title: Enzymatic synthesis of chiral organophosphothioates from prochiral precursors.
abstract: The phosphotriesterase from Pseudomonas diminuta has been shown to selectively cleave the pro-R p-nitrophenolate substituent from bis-p-nitrophenyl alkyl phosphothioate esters. When the alkyl substituent is methyl, ethyl, or isopropyl the enantiomeric excess of the product is >/=99%. Manipulation of the active site through mutagenesis has enabled the preparation of protein variants that preferentially hydrolyze the pro-S substituent of the target substrates. This methodology thus permits the preparation of chiral products from prochiral precursors.
authors.affiliation: Department of Chemistry, Texas A&M University, P.O. Box 30012, College Station, Texas 77842-3012, USA.
authors.forename: Wen-Shan
authors.initials: WS
authors.lastname: Li
authors.forename: Yingchun
authors.initials: Y
authors.lastname: Li
authors.forename: Craig M
authors.initials: CM
authors.lastname: Hill
authors.forename: Karin T
authors.initials: KT
authors.lastname: Lum
authors.forename: Frank M
authors.initials: FM
authors.lastname: Raushel
mesh_terms: D043303:Aryldialkylphosphatase; D018360:Crystallography, X-Ray; D004950:Esterases / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D009946:Organothiophosphorus Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D013237:Stereoisomerism
chemical_list: D009946:Organothiophosphorus Compounds; D004950:Esterases; D043303:Aryldialkylphosphatase