28446-21-1

Basic information

• Product Name: N-acetylglucosamine-1-phosphate
• Synonyms: N-acetylglucosamine-1-phosphate
• CAS NO: 28446-21-1
• Molecular Weight: 301.19
• Mol File: 28446-21-1.mol
• Article Data: 5

Chemical Properties

• CAS DataBase Reference: N-acetylglucosamine-1-phosphate(CAS DataBase Reference)
• NIST Chemistry Reference: N-acetylglucosamine-1-phosphate(28446-21-1)
• EPA Substance Registry System: N-acetylglucosamine-1-phosphate(28446-21-1)

Safety Data

• Hazardous Substances Data: 28446-21-1(Hazardous Substances Data)

Upstream product

• 14200-67-0 N,N'-diacetylchitobiose 
• 10036-64-3 N-acetyl-D-glucosamine 
• 56-65-5 ATP 
• 3006-60-8 2-acetamido-1,3,4,6-tetra-O-acetyl-2-deoxy-β-D-glucopyranose 
• 7512-17-6 N-Acetyl-D-glucosamine 
• 2152-75-2 2-amino-2-deoxy-D-glucopyranose-1-(dihydrogen phosphate) 
• 72-89-9 S-acetyl coenzyme A 
• 18191-20-3 N-acetyl-D-glucosamine-6-phosphate 
• 3068-34-6 Acetic acid (2R,3S,4R,5R,6R)-3-acetoxy-2-acetoxymethyl-5-acetylamino-6-chloro-tetrahydro-pyran-4-yl ester 
• 35946-68-0 O³,O⁴,O⁶-triacetyl-2-amino-O¹-diphenoxyphosphoryl-2-deoxy-α-D-glucopyranose; hydrochloride 

Downstream Products

• 528-04-1 uridine 5'-diphospho-N-acetylglucosamine 
• 16426-39-4 uridine diphosphate N-acetylglucosamine 
• 16426-39-4 UDP-α-D-N-acetylglucosamine 

Relevant articles and documents

Biocatalytic synthesis of uridine 5′-diphosphate N-acetylglucosamine by multiple enzymes co-immobilized on agarose beads

Recombinant N-acetylglucosamine kinase, pyruvate kinase, N-acetylglucosamine phosphate mutase, uridine 5′-diphosphate N-acetylglucosamine pyrophosphorylase, and inorganic pyrophosphatase were overexpressed in E. coli and co-immobilized on agarose beads for the practical synthesis of uridine 5′-diphosphate N-acetylglucosamine.

Facile enzymatic synthesis of sugar 1-phosphates as substrates for phosphorylases using anomeric kinases

Three sugar 1-phosphates that are donor substrates for phosphorylases were produced at the gram scale from phosphoenolpyruvic acid and the corresponding sugars by the combined action of pyruvate kinase and the corresponding anomeric kinases in good yields. These sugar 1-phosphates were purified through two electrodialysis steps. α-d-Galactose 1-phosphate was finally isolated as crystals of dipotassium salts. α-d-Mannose 1-phosphate and 2-acetamido-2-deoxy-α-d-glucose 1-phosphate were isolated as crystals of bis(cyclohexylammonium) salts.

One-step synthesis of labeled sugar nucleotides for protein O-GlcNAc modification studies by chemical function analysis of an archaeal protein

Herein we present the chemical function analysis of a recombinant sugar nucleotidyltransferase from the hyperthermophile Pyrococcus furiosus and its use in the one-pot synthesis of chloroacetyl- and alkyne-tagged analogues of uridinediphospho-N-acetylglucosamine (UDP-GlcNAc). The gene was originally annotated as a glucose-1-phosphate deoxythymidylyltransferase; however, kinetic analysis of a panel of sugar-1-phosphates with the protein shows that it is better described as a bifunctional protein that synthesizes UDP-GlcNAc from glucosamine-1-phosphate and acetyl coenzyme A (CoA). A new mass-spectrometry-based assay for the rapid analysis of the acyltransferase activity demonstrates that the enzyme can also accept cheaper truncated N-acetylcysteamine thioester substrates in place of the natural acetyl CoA. The enzyme can tolerate alkyne or chloride substitutions in the acyl moiety, thereby allowing the facile synthesis of tagged sugar nucleotides for future use in protein O-GlcNAc modification studies. Copyright