895558-57-3

Upstream product

• 358-23-6 trifluoromethylsulfonic anhydride 
• 19139-80-1 ((3aS,5R,6R,6aS)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl)methanol 
• 40429-53-6 5-O-p-toluenesulfonyl-3-O-benzyl-1,2-O-isopropylidene-β-D-arabinofuranose 
• 168103-00-2 (((3aS,5R,6R,6aS)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl)methoxy)(tert-butyl)diphenylsilane 
• 114738-04-4 (3aS,5R,6R,6aS)-5-(((tert-butyldiphenylsilyl)oxy)methyl)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-6-ol 
• 168608-39-7 (3S,4S,5R)-5-(((tert-butyldiphenylsilyl)oxy)methyl)tetrahydrofuran-2,3,4-triol 
• 532-20-7 D-arabinofuranose 
• 100-39-0 benzyl bromide 
• 40429-51-4 1,2-O-isopropylidene-5-O-toluene-p-sulphonyl-β-D-arabinofuranose 

Downstream Products

• 866878-98-0 3-((3aS,5R,6R,6aS)-6-benzyloxy-2,2-dimethyl-tetrahydrofuro[2,3-d][1,3]dioxol-5-yl)-2-(diethoxyphosphoryl)propionic acid methyl ester 
• 1607447-59-5 dibenzyl 2-(((3aS,5R,6R,6aS)-6-(benzyloxy)-2,2-dimethyltetrahydrofuro[2,3-d][1,3]dioxol-5-yl)methyl)malonate 
• 866879-14-3 [4-2H]chorismic acid 
• 866879-12-1 methyl [4-2H]shikimate 
• 786709-76-0 Benzoic acid (2R,3S)-2,3-bis-benzyloxy-3-(2-fluoromethyl-[1,3]dioxan-2-yl)-propyl ester 
• 786709-78-2 Phosphoric acid (2R,3S)-2,3-bis-benzyloxy-3-(2-fluoromethyl-[1,3]dioxan-2-yl)-propyl ester dimethyl ester 
• 786709-72-6 1-deoxy-1-fluoro-3,4-di-O-benzyl-5-O-benzoyl-D-lyxitol 
• 786709-74-8 1-deoxy-1-fluoro-3,4-di-O-benzyl-5-O-benzoyl-D-xylulose 
• 786709-77-1 (2R,3S)-2,3-Bis-benzyloxy-3-(2-fluoromethyl-[1,3]dioxan-2-yl)-propan-1-ol 
• 786709-70-4 1-deoxy-1-fluoro-3,4-di-O-benzyl-D-lyxitol 
• 786709-64-6 1-deoxy-1-fluoro-D-xylulose-5-phosphate 

Relevant academic research and scientific papers

Synthesis and biological evaluation of arabinose 5-phosphate mimics modified at position five

A set of new metabolically stable arabinose 5-phosphate analogues possessing phosphate mimetic groups at position 5 was synthesised. Their ability to interact with arabinose 5-phosphate isomerase from Pseudomonas aeruginosa was evaluated by STD-NMR studie

Phosphonate analogues of arabinose 5-phosphate: Putative ligands for arabinose 5-phosphate isomerases

Metabolically stable arabinose 5-phosphate analogues possessing phosphate mimetic groups at the 5-position were synthesized and evaluated by saturation-transfer-difference (STD) NMR studies for their ability to interact with arabinose 5-phosphate isomeras

Isotope effects on the enzymatic and nonenzymatic reactions of chorismate

The important biosynthetic intermediate chorismate reacts thermally by two competitive pathways, one leading to 4-hydroxybenzoate via elimination of the enolpyruvyl side chain, and the other to prephenate by a facile Claisen rearrangement. Measurements with isotopically labeled chorismate derivatives indicate that both are concerted sigmatropic processes, controlled by the orientation of the enolpyruvyl group. In the elimination reaction of [4- 2H]chorismate, roughly 60% of the label was found in pyruvate after 3 h at 60 °C. Moreover, a 1.846 ± 0.057 2H isotope effect for the transferred hydrogen atom and a 1.0374 ± 0.0005 18O isotope effect for the ether oxygen show that the transition state for this process is highly asymmetric, with hydrogen atom transfer from C4 to C9 significantly less advanced than C-O bond cleavage. In the competing Claisen rearrangement, a very large 18O isotope effect at the bond-breaking position (1.0482 ± 0.0005) and a smaller 13C isotope effect at the bond-making position (1.0118 ± 0.0004) were determined. Isotope effects of similar magnitude characterized the transformations catalyzed by evolutionary unrelated chorismate mutases from Escherichia coli and Bacillus subtilis. The enzymatic reactions, like their solution counterpart, are thus concerted [3,3]-sigmatropic processes in which C-C bond formation lags behind C-O bond cleavage. However, as substantially larger 18O and smaller 13C isotope effects were observed for a mutant enzyme in which chemistry is fully rate determining, the ionic active site may favor a somewhat more polarized transition state than that seen in solution.

Study of 1-deoxy-D-xylulose-5-phosphate reductoisomerase: Synthesis and evaluation of fluorinated substrate analogues

(Chemical Equation Presented) 1-Deoxy-D-xylulose-5-phosphate (DXP) reductoisomerase is a NADPH-dependent enzyme catalyzing the conversion of DXP to methyl-D-erythritol 4-phosphate (MEP). In this study, each of the hydroxyl groups in DXP and one of its C-1