title: Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters.
abstract: The enzyme OPAA hydrolyzes p-nitrophenyl phosphotriesters bearing substituents at the phosphorus center ranging in size from methyl to phenyl. The enzyme exhibits stereoselectivity toward the hydrolysis of chiral substrates with a preference for the Sp enantiomer.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station 77843, USA.
authors.forename: C M
authors.initials: CM
authors.lastname: Hill
authors.forename: F
authors.initials: F
authors.lastname: Wu
authors.forename: T C
authors.initials: TC
authors.lastname: Cheng
authors.forename: J J
authors.initials: JJ
authors.lastname: DeFrank
authors.forename: F M
authors.initials: FM
authors.lastname: Raushel
mesh_terms: D020591:Alteromonas / Q000201:enzymology*; D043303:Aryldialkylphosphatase; D004950:Esterases / Q000378:metabolism*; D004952:Esters / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D004952:Esters; D009943:Organophosphorus Compounds; D004950:Esterases; D043303:Aryldialkylphosphatase