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T1 - Mammalian Glycan Biosynthesis

KW - Mammalian glycan biosynthesis, biological recognition - mammalian glycosylation mechanics

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KEGG PATHWAY: N-Glycan biosynthesis - Reference pathway

Bouhss A, Trunkfield AE, Bugg TDH and Mengin‐Lecreulx D (2008) The biosynthesis of peptidoglycan lipid‐linked intermediates. FEMS Microbiology Reviews 32: 208–233.

KW - Methodology, new technologies and

a) Glycan biosynthesis
Glycans are synthesized by enzymes called glycosyltransferases which transfer a sugar residue from an activated nucleotide sugar donor to specific acceptor molecules, forming glycosidic bonds (Breton et al.(2006)). Transfer of the sugar residue occurs with either the retention or the inversion of the configuration of the anomeric carbon (McNaught and Wilkinson (1997)). These enzymes can be found in both prokaryotes and eukaryotes, having high specificity for both the glycosyl donor as well as the acceptor substates. In this section, the major biosynthesis pathways of glycans will be introduced.
Glycosylation produces different types of glycans that are typically attached to proteins or lipids. Protein glycosylation includes N-glycans, O-glycans and glycosaminoglycans (GAGs). Lipid glycosylation includes glycolipids (glycosphingolipids) and glycosylphosphatidylinositol (GPI)-anchors. In mammalian systems, these glycans are constructed in an ordered manner through the workings of glycosyltransferases and also glycosidases, which are enzymes that remove specific glycosidic linkages from a glycan structure.





























Glycan Biosynthesis and MetabolismRelease 2

For example, N-glycan biosynthesis is shown both as a pathway map and a structure map in .

Peptidoglycan is the rigid, but flexible, macromolecule that surrounds and protects individual bacterial cells. It supplies the foundation for bacterial cell walls, defines an organism's shape and anchors protein complexes and extracellular organelles to the cell surface, all while remaining porous enough to admit essential nutrients and large compounds. Peptidoglycan fragments trigger neighbouring microorganisms to grow or to modify their own walls, serve as maturation signals for vertebrate immune systems and may be used to manipulate the immune system for the benefit of pathogenic organisms. Because it is unique to bacteria, peptidoglycan is one of the most valuable targets to which antibiotics may be directed. Although the components of peptidoglycan are known and we have a basic understanding of its biosynthesis, there remains a great deal to learn about its three‐dimensional organisation, its biological properties and activities, and how it expands and divides during bacterial growth.

The trypanosome variant surface glycoprotein (VSG), like many other eukaryotic cell surface proteins, is anchored to the plasma membrane by a glycosyl-phosphatidylinositol (GPI) moiety. This glycolipid is assembled first as a precursor (glycolipid A) that is then covalently attached to the newly synthesized polypeptide. We have developed a trypanosome cell-free system capable of performing all of the steps in the biosynthesis of the glycan portion of glycolipid A. Using [3H]sugar nucleotides as substrates, several biosynthetic intermediates have been identified. From structural analyses of these intermediates, we propose a pathway for GPI biosynthesis. Based on comparisons between the VSG GPI anchor and similar structures in other cells, we believe that this same pathway will apply to the GPI anchors, and the related insulin-mediator compound, of higher eukaryotes.

Pathways of O-glycan biosynthesis in cancer cells.

Defects in N-glycan biosynthesis lead to a variety of human diseases known as congenital disorders of glycosylation [DS:H00118 H00119].

Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol.

Metabolism1.0 Global and overview maps1.1 Carbohydrate metabolism1.2 Energy metabolism1.3 Lipid metabolism1.4 Nucleotide metabolism1.5 Amino acid metabolism1.6 Metabolism of other amino acids1.7 Glycan biosynthesis and metabolism1.8 Metabolism of cofactors and vitamins1.9 Metabolism of terpenoids and polyketides1.10 Biosynthesis of other secondary metabolites1.11 Xenobiotics biodegradation and metabolism1.12 Chemical structure transformation maps

Barreteau H, Kovac A, Boniface A et al. (2008) Cytoplasmic steps of peptidoglycan biosynthesis. FEMS Microbiology Reviews 32: 168–207.
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  • PIGP phosphatidylinositol glycan anchor biosynthesis …

    Biosynthesis of the N-Linked Glycan in Campylobacter jejuni and Addition onto Protein through Block Transfer

  • Phosphatidylinositol glycan anchor biosynthesis (PIG) …

    This gene encodes an enzyme involved in the first step of glycosylphosphatidylinositol (GPI)-anchor biosynthesis

  • Gene Family: Phosphatidylinositol glycan anchor biosynthesis ..

    O-Glycan Synthesis and Modification Return to Biosynthesis of Glycans in Eukaryotes

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Phosphatidylinositol Glycan Anchor Biosynthesis, Class …

AB - The trypanosome variant surface glycoprotein (VSG), like many other eukaryotic cell surface proteins, is anchored to the plasma membrane by a glycosyl-phosphatidylinositol (GPI) moiety. This glycolipid is assembled first as a precursor (glycolipid A) that is then covalently attached to the newly synthesized polypeptide. We have developed a trypanosome cell-free system capable of performing all of the steps in the biosynthesis of the glycan portion of glycolipid A. Using [3H]sugar nucleotides as substrates, several biosynthetic intermediates have been identified. From structural analyses of these intermediates, we propose a pathway for GPI biosynthesis. Based on comparisons between the VSG GPI anchor and similar structures in other cells, we believe that this same pathway will apply to the GPI anchors, and the related insulin-mediator compound, of higher eukaryotes.

GSEA | MSigDB | Gene Set: KEGG_N_GLYCAN_BIOSYNTHESIS

Sauvage E, Kerff F, Terrak M, Ayala JA and Charlier P (2008) The penicillin‐binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiology Reviews 32: 234–258.

Mammalian Glycan Biosynthesis: Building a Template …

N2 - The trypanosome variant surface glycoprotein (VSG), like many other eukaryotic cell surface proteins, is anchored to the plasma membrane by a glycosyl-phosphatidylinositol (GPI) moiety. This glycolipid is assembled first as a precursor (glycolipid A) that is then covalently attached to the newly synthesized polypeptide. We have developed a trypanosome cell-free system capable of performing all of the steps in the biosynthesis of the glycan portion of glycolipid A. Using [3H]sugar nucleotides as substrates, several biosynthetic intermediates have been identified. From structural analyses of these intermediates, we propose a pathway for GPI biosynthesis. Based on comparisons between the VSG GPI anchor and similar structures in other cells, we believe that this same pathway will apply to the GPI anchors, and the related insulin-mediator compound, of higher eukaryotes.

Lipids in Glycan Biosynthesis - Biochemistry of Lipids - 2.

In contrast, the structures of glycans, lipids, polyketides, nonribosomal peptides, and various secondary metabolites are determined by biosynthetic pathways.

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