357979-11-4

Upstream product

• 31077-89-1 1,3,4,6-tetra-O-acetyl-2-deoxy-2-fluoro-β-D-glucopyranose 
• 48168-03-2 diphenylphosphatoxy anion 
• 141395-48-4 1,3,4,6-tetra-O-acetyl-2-deoxy-2-fluoro-α/β-D-glucopyranoside 
• 226382-58-7 3,4,6-tri-O-acetyl-2-deoxy-2-fluoro-α-D-glucopyranose 
• 2524-64-3 chlorophosphoric acid diphenyl ester 
• 108794-37-2 3,4,6-tri-O-acetyl-2-deoxy-2-fluoro-α,β-D-glucopyranose 

Relevant academic research and scientific papers

Synthesis of α-Deoxymono and Difluorohexopyranosyl 1-Phosphates and Kinetic Evaluation with Thymidylyl- and Guanidylyltransferases

Eight fluorinated isosteric α-d-glucopyranosyl 1-phosphate (Glc 1P) analogues have been synthesized. A promiscuity investigation of the thymidylyltransferase Cps2L and the guanidylyltansferase GDP-ManPP with these analogues showed that all were accepted b

Synthesis of fluorosugar reagents for the construction of well-defined fluoroglycoproteins

2-Deoxy-2-fluoroglycosyl iodides are privileged glycosyl donors for the stereoselective preparation of 1-Nu-β-fluorosugars, which are useful reagents for chemical site-selective protein glycosylation. Ready access to such β-fluorosugars enables the mild a

Substrate specificity of N-Acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, a key enzyme in the dolichol pathway

N-Acetylglucosaminyl(diphosphodolichol) N-acetylglucosaminyl transferase, also known as Enzyme II, is the second enzyme in the dolichol pathway. This pathway is responsible for the assembly of the tetradecasaccharide pyrophosphate dolichol, which is the substrate for oligosaccharyl transferase. In order to study the specificity of Enzyme II, four unnatural dolichol diphosphate monosaccharides were synthesized, with the C-2 acetamido group in the natural substrate Dol-PP-GlcNAc 1a replaced by fluoro, ethoxy, trifluoroacetamido, and amino functionalities. These analogues 1b-e were evaluated as glycosyl acceptors for Enzyme II, which catalyzes the formation of dolichol diphosphate chitobiose (Dol-PP-GlcNAc2) from UDP-GlcNAc and Dol-PP-GlcNAc. Enzyme II from pig liver was found to be highly specific for its glycosyl acceptor and the acetamido group shown to be a key functional determinant for this glycosylation reaction.