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| Names | |
|---|---|
| IUPAC name β-D-(Acetylamino)-2-deoxy-glucopyranose | |
| Other names N-Acetyl-D-glucosamine GlcNAc NAG | |
| Identifiers | |
3D model (JSmol) | |
| 1247660 | |
| ChEBI | |
| ChEMBL | |
| ChemSpider |
|
| ECHA InfoCard | 100.028.517 |
| EC Number |
|
| 721281 | |
| KEGG | |
| UNII | |
| |
| |
| Properties | |
| C8H15NO6 | |
| Molar mass | 221.21 |
| Melting point | 211 |
| Related compounds | |
Related Monosaccharides | N-Acetylgalactosamine |
Related compounds | Glucosamine Glucose |
Except where otherwise noted, data are given for materials in theirstandard state (at 25 °C [77 °F], 100 kPa). | |
N-Acetylglucosamine (GlcNAc) is anamide derivative of themonosaccharideglucose. It is a secondary amide betweenglucosamine andacetic acid. It is significant in several biological systems.
It is part of a biopolymer in the bacterialcell wall, which is built from alternating units of GlcNAc andN-acetylmuramic acid (MurNAc), cross-linked witholigopeptides at thelactic acid residue of MurNAc. This layered structure is calledpeptidoglycan (formerly called murein).
GlcNAc is the monomeric unit of thepolymerchitin, which forms theexoskeletons ofarthropods likeinsects andcrustaceans. It is the main component of theradulas ofmollusks, thebeaks ofcephalopods, and a major component of thecell walls of mostfungi.
Polymerized withglucuronic acid, it formshyaluronan.
GlcNAc has been reported to be an inhibitor ofelastase release from humanpolymorphonuclear leukocytes (range 8–17% inhibition), however this is much weaker than the inhibition seen withN-acetylgalactosamine (range 92–100%).[1]
It has been proposed as a treatment forautoimmune diseases and recent tests have claimed some success.[2][3]
O-GlcNAcylation is the process of adding a singleN-acetylglucosamine sugar to theserine orthreonine of a protein.[4] Comparable tophosphorylation, addition or removal ofN-acetylglucosamine is a means of activating or deactivating enzymes ortranscription factors.[4] In fact,O-GlcNAcylation and phosphorylation often compete for the same serine/threonine sites.[4]O-GlcNAcylation most often occurs onchromatin proteins, and is often seen as a response to stress.[4]
Hyperglycemia increasesO-GlcNAcylation, leading toinsulin resistance.[5] IncreasedO-GlcNAcylation due to hyperglycemia is evidently a dysfunctional form ofO-GlcNAcylation.O-GlcNAcylation decline in the brain with age is associated withcognitive decline. WhenO-GlcNAcylation was increased in thehippocampus of aged mice,spatial learning and memory improved.[6]
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| Biochemistry andecology |
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