Enzymatic resolution of chiral phosphinate esters

…, SD Aubert, EG Maes, FM Raushel

Index: Li, Yingchun; Aubert, Sarah D.; Raushel, Frank M. Journal of the American Chemical Society, 2003 , vol. 125, # 25 p. 7526 - 7527

Full Text: HTML

Citation Number: 36

Abstract

The bacterial phosphotriesterase has been shown to catalyze the stereoselective hydrolysis of phosphinate esters. The wild-type enzyme preferentially hydrolyzes the SP-enantiomers of methyl phenyl pX-phenylphosphinate esters by 3 orders of magnitude. The mutant enzyme, I106T/F132A/H254G/H257W, exhibits the opposite stereoselectivity and hydrolyzes the RP-enantiomer up to 30 times faster than the corresponding SP-enantiomer. The ...