91183-98-1 Usage
Description
UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT, also known as Uridine-5'-diphospho-N-acetylglucosamine sodium salt, is a chemical compound that plays a crucial role in various biological processes. It is a nucleotide sugar that serves as a substrate for enzymes involved in the biosynthesis of glycoproteins and glycolipids. Its unique structure and properties make it a valuable tool in scientific research and various applications across different industries.
Uses
Used in Chemical Research:
UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT is used as a chemical reagent in studies relating to the synthesis of immunogens. It aids in understanding the mechanisms of immune responses and the development of vaccines and therapeutic agents.
Used in Enzyme Activity Assays:
As a GlcNAc transferase substrate, UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT is utilized in assays to evaluate the activity of enzymes involved in the transfer of N-acetylglucosamine residues to proteins and other molecules. This helps in studying the role of these enzymes in various biological processes and their potential as therapeutic targets.
Used in Endoplasmic Reticulum to Golgi Transport Assay:
In this application, UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT serves as a component of the reaction cocktail, enabling researchers to investigate the transport mechanisms of proteins and lipids between the endoplasmic reticulum and Golgi apparatus. This knowledge is essential for understanding cellular functions and the development of targeted therapies.
Used in Quantification of UDP-GlcNAc in Liver Tissues:
As a reference standard, UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT is employed in high-performance liquid chromatography (HPLC) to quantify UDP-GlcNAc levels in liver tissues. This helps in assessing the metabolic status of the liver and the involvement of UDP-GlcNAc in various liver diseases.
Used in Testing the Glycosylation Activity of O-GlcNAc Transferase (OGT):
UDP-ALPHA-D-N-ACETYLGLUCOSAMINE, DISODIUM SALT is used to evaluate the glycosylation activity of OGT against peptide substrates. This is crucial for understanding the role of OGT in the regulation of protein function and its implications in various diseases, including diabetes and neurodegenerative disorders.
Biochem/physiol Actions
Uridine 5′-diphospho-N-acetylglucosamine (UDP-GlcNAc) is a sugar donor and aids in the endomembrane glycosylation of endoplasmic reticulum and Golgi. The decreased levels of UDP-GlcNAc has an influence on the normal cellular proliferation and apoptosis. UDP-GlcNAc elicits feedback inhibition of the enzyme glutamine:fructose-6-phosphate amidotransferase (GFAT).
Check Digit Verification of cas no
The CAS Registry Mumber 91183-98-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,1,1,8 and 3 respectively; the second part has 2 digits, 9 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 91183-98:
(7*9)+(6*1)+(5*1)+(4*8)+(3*3)+(2*9)+(1*8)=141
141 % 10 = 1
So 91183-98-1 is a valid CAS Registry Number.
91183-98-1Relevant articles and documents
Chemoenzymatic synthesis of uridine diphosphate-GlcNAc and uridine diphosphate-GalNAc analogs for the preparation of unnatural glycosaminoglycans
Masuko, Sayaka,Bera, Smritilekha,Green, Dixy E.,Weiwer, Michel,Liu, Jian,Deangelis, Paul L.,Linhardt, Robert J.
experimental part, p. 1449 - 1456 (2012/03/11)
Eight N-acetylglucosamine-1-phosphate and N-acetylgalactosamine-1-phosphate analogs have been synthesized chemically and were tested for their recognition by the GlmU uridyltransferase enzyme. Among these, only substrates that have an amide linkage to the C-2 nitrogen were transferred by GlmU to afford their corresponding uridine diphosphate(UDP)-sugar nucleotides. Resin-immobilized GlmU showed comparable activity to nonimmobilized GlmU and provides a more facile final step in the synthesis of an unnatural UDP-donor. The synthesized unnatural UDP-donors were tested for their activity as substrates for glycosyltransferases in the preparation of unnatural glycosaminoglycans in vitro. A subset of these analogs was useful as donors, increasing the synthetic repertoire for these medically important polysaccharides.
Gram-Scale Synthesis of Uridine 5'-Diphospho-N-acetylglucosamine: Comparison of Enzymatic and Chemical Routes
Heidlas, Juergen E.,Lees, Watson J.,Pale, Patrick,Whitesides, George M.
, p. 146 - 151 (2007/10/02)
Practical chemoenzymatic and chemical routes to uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc) on a gram scale have been developed.The chemoenzymatic synthesis provided convenient access to glucosamine-6-phosphate and N-acetylglucosamine-6-phosphate (GlcNAc-6-P) in > 10 mmol quantities.The condensation between GlcNAc-6-P and UTP was catalyzed by readily available crude enzyme extract from dried cells of the yeast Candida utilis and afforded a 17 percent yield of UDP-GlcNAc from GlcNAc-6-P.The otherwise straightforward chemoenzymatic sequence was hampered by the need to purify the product from the final complex reaction mixture.The chemical synthesis of UDP-GlcNAc proceeded through five steps in an overall yield of 15 percent from pentaacetylglucosamine with the selective formation of tetraacetylglucosamine-α-1-phosphate as the key reaction.
