10036-64-3

Usage

Uses

Used in Research Applications:
N-ACETYL-ALPHA-D-GLUCOSAMINE is used as a research chemical compound for studying various biological processes and molecular interactions. It plays a crucial role in understanding the structure and function of glycoconjugates, which are essential for numerous cellular functions, including cell adhesion, signaling, and immune response.
Used in Pharmaceutical Industry:
N-ACETYL-ALPHA-D-GLUCOSAMINE is used as a building block for the synthesis of various pharmaceutical compounds, including antibiotics, antifungals, and antiviral agents. Its unique structure allows for the development of novel drugs with improved efficacy and reduced side effects.
Used in Diagnostic Industry:
NAG is used as a diagnostic marker for various diseases, such as kidney and liver dysfunction, as well as certain types of cancer. Its presence in biological samples can be detected and quantified, providing valuable information for disease diagnosis and monitoring.
Used in Cosmetics Industry:
N-ACETYL-ALPHA-D-GLUCOSAMINE is used as an active ingredient in the cosmetics industry, particularly in skin care products. It is known to promote skin hydration, improve skin elasticity, and reduce the appearance of fine lines and wrinkles. Additionally, NAG has been shown to have anti-inflammatory and antimicrobial properties, making it a valuable component in various cosmetic formulations.
Used in Food Industry:
NAG is used in the food industry as a natural sweetener and a source of dietary fiber. Its unique properties make it an attractive alternative to traditional sugars, offering potential health benefits such as improved gut health and reduced glycemic response.
Used in Biotechnology Industry:
N-ACETYL-ALPHA-D-GLUCOSAMINE is used in the biotechnology industry for the development of novel biomaterials and drug delivery systems. Its ability to interact with various biological molecules makes it a promising candidate for the design of targeted drug delivery systems and tissue engineering applications.

InChI:InChI=1/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5+,6+,7-,8-/m0/s1

Upstream product

• 19342-33-7 N-acetyl neuraminic acid 
• 528-04-1 uridine 5'-diphospho-N-acetylglucosamine 
• 1337923-38-2 4,6-dimethoxy-1,3,5-triazin-2-yl α-N-acetylglucosaminide 
• 42890-21-1 2-acetamido-2-deoxy-D-mannose diethyl dithioacetal 
• 7732-18-5 water 
• 2776-93-4 2-acetamido-1-N-(L-β-aspartyl)-2-deoxy-β-D-glucopyranosylamine 
• 108-24-7 acetic anhydride 
• 2776-93-4 2-acetamido-1-N-(L-aspart-4-oyl)-2-deoxy-β-D-glucopyranosylamine 
• 80265-04-9 4-methylumbelliferyl 2-acetamido-2-deoxy-α-D-glucopyranoside 
• 22595-97-7 2-acetamido-2-deoxy-3,4:5,6-di-O-isopropylidene-aldehydo-D-glucose 
• 13319-32-9 chitotriose 
• 1078691-95-8 (+)-D-glucosamine hydrochloride 
• 7284-16-4 p-nitrophenyl 2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→4)-2-acetamido-2-deoxy-β-D-glucopyranoside 
• 3459-18-5 4-nitrophenyl N-acetyl-β-D-glucosaminide 

Downstream Products

• 3006-60-8 1,3,4,6-tetra-O-acetyl-2-acetamido-2-deoxy-α,β-D-mannopyranose 
• 131-48-6 N-Acetylneuraminic acid 
• 14635-94-0 2-amino-2-deoxy-D-mannitol 
• 209977-51-5 β-D-galactopyranosyl-(1->6)-2-acetamido-2-deoxy-β-D-mannopyranose 
• 209977-51-5 β-D-galactopyranosyl-(1->6)-2-acetamido-2-deoxy-α-D-mannopyranose 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 58546-02-4 2-acetamido-2,3-dideoxy-α-D-erythro-hex-2-enofuranose 
• 1262206-14-3 2-acetamido-3,6-anhydro-2-deoxy-β-D-mannofuranose 
• 34972-56-0 2-acetamido-3,6-anhydro-2-deoxy-α-D-mannofuranose 
• 144846-62-8 2-acetamido-3,6-anhydro-2-deoxy-β-D-glucofuranose 
• 144846-61-7 2-acetamido-3,6-anhydro-2-deoxy-α-D-glucofuranose 
• 10378-06-0 2-methyl-(3,4,6-tri-O-acetyl-1,2-dideoxy-β-D-mannopyrano)-[2,1:4',5']-2-oxazoline 
• 1379001-47-4 C₂₀H₂₄N₂O₁₁ 
• 1379001-48-5 o-nitrophenyl 2-acetamido-2-deoxy-α-D-mannopyranoside 

