Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

96
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
96
Amino Acid Catabolism01:18

Amino Acid Catabolism

78
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
78
Hydrolysis01:15

Hydrolysis

106.8K
Overview
Hydrolysis is a chemical reaction in which the addition of water breaks down a polymer into its simpler monomer units. For example, peptides break into amino acids, carbohydrates into simple sugars, and DNA into nucleotides. Enzymes often facilitate these processes.
Hydrolysis Reverses Dehydration Synthesis
Complex carbohydrates can be broken down by breaking the bonds between individual sugar units. The reaction breaks a glycosidic bond as water is added to the compound. The...
106.8K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.9K
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...
2.9K
Proteoglycans01:05

Proteoglycans

4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.0K
Lipid Catabolism01:25

Lipid Catabolism

119
Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...
119

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Human milk oligosaccharide mediates mutualism between Escherichia coli and Bifidobacterium bifidum.

Nature communications·2026
Same author

PNGaseL from <i>Flavobacterium akiainvivens</i> targets a diverse range of N-glycan structures.

Royal Society open science·2025
Same author

Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion.

Nature microbiology·2025
Same author

A sweet feast.

Nature chemical biology·2022
Same author

Plant <i>N</i>-glycan breakdown by human gut <i>Bacteroides</i>.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

Prominent members of the human gut microbiota express endo-acting O-glycanases to initiate mucin breakdown.

Nature communications·2020

Related Experiment Video

Updated: Aug 2, 2025

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
08:26

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

Published on: June 25, 2018

6.7K

N-glycan breakdown by bacterial CAZymes.

Lucy I Crouch1

  • 1Institute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham B15 2TT, U.K.

Essays in Biochemistry
|April 17, 2023
PubMed
Summary

Microbes use carbohydrate-active enzymes (CAZymes) to break down N-glycans, which modify proteins and aid cell interactions. Studying these CAZymes offers insights into microbial metabolism and new tools for glycoprotein modification.

Keywords:
CAZymesN-glycanhuman gut microbes

More Related Videos

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

36.8K
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

518

Related Experiment Videos

Last Updated: Aug 2, 2025

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+
08:26

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

Published on: June 25, 2018

6.7K
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

36.8K
Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
13:35

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota

Published on: May 23, 2025

518

Area of Science:

  • Biochemistry and Microbiology
  • Glycobiology

Background:

  • N-glycans are crucial post-translational modifications with diverse biological roles, including protein protection and cell-cell interactions.
  • Microorganisms possess carbohydrate-active enzymes (CAZymes) that degrade various N-glycan structures.
  • CAZymes from different microbial niches (commensals and pathogens) have been identified, hinting at specialized functions.

Purpose of the Study:

  • To explore the diversity and specificity of microbial CAZymes targeting N-glycans.
  • To understand how CAZyme specificity relates to microbial metabolic strategies and substrate utilization.
  • To highlight the potential of N-glycan-specific CAZymes as biotechnological tools.

Main Methods:

  • Characterization of CAZymes from various microbial sources.
  • Analysis of CAZyme substrate specificity against different N-glycan structures.
  • Investigating potential cross-feeding mechanisms mediated by N-glycan breakdown products.

Main Results:

  • Identification of microbial CAZymes with varying specificities for N-glycans.
  • Correlation between CAZyme profiles and microbial ecological niches.
  • Demonstration of N-glycan deconstruction by microbial enzymes.

Conclusions:

  • Microbial CAZymes play a significant role in N-glycan metabolism.
  • CAZyme specificity provides insights into microbial ecology and metabolic interactions.
  • N-glycan-specific CAZymes represent valuable tools for glycoprotein engineering and research.