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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
Synthesis of Phosphatidylcholine in the ER Membrane01:27

Synthesis of Phosphatidylcholine in the ER Membrane

The ER synthesizes lipids for building cell membranes and performing cellular functions such as energy storage and signaling. The lipid synthesis machinery embedded in the ER membrane primarily collects all reactants from the cytosol. Following synthesis, the secretory pathway and the ER contact sites distribute these lipids to other cellular organelles. Additionally, the energy-rich triacylglycerides are transported from the ER via lipid droplets.
The major components of all eukaryotic cell...

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High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles
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High-throughput Synthesis of Carbohydrates and Functionalization of Polyanhydride Nanoparticles

Published on: July 6, 2012

Dolichol-phosphate mannose synthase: structure, function and regulation.

Yusuke Maeda1, Taroh Kinoshita

  • 1Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan.

Biochimica Et Biophysica Acta
|April 5, 2008
PubMed
Summary

Protein glycosylation, a key modification, involves N- and O-linked pathways, GPI-anchors, and C-mannosylation. This review details dolichol-phosphate-mannose biosynthesis and the mammalian enzyme complex.

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Published on: July 6, 2012

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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Glycosylation is a major post-translational modification impacting protein structure, function, and localization.
  • It occurs in the endoplasmic reticulum and Golgi apparatus, involving N-linked, O-linked, GPI-anchor, and C-mannosylation pathways.
  • These pathways utilize either sequential monosaccharide addition or en bloc transfer of lipid-linked oligosaccharides.

Purpose of the Study:

  • To review the biosynthesis of dolichol-phosphate-mannose.
  • To focus on the mammalian enzyme complex responsible for this process.
  • To provide insight into the mechanisms of protein glycosylation.

Main Methods:

  • Literature review of glycosylation pathways.
  • Focus on enzyme complexes involved in dolichol-phosphate-mannose synthesis.
  • Analysis of sugar donor types (nucleotide-sugars and dolichol-phosphate-sugars).

Main Results:

  • Glycosyltransferases are categorized by sugar donor type.
  • Dolichol-phosphate-sugars are crucial for all four glycosylation pathways.
  • The review specifically examines the mammalian enzyme complex in dolichol-phosphate-mannose biosynthesis.

Conclusions:

  • Dolichol-phosphate-mannose biosynthesis is a critical step in protein glycosylation.
  • Understanding the mammalian enzyme complex is key to elucidating glycosylation mechanisms.
  • This review highlights the importance of sugar donors in protein modification.