Relevant academic research and scientific papers

Isolation and structures of erylosides from the carribean sponge Erylus formosus

Nine new triterpene glycosides, erylosides F1-F4 (1-4), M (5), N (6), O (7), P (8), and Q (9), along with previously known erylosides F (10) and H (11) were isolated from the sponge Erylus formosus collected from the Mexican Gulf (Puerto Morelos, Mexico). Structures of 1-4 were determined as the corresponding biosides having aglycons related to penasterol with additional oxidation patterns in their side chains. Erylosides 5-9 contain new variants of carbohydrate chains with three (5, 6), four (7), and six (8, 9) sugar units, respectively. Erylosides 5, 7, 8, and 6, 9 contain 14-carboxy-24-methylenelanost-8(9)-en-3β-ol and penasterol as aglycons, respectively. In contrast with its epimer 2, the compound 3 induced the early apoptosis of Ehrlich carcinoma cells at a concentration of 100 μg/mL, while 1 and 10 activated the Ca2+ influx into mouse spleenocytes (130% of the control) at the same doses.

Effect of sub- and supercritical water pretreatment on enzymatic degradation of chitin

We examined the effect of sub- and supercritical water pretreatment (300-400 °C, 0.5-15 min) on enzymatic degradation of chitin to N,N′-diacetylchitobiose (GlcNAc)2. The yield of (GlcNAc) 2 by enzymatic degradation of supercritical water pretreated chitin at 400 °C for 1.0 min was up to 37%, compared to 5% without the pretreatment. X-ray diffraction (XRD) analysis revealed that the d-spacing and the crystallite size increased by sub- and supercritical water pretreatment, which is indicative of swelling of the chitin. The swelling of the chitin crystal structure improved enzymatic degradation by allowing the enzymes easy access to the chitin.

Separation of yeast asparagine-linked oligosaccharides by high-performance anion-exchange chromatography.

Oligosaccharides obtained from Saccharomyces cerevisiae mannoproteins by digestion with endo-N-acetyl-beta-D-glucosaminidase H were fractionated by anion-exchange chromatography, by elution with 50-100mM NaOH without or with a sodium-acetate gradient, and detected with a pulsed amperometric detector (PAD). The elution times of homologous oligosaccharides fell on a straight line having a slope characteristic of the structural type. The response of the PAD detector per mole of oligosaccharide increased about 2-fold going from Man3GlcNAc to Man13GlcNAc, and appeared to depend primarily on the oxidation of the reducing-end N-acetylglucosamine unit common to all the oligosaccharides. The digestion of a Man10GlcNAc with jack-bean alpha-mannosidase was monitored by injecting portions of the crude reaction mixture, and the intermediates were characterized by their elution positions and n.m.r. spectra in the anomeric proton region. One commercial jack-bean alpha-mannosidase preparation contained a novel endolytic activity that released N-acetylglucosamine from the reducing ends of the oligosaccharides and was shown to convert P----6 alpha Man----6 alpha Man----6 beta Man----4 alpha beta GlcNAc to P----6 alpha Man----6 alpha Man----6 alpha beta Man plus free N-acetylglucosamine. Another commercial jack-bean alpha-mannosidase converted the Man10GlcNAc to a Man3GlcNAc having the structure alpha Man----6 beta Man----4 alpha beta GlcNAc, [formula: see text] whereas the Oerskovia sp. alpha-mannosidase converted the same oligosaccharide to a Man4GlcNAc having the structure alpha Man----6 alpha Man----6 beta Man----4 alpha beta GlcNAc. [formula: see text]

Kinetics of acid hydrolysis of acetylglucosamine

The kinetics of acid hydrolysis of N-acetylglucosamine at different temperatures and reagent concentrations was studied. A mathematical model of the hydrolysis was proposed. The rate constant and activation energy of deacetylation were calculated.

Production of N-acetyl-D-glucosamine from β-chitin by enzymatic hydrolysis

N-Acetyl-D-glucosamine, which is a focusing material for the improvement of osteoarthritis, was obtained from β-chitin by enzymatic hydrolysis in high yield (76%).

