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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Protein Glycosylation01:25

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Screening Glycosyltransferases for Polyphenol Modifications.

Nele Ilmberger1, Ulrich Rabausch2

  • 1Microbiology and Biotechnology, Biocenter Klein Flottbek, University of Hamburg, Ohnhorststr. 18, 22609, Hamburg, Germany.

Methods in Molecular Biology (Clifton, N.J.)
|December 1, 2016
PubMed
Summary

Researchers developed a new metagenome screen to find enzymes that add sugars to flavonoids. This method enhances flavonoid properties like solubility and stability, aiding in the discovery of beneficial plant compounds.

Keywords:
BiotransformationFlavonoidGlycosyltransferaseMETATLC

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Area of Science:

  • Biochemistry
  • Enzymology
  • Metagenomics

Background:

  • Flavonoids are plant compounds with health benefits, including antimicrobial and antioxidative effects.
  • Glycosylation of flavonoids can improve their solubility, stability, and bioavailability.
  • Glycosyltransferases are enzymes capable of regioselective glycosylation.

Purpose of the Study:

  • To establish a functional metagenome screen for discovering novel flavonoid glycosylating enzymes.
  • To identify enzymes that modify plant secondary metabolites.

Main Methods:

  • Development of a function-based metagenome screen.
  • Utilizing thin-layer chromatography (TLC) for analysis of culture supernatant extracts.
  • Employing biotransformation reactions to detect enzymatic modifications.

Main Results:

  • Successful establishment of a screening method for identifying glycosylating enzymes.
  • Demonstration of the screen's capability to detect other modifications like methylation.
  • The method allows for the discovery of novel modifying enzymes from environmental DNA.

Conclusions:

  • The developed metagenome screen is effective for discovering enzymes involved in glycosylation and other modifications.
  • This approach facilitates the identification of enzymes that can enhance the properties of beneficial molecules like flavonoids.
  • The screening technique offers a powerful tool for enzyme discovery in metagenomic libraries.