7512-17-6 Usage
Description
N-Acetyl-D-Glucosamine (GlcNAc) is a monosaccharide derivative of glucose, playing a crucial role in various biological processes and possessing significant therapeutic potential. It is a component of heterogenous polysaccharides, such as murein and hyaluronic acid, and is involved in post-translational protein modification. GlcNAc exhibits anti-inflammatory properties and is considered a potential drug for treating osteoarthritis.
Uses
Used in Pharmaceutical Applications:
N-Acetyl-D-Glucosamine is used as a pharmaceutical compound for the treatment of osteoarthritis and inflammatory bowel disease (IBD), including ulcerative colitis and Crohn's disease. It acts as a cytoprotective agent, restoring the integrity and normal function of mucous membranes in humans.
Used in Cosmetic Applications:
GlcNAc is used as a valuable ingredient in cosmetics for improving skin wrinkles and color. It enhances the proliferation and collagen expression of fibroblasts and reduces hyperpigmentation.
Used in Drug Development Research:
N-Acetyl-D-Glucosamine is used as a substrate in sialic acid production and serves as an acceptor substrate for galactosyltransferases. It is also used to identify, differentiate, and characterize N-acetyl-β-D-hexoaminidase(s) and in the development of novel drug delivery systems.
Used in Food Supplement Applications:
GlcNAc is used in multiple applications, including drug development and as a component of food supplements, based on a newly described bio-wave model.
Used in the Identification and Characterization of Enzymes:
N-Acetyl-D-glucosamine is used to identify, differentiate, and characterize N-acetyl-beta-D-hexoaminidase, which is involved in various biological processes.
Used in the Production of Sialic Acids:
GlcNAc is an important substrate for the production of sialic acids, which are essential components of many biological molecules.
Used in the Study of Alzheimer's Disease:
Levels of O-GlcNAcylation proteins from Alzheimer's disease brain extracts are decreased compared to controls, suggesting that the release of GlcNAc may contribute to the pathogenesis of the disease.
Used in the Regulation of Gene Expression:
In E. coli, GlcNAc induces the expression of multidrug exporter genes, indicating that this sugar can alter gene expression.
Used in the Treatment of Microbial Infections:
GlcNAc is a valuable component in the development of chemicals that inhibit the incorporation of GlcNAc into chitin, which is found in fungi and many invertebrates. These chemicals are cytotoxic to these organisms, making them potential treatments for various infections.
Used in the Study of Metabolic Disorders:
D-GlcNAc inhibits purified hexokinase, which is involved in glucose metabolism and obesity, suggesting its potential use in studying and treating metabolic disorders.
Flammability and Explosibility
Notclassified
Biochem/physiol Actions
N-Acetylglucosamine (GlcNAc) oligomer may have the ability to initiate factors for canine polymorphonuclear cells (PMN) in vivo. It possesses wound healing and chemotactic activity. GlcNAc and its derivatives are usually employed in preparing dietary supplements and also used in therapeutic development.
Check Digit Verification of cas no
The CAS Registry Mumber 7512-17-6 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,5,1 and 2 respectively; the second part has 2 digits, 1 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 7512-17:
(6*7)+(5*5)+(4*1)+(3*2)+(2*1)+(1*7)=86
86 % 10 = 6
So 7512-17-6 is a valid CAS Registry Number.
InChI:InChI=1/C8H15NO6/c1-4(12)9-5(2-10)7(14)8(15)6(13)3-11/h2,5-8,11,13-15H,3H2,1H3,(H,9,12)
7512-17-6Relevant articles and documents
Synthesis and anti-acetylcholinesterase activities of novel glycosyl coumarylthiazole derivatives
Cao, Lian-Gong,Cao, Zhi-Ling,Jiang, Kai-Jun,Liu, Shu-Hao,Liu, Wei-Wei,Lu, Xing,Shao, Zhong-Bai,Shi, Da-Hua,Wang, Lei,Wang, You-Xian
, p. 359 - 364 (2020/12/28)
Eleven glycosyl coumarylthiazole derivatives are synthesized by cyclization and condensation of glycosyl thiourea with 3-bromoacetyl coumarins in ethanol. The reaction conditions are optimized and good yields of products (80%–95%) are obtained. The structures of all new products were confirmed by IR, 1H and 13C NMR, and by HRMS (electrospray ionization). The in vitro acetylcholinesterase (AChE) inhibitory activities of these new compounds are tested by Ellman’s method. Among them, N-(2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-β-D-glucopyranosyl)-4-(6-nitrocoumarinyl)-1,3-thiazole-2-amine showed the best activity with an in vitro AChE inhibitory rate of 58% and an IC50 value of 12 ± 0.38 μg/mL.
Synthesis and anticholinesterase activities of novel glycosyl benzoxazole derivatives
Cao, Zhi-Ling,Liu, Shu-Hao,Liu, Wei-Wei,Ren, Shu-Ting,Shi, Da-Hua,Wang, Lei,Wang, You-Xian,Wu, Yu-Ran
, p. 363 - 366 (2020/02/05)
Eight glycosyl benzoxazole derivatives are synthesized by nucleophilic addition reactions of glycosyl isothiocyanate with o-aminophenol in tetrahydrofuran. The reaction conditions are optimized, and good yields (86%–94%) were obtained. The structures of all new products are confirmed by infrared, 1H nuclear magnetic resonance, and high-resolution mass spectrometry (electrospray ionization). In addition, the in vitro cholinesterase inhibitory activities of these new compounds are tested by Ellman’s method.
Biochemical Characterization and Structural Analysis of a β- N-Acetylglucosaminidase from Paenibacillus barengoltzii for Efficient Production of N-Acetyl- d -glucosamine
Liu, Yihao,Jiang, Zhengqiang,Ma, Junwen,Ma, Shuai,Yan, Qiaojuan,Yang, Shaoqing
, p. 5648 - 5657 (2020/06/03)
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.