Enzyme-catalysed enantioselective hydrolysis of racemic naproxen nitrile.
The bacterial strain Rhodococcus butanica (ATCC 21197), which exhibits nitrilase and nitrile hydratase/amidase activities, catalyses the enantioselective hydrolysis of racemic naproxen nitrile (R/S)-1 to furnish a moderate enantiomeric excess of (S)-naproxen (S)-3. Racemic naproxen amide (R/S)-2 is not a good substrate for this strain. Resting cells of the newly selected bacterial strain Rhodococcus sp. C3II catalyse the enantioselective hydrolyses of racemic naproxen nitrile (R/S)-1 and naproxen amide (R/S)-2 as well, to give (S)-3 in excellent optical (99% e.e.) and good chemical yields in aqueous medium and in the biphasic system of phosphate buffer/hexane.
Effenberger
F
F
Institut für Organische Chemie der Universität Stuttgart, Germany.
Böhme
J
J
D000619:Aminohydrolases / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D006836:Hydro-Lyases / Q000378:metabolism; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009288:Naproxen / Q000031:analogs & derivatives* / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D009570:Nitriles / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012240:Rhodococcus / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity
D009570:Nitriles; C092085:naproxen nitrile; D009288:Naproxen; D000619:Aminohydrolases; C021867:nitrilase; D006836:Hydro-Lyases; C048831:nitrile hydratase