Application of nuclear magnetic resonance spectrometry to measure the activity of bacterial macrolide esterase.
A new method of measuring the activity of macrolide antibiotic esterase in whole bacteria and in crude enzyme extracts was determined through the application of nuclear magnetic resonance spectrometry. The structure of the enzymatically esterolytic cleavage compound of oleandomycin was clearly shown to be the cyclic hemiacetal between the C-9 keto and the hydroxy group of C-13 in the open macrolide nucleus by physicochemical techniques.
Department of Microbiology, School of Pharmaceutical Sciences, Tokyo College of Pharmacy, Japan.
K
K
O'Hara
D000900:Anti-Bacterial Agents / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009827:Oleandomycin / Q000737:chemistry / Q000378:metabolism*; D001618:beta-Lactamases / Q000378:metabolism
D000900:Anti-Bacterial Agents; D002265:Carboxylic Ester Hydrolases; C046388:erythromycin esterase; D001618:beta-Lactamases; D009827:Oleandomycin