Enzymatic resolution of chiral phosphinate esters. Academic Article

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 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.

authors

• Raushel, Frank

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

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Esters
• Phosphinic Acids
• Phosphoric Triester Hydrolases
• Stereoisomerism
• Structure-Activity Relationship

PubMed Central ID

• 15264807

Digital Object Identifier (DOI)

• 10.1021/ja048457m

start page

• 8888

end page

• 8889

volume

• 126

issue

• 29

URL

• http://dx.doi.org/10.1021/ja048457m