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Full-Text Articles in Enzymes and Coenzymes
Biochemical Characterization Of Diamide Inhibitors With N-Acetylglucosaminidases Lytg From Bacillus Subtilis, Drew Phelan
Biochemical Characterization Of Diamide Inhibitors With N-Acetylglucosaminidases Lytg From Bacillus Subtilis, Drew Phelan
Honors Projects in Science and Technology
In recent years the frequency of antibiotic resistance has been on the rise creating a need for antibiotic development with specific and lethal targets. It has been recently reported that glycosyl trizole are a novel class of antibacterial agents (1). Further investigation on the antibacterial ability of glycosyl triazole inhibitors has shown that targets include exo-acting N-acetylglucosaminidases (GlcNAcase) LytG (Bacillus subtilis) and FlgJ (Salmonella enterica) of the GH73 family (2). The Glycoside Hydrolase Family 73 (GH73) is characterized by bacterial and viral glycoside hydrolase. This enzyme cleaves the β-1,4-glycosidic linkage between N-acetylglucosaminyl (NAG) and N-acetylmuramyl (NAM) of the carbohydrate backbone …