On October 15, 2006, Tao, Haiyan; Peralta-Yahya, Pamela; Lin, Hening; Cornish, Virginia W. published an article.Name: (S)-5-tert-Butyl 1-methyl 2-aminopentanedioate The title of the article was Optimized design and synthesis of chemical dimerizer substrates for detection of glycosynthase activity via chemical complementation. And the article contained the following:
Glycosynthases catalyze the formation of a glycosidic bond between a glycosyl fluoride donor substrate and a glycosyl acceptor substrate with high yield, thus providing a valuable approach for the synthesis of carbohydrates and glycoconjugates. Chem. complementation can be used to link glycosynthase activity to the transcription of a reporter gene in vivo, providing a selection for the directed evolution of glycosynthase enzymes with improved properties. In this approach, glycosynthase activity is detected as covalent coupling between a small mol. disaccharide acceptor substrate and a small mol. disaccharide α-fluoro donor substrate. Here the authors report the optimized design and synthesis of these small mol. substrates. These optimized substrates are shown to give a robust, glycosynthase-dependent transcriptional read-out in the chem. complementation assay. The full synthesis and characterization of these substrates are reported for the first time. These optimized chem. dimerizer substrates should allow the potential of chem. complementation for the directed evolution of glycosynthases with diverse substrate specificities and improved properties to be fully realized. The experimental process involved the reaction of (S)-5-tert-Butyl 1-methyl 2-aminopentanedioate(cas: 53838-27-0).Name: (S)-5-tert-Butyl 1-methyl 2-aminopentanedioate
The Article related to glycosynthase substrate design preparation, Enzymes: Analysis (Determination-Detection) and other aspects.Name: (S)-5-tert-Butyl 1-methyl 2-aminopentanedioate
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