Mannotriose-di-(N-acetyl-D-glucosamine) NEW

Mannotriose-di-(N-acetyl-D-glucosamine) is an oligosaccharide composed of three mannose (mannotriose) units and two N-acetyl-D-glucosamine (GlcNAc) residues. Here's a structured breakdown:

Mannotriose Backbone:

• A trisaccharide consisting of three mannose molecules linked by glycosidic bonds. Common linkages in biological systems include α-1,2, α-1,3, or α-1,6 configurations, though the exact positions are not specified in the name.

  N-Acetyl-D-Glucosamine (GlcNAc) Units:

• Two GlcNAc residues are attached to the mannotriose. GlcNAc is a glucose derivative with an N-acetylated amine group, often involved in glycosidic bonds via β-linkages (e.g., β-1,4 in chitobiose).

  Structural Context:

• Likely resembles components of N-linked glycans found in glycoproteins. The core structure of N-linked glycosylation typically includes a trimannose (mannotriose) attached to a chitobiose unit (two GlcNAc residues via β-1,4 linkages). This compound may represent a fragment or simplified version of this core.

• Potential biological roles include participation in protein folding, cell-cell recognition, or immune responses.

  Possible Linkages:

• The GlcNAc units could be linked to the mannotriose in various configurations (e.g., one at each end or branched on a central mannose). In N-glycans, the first GlcNAc is β-1,4-linked to the second GlcNAc, which is β-1,4-linked to the first mannose of the trimannose core.

  Biological Relevance:

• Found in eukaryotic glycoproteins, potentially as part of the endoplasmic reticulum (ER) processing pathway or in microbial cell wall components (though distinct from peptidoglycan, which contains alternating GlcNAc and muramic acid).

Summary: This compound is a carbohydrate structure integral to complex glycosylation processes, particularly in forming the core of N-linked glycoproteins. Its exact function and linkage specificity depend on the biological context, but it exemplifies the structural complexity of glycans in cellular systems.