33026-79-8

Upstream product

• 100-49-2 cyclohexylmethyl alcohol 
• 136025-57-5 Phosphoric acid dibenzyl ester cyclohexylmethyl ester 
• 33026-78-7 cyclohexylmethyl phosphate diphenyl 

Downstream Products

• 93605-02-8 C₁₆H₂₇N₃O₁₁P₂ 

Relevant academic research and scientific papers

Regioselective phosphorylation of carbohydrates and various alcohols by bacterial acid phosphatases; probing the substrate specificity of the enzyme from Shigella flexneri

Bacterial non-specific acid phosphatases normally catalyze the dephosphorylation of a variety of substrates. As shown previously the enzymes from Shigella flexneri and Salmonella enterica are also able to catalyze the phosphorylation of inosine to inosine monophosphate and D-glucose to D-glucose 6-phosphate (D-G6P) using cheap pyrophosphate as the phosphate donor. After optimization high yields (95%) are achieved in the latter reaction and we show here that it is possible to use these enzymes in a preparative manner. This prompted us to investigate by using 31P NMR and HPLC also the phosphorylation of a broad range of carbohydrates and alcohols. Many cyclic carbohydrates are phosphorylated in a regioselective manner. Non-cyclic carbohydrates are phosphorylated as well. Phosphorylation of linear alcohols, cyclic and aromatic alcohols is also possible. In all cases the acid phosphatase from Shigella prefers a primary alcohol function above a secondary one. We conclude that these enzymes are an attractive alternative to existing chemical and enzymatic methods in the phosphorylation of a broad range of compounds.

A new method for transforming primary amines into phosphoric acid monoesters

Nitrosation of dibenzylphosphoramidates enables the synthesis of phosphoric acid monoesters from primary n-alkylamines in good yield.

Nucleoside conjugates. 6. Synthesis and comparison of antitumor activity of 1-β-D-arabinofuranosylcytosine conjugates of corticosteroids and selected lipophilic alcohols

Five new P1-(steroid-21-yl)-P2-(1-β-D-arabinofuranosylcytosin-5'-yl)pyrophosphat es (ara-CDP-steroids), five 1-β-D-arabinofuranosylcytosine 5'-O-(alkyl)phosphates (ara-CMP-alkyl esters), and two P1-(alkyl)-P2-(1-β-D-arabinofuranosylcytosin-5'-yl)pyrophosphate (ara-CDP-alkyl esters) have been prepared and evaluated against L1210 lymphoid leukemia in culture and in mice (C3D2F1/J). These include ara-CDP-11-deoxycorticosterone, ara-CDP-cortisone, ara-CDP-corticosterone, ara-CDP-cortexolone, and ara-CDP-prednisone, ara-CMP hexadecyl ester, ara-CMP 1-cyclohexylmethyl ester, ara-CMP 1-adamantylmethyl ester, ara-CMP 2-(1-adamanthyl)ethyl ester, ara-CMP 2-chloroethyl ester, ara-CDP hexadecyl ester, and ara-CDP 1-cyclohexylmethyl ester. The in vitro antitumor results indicated that ara-CDP-steroids were as active as the previously reported ara-CMP-steroids and that ara-CMP and ara-CDP-alkyl esters were less growth inhibiting than ara-CDP-steroids and ara-C. However, the in vivo antitumor results indicated that ara-CDP-steroids were generally less effective than the previous monophosphate derivatives. Among them ara-CDP-corticosterone and the known ara-CDP-cortisol showed greater efficacy than ara-C with ILS value of 152% and 209%, respectively, at the optimal dose of 40 and 80 (mg/kg)/day for 9 days, while that of ara-C was 138% at the optimum dose of 9.2 (mg/kg)/day. Generally, ara-CMP alkyl esters, given ip to the L1210 leukemic mice, were found to be toxic and ineffective. However, ara-CDP hexadecyl ester showed marginal activity (ILS, 38%). These preliminary results support the thesis that the ara-C conjugates of this type may require a lipophilic and naturally occurring moiety for improved efficacy.