208997-95-9

Upstream product

• 208997-82-4 methyl hydrogen (RS) 3-(benzyloxycarbonylamino)-3-(methoxycarbonyl)-propylphosphonate 
• 208997-79-9 2-Benzyloxycarbonylamino-4-(dimethoxy-phosphoryl)-butyric acid methyl ester 
• 109-89-7 diethylamine 

Relevant academic research and scientific papers

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.