic cleavage of C-C glycosidic bond with an emphasis on the identification of enzymes manipulation the deglycosylation. Finally, we give a brief conclusion about the mechanism of C-glycoside deglycosylation and perspectives for future study in this field.

Keywords: C-glycosides; C–C glycosidic bond; Deglycosylation; Intestinal bacteria; Puerarin.

Publication types

  • Review

MeSH terms

  • Animals
  • Bacteria / enzymology*
  • Bacteria / isolation & purification
  • Bacteria / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biotransformation
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism*
  • Glycosides / chemistry
  • Glycosides / metabolism*
  • Glycosylation
  • Humans
  • Intestines / microbiology*
  • Molecular Structure

Substances

  • Bacterial Proteins
  • C-glycoside
  • Glycosides
  • Glycoside Hydrolases