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

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.0K
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...
3.0K
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
Protein Glycosylation01:25

Protein Glycosylation

7.4K
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.
Glycosylation occurs in...
7.4K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

3.9K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.9K
Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

106
Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
106
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors01:19

Oral Hypoglycemic Agents: α-Glucosidase Inhibitors

280
α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
Acarbose and miglitol are...
280

You might also read

Related Articles

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

Sort by
Same author

Development and Deployment of an Activity-Based N-Glycan Hydrolase Probe Suitable for Droplet-Based Screening.

Journal of the American Chemical Society·2026
Same author

Generation of enzyme-converted type O whole blood from type A whole blood: A translational study using swine whole blood.

Transfusion·2025
Same author

Synthesis and evaluation of carbagalactosyl 1,2-aziridines and -epoxides as glycosidase inhibitors.

Organic & biomolecular chemistry·2025
Same author

Reshaping of a Glycoside Hydrolase Active Site through Expression-Compensated Droplet-Based Microfluidic Screening Provides Useful Tools for Glycomics.

ACS central science·2025
Same author

Enzyme-converted O kidneys allow ABO-incompatible transplantation without hyperacute rejection in a human decedent model.

Nature biomedical engineering·2025
Same author

Streamlining Sulfated Oligosaccharide and Glycan Synthesis with Engineered Mutant 6-SulfoGlcNAcases.

Journal of the American Chemical Society·2025

Related Experiment Video

Updated: Sep 21, 2025

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

8.8K

Azido Groups Hamper Glycan Acceptance by Carbohydrate Processing Enzymes.

Feng Liu1, Hong-Ming Chen1, Zachary Armstrong1

  • 1Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, British Columbia V6T1Z1, Canada.

ACS Central Science
|June 1, 2022
PubMed
Summary

Azido sugars are useful biological probes, but their azide group may not mimic natural sugars. Researchers found that azide position significantly impacts enzyme processing, cautioning against using these probes for quantitative glycosylation studies.

More Related Videos

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

2.4K
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

Related Experiment Videos

Last Updated: Sep 21, 2025

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

8.8K
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

Published on: March 11, 2022

2.4K
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

Area of Science:

  • Biochemistry
  • Carbohydrate Chemistry
  • Enzymology

Background:

  • Azido sugars are widely used as probes in biological systems, including metabolic labeling and proteomic profiling.
  • The structural and size differences between azide and hydroxyl groups raise questions about how well azido sugars represent their parent molecules.

Purpose of the Study:

  • To quantitatively assess the accommodation of azide-substituted sugars by enzymes.
  • To evaluate the fidelity of azido sugar probes in representing natural sugars in enzymatic assays.

Main Methods:

  • Utilized glycosidases as model enzyme systems to study the hydrolysis of azidodeoxy glucosides and N-acetylhexosaminides.
  • Measured specificity constants for a diverse panel of glycosidases from synthetic gene and metagenomic libraries.

Main Results:

  • Azides at secondary carbon positions are poorly accommodated, leading to no substrate processing.
  • Azides at primary carbon positions are recognized by a limited number of enzymes, often with low efficiency.
  • Enzyme processing efficiency is highly dependent on the azide substitution site.

Conclusions:

  • Azido sugar probes may not accurately represent natural sugars, especially when azides are at secondary carbons.
  • Results from studies using azide-modified sugars should be interpreted with caution, particularly for quantitative assessments of glycosylation.
  • Careful selection of azide substitution sites is crucial for reliable monitoring and detection of glycosylation.