10044-27-6Relevant academic research and scientific papers
Investigation of mechanism of nitrogen transfer in glucosamine 6- phosphate synthase with the use of transition state analogs
Milewski, SlLawomir,Hoffmann, Maria,Andruszkiewicz, Ryszard,Borowski, Edward
, p. 283 - 296 (2007/10/03)
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.
