Enzymatic resolution of chiral phosphinate esters. Academic Article uri icon


  • 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 p-X-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 enantiomerically pure phosphinate esters, prepared from the kinetic resolution of racemic mixtures, can serve as the entry point for the chemoenzymatic preparation of P-chiral phosphines and phosphine oxides.

published proceedings

  • J Am Chem Soc

altmetric score

  • 3

author list (cited authors)

  • Li, Y., Aubert, S. D., Maes, E. G., & Raushel, F. M.

citation count

  • 33

complete list of authors

  • Li, Yingchun||Aubert, Sarah D||Maes, Eugene G||Raushel, Frank M

publication date

  • July 2004