Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6. 5 toward p-nitrophenyl phosphotriesters

…, F Wu, TC Cheng, JJ DeFrank, FM Raushel

Index: Hill, Craig M.; Wu, Feiyue; Cheng, Tu-Chen; Defrank, Joseph J.; Raushel, Frank M. Bioorganic and Medicinal Chemistry Letters, 2000 , vol. 10, # 11 p. 1285 - 1288

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Citation Number: 34

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.