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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.
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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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Peptidoglycan Synthesis01:28

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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...
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Proteoglycans01:05

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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,...
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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...
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N-Glycan Engineering: Constructing the N-GlcNAc Stump.

Qifan Wu1, Suwei Dong2, Weimin Xuan1,3

  • 1State Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin, 300071, P. R. China.

Chembiochem : a European Journal of Chemical Biology
|August 17, 2022
PubMed
Summary
This summary is machine-generated.

Generating homogeneous N-glycosylated proteins is crucial for research and therapeutics. Endoglycosidase-catalyzed transglycosylation converts N-acetylglucosamine (N-GlcNAc) on proteins into uniform glycosylation patterns, overcoming natural heterogeneity.

Keywords:
N-acetylglucosaminesN-glycosylationendoglycosidasesglycoproteinstransglycosylation

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Area of Science:

  • Biochemistry and Molecular Biology
  • Glycobiology
  • Protein Chemistry

Background:

  • N-Glycosylation is vital for protein structure and function.
  • Natural N-glycosylated proteins display significant glycan heterogeneity, complicating research and therapeutic use.
  • Existing methods for producing homogeneous N-glycoproteins are limited.

Purpose of the Study:

  • To review methods for generating N-acetylglucosamine (N-GlcNAc) and analogues on proteins and peptides.
  • To highlight the potential of endoglycosidase-catalyzed transglycosylation for creating homogeneous N-glycoproteins.
  • To discuss current challenges and future opportunities in homogeneous N-glycoprotein synthesis.

Main Methods:

  • Overview of synthetic, enzymatic, and chemoenzymatic strategies for N-glycoprotein modification.
  • Focus on endoglycosidase-catalyzed transglycosylation using N-GlcNAc as a 'tree stump' acceptor.
  • Discussion of methods for introducing N-GlcNAc or its analogues onto proteins and peptides.

Main Results:

  • Endoglycosidase-catalyzed transglycosylation enables the conversion of a single N-GlcNAc residue into diverse homogeneous N-glycans.
  • This approach effectively addresses the heterogeneity issue found in naturally occurring N-glycosylated proteins.
  • The generation of homogeneous N-glycans on proteins and peptides is feasible through described methods.

Conclusions:

  • Homogeneous N-glycosylation of proteins is achievable using enzymatic transglycosylation methods.
  • This strategy offers significant advantages for both fundamental research and therapeutic applications of N-glycoproteins.
  • Further research is needed to overcome current challenges and fully exploit opportunities in this field.