Operational control of stereoselectivity during the enzymatic hydrolysis of racemic organophosphorus compounds. Academic Article

abstract

• The wild-type bacterial phosphotriesterase catalyzes the stereoselective hydrolysis of racemic pairs of organophosphorus compounds. The enzymatic stereoselectivity can be substantially enhanced via systematic alteration of the pKa for the leaving group phenol in the target substrates. These changes alter the rate-limiting step for substrate turnover from a diffusional event to phosphorus-oxygen bond cleavage. Turnover ratios in excess of 5000:1 were achieved using phenols with pKa values greater than 8.5. This method has enabled the isolation of the RP-enantiomer of 4-acetylphenyl methyl phenylphosphonate with an enantiomeric excess of >99% via a kinetic resolution of the racemate.

authors

• Raushel, Frank

published proceedings

• J Am Chem Soc

altmetric score

• 3

author list (cited authors)

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

citation count

• 22

complete list of authors

• Li, Yingchun||Aubert, Sarah D||Raushel, Frank M

publication date

• June 2003

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Aryldialkylphosphatase
• Esterases
• Hydrolysis
• Kinetics
• Organophosphorus Compounds
• Stereoisomerism

PubMed Central ID

• 12812487

Digital Object Identifier (DOI)

• 10.1021/ja035625m

start page

• 7526

end page

• 7527

volume

• 125

issue

• 25

URL

• http://dx.doi.org/10.1021/ja035625m