Enzymatic resolution of chiral phosphinate esters.
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.
Li
Yingchun
Y
Department of Chemistry, Texas A&M University, P.O. Box 30012, College Station, Texas 77842-3012, USA.
Aubert
Sarah D
SD
Maes
Eugene G
EG
Raushel
Frank M
FM
D004952:Esters / Q000138:chemical synthesis / Q000737:chemistry* / Q000302:isolation & purification; D010721:Phosphinic Acids / Q000737:chemistry* / Q000302:isolation & purification; D044345:Phosphoric Triester Hydrolases / Q000737:chemistry*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D004952:Esters; D010721:Phosphinic Acids; D044345:Phosphoric Triester Hydrolases