208997-82-4

Upstream product

• 208997-79-9 2-Benzyloxycarbonylamino-4-(dimethoxy-phosphoryl)-butyric acid methyl ester 

Downstream Products

• 208997-95-9 DL-methyl N,N-diethyl-{3-[(benzyloxycarbonyl)amino]-3-methoxycarbonylpropyl}-SR-phosphonamidate 
• 208997-91-5 DL-methyl N,N-dimethyl-{3-[(benzyloxycarbonyl)amino]-3-methoxycarbonylpropyl}-SR-phosphonamidate 
• 208997-93-7 DL-methyl N-ethyl-{3-[(benzyloxycarbonyl)amino]-3-methoxycarbonylpropyl}-SR-phosphonamidate 
• 208997-89-1 DL-methyl {3-[(benzyloxycarbonyl)amino]-3-methoxycarbonylpropyl}-SR-phosphonamidate 

Relevant academic research and scientific papers

Selective cleavage of one ester group in dibenzyl Di-P-nitrobenzyl and dimethyl N-protected aminoalkylphosphonates

Benzyl, p-nitrobenzyl and methyl hydrogen N-protected aminoalkylphosphonates were efficiently prepared by selective cleavage of one ester group in the corresponding diesters using DABCO (1,4-diazabicyclo(2.2.2]octane).

Investigation of mechanism of nitrogen transfer in glucosamine 6- phosphate synthase with the use of transition state analogs

Several structural analogs of putative tetrahedral intermediates of the reaction catalyzed by the glutamine amide transfer domain of Candida albicans glucosamine 6-phosphate synthase have been designed and synthesized. Esters and amides of γ-phosphonic and γ-sulfonic analogs of glutamine and glutamic acid were tested as potential inhibitors of the enzyme. N-substituted amides 9 and 15 were found to be the strongest inhibitors in the series. Structure- activity relationship studies led to conclusions supporting the possibility of a direct nucleophilic attack of the glutamine amide nitrogen on an electrophilic site of the enzyme-bound fructose 6-phosphate as the most likely mechanism of nitrogen transfer in glucosamine 6-phosphate synthase.