Structure of a new pseudaminic acid-containing capsular polysaccharide of Acinetobacter baumannii LUH5550 having the KL42 capsule biosynthesis locus

The capsular polysaccharide from Acinetobacter baumannii LUH5550 was studied by 1D and 2D 1H and 13C NMR spectroscopy. The following structure of the branched trisaccharide repeating unit was established: (Formula presented.) where Pse5Ac7RHb indicates 5-acetamido-3,5,7,9-tetradeoxy-7-[(R)-3-hydroxybutanoylamino]-l-glycero-l-manno-non-2-ulosonic acid. The genes in the capsule biosynthesis locus designated KL42 are consistent with the structure established.

MODEL STUDIES PERTAINING TO THE HYDRAZINOLYSIS OF GLYCOPEPTIDES AND GLYCOPROTEINS: HYDRAZINOLYSIS OF THE 1-N-ACETYL AND 1-N-(L-β-ASPARTYL) DERIVATIVES OF 2-ACETAMIDO-2-DEOXY-β-D-GLUCOPYRANOSYLAMINE

The products of hydrazinolysis of the 1-N-acetyl and 1-N-(L-β-aspartyl) derivatives of 2-acetamido-2-deoxy-β-D-glucopyranosylamine could not be converted quantitatively into 2-amino-2-deoxy-D-glucose under mild conditions.Proton and (13)C-n.m.r. measurements indicated that the hydrazone of 2-amino-2-deoxy-D-glucose was a major product of the hydrazinolysis of 2-acetamido-1-N-acetyl-2-deoxy-β-D-glucopyranosylamine.Control experiments showed that acetohydrazide is slowly converted into 4-amino-3,5-dimethyl-1,2,4-triazole under the conditions of hydrazinolysis, and hat 2-amino-2-deoxy-D-glucose reacts slowly with acetohydrazide in dilute acetic acid.The implications of these results in relation to the hydrazinolysis of glycopeptides and glycoproteins are discussed.

Synthesis and biological activity of glycosyl-1H-1,2,3-triazoles

Glycosyl 1,2,3-triazoles with α-d-gluco, β-d-gluco, α-d-galacto, β-d-galacto and β-2-acetamido-2-deoxygluco (GlcNAc) stereochemistry were prepared by reaction of the corresponding azides with vinyl acetate under microwave irradiation. The deprotected glucosyl and galactosyl triazoles did not display inhibitory activity against the tested glycosidases at 1 mM. Of the four fungal glycosidases evaluated, GlcNAc-triazole was found to be hydrolyzed by Talaromyces flavus CCF 2686 β-N-acetylhexosaminidase. β-GlcNAc-triazole was furthermore established to act as a strong ligand of rat and human natural killer cell activating receptors.

Production of N-acetyl-D-glucosamine from alpha-chitin by crude enzymes from Aeromonas hydrophila H-2330.

The selective and efficient production of N-acetyl-D-glucosamine (GlcNAc) was achieved from flake type of alpha-chitin by using crude enzymes derived from Aeromonas hydrophila H-2330.

Biochemical Characterization and Structural Analysis of a β- N-Acetylglucosaminidase from Paenibacillus barengoltzii for Efficient Production of N-Acetyl- d -glucosamine

Bioproduction of N-acetyl-d-glucosamine (GlcNAc) from chitin, the second most abundant natural renewable polymer on earth, is of great value in which chitinolytic enzymes play key roles. In this study, a novel glycoside hydrolase family-18 β-N-acetylglucosaminidase (PbNag39) from Paenibacillus barengoltzii suitable for GlcNAc production was identified and biochemically characterized. It possessed a unique shallow catalytic groove (5.8 ?) as well as a smaller C-terminal domain (solvent-accessible surface area, 5.1 × 103 ?2) and exhibited strict substrate specificity toward N-acetyl chitooligosaccharides (COS) with GlcNAc as the sole product, showing a typical manner of action of β-N-acetylglucosaminidases. Thus, an environmentally friendly bioprocess for GlcNAc production from ball-milled powdery chitin by an enzyme cocktail reaction was further developed. By using the new route, the powdery chitin conversion rate increased from 23.3% (v/v) to 75.3% with a final GlcNAc content of 22.6 mg mL-1. The efficient and environmentally friendly bioprocess may have great application potential in GlcNAc production.