Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters.
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.
Hill
C M
CM
Department of Chemistry, Texas A&M University, College Station 77843, USA.
Wu
F
F
Cheng
T C
TC
DeFrank
J J
JJ
Raushel
F M
FM
D020591:Alteromonas / Q000201:enzymology*; D043303:Aryldialkylphosphatase; D004950:Esterases / Q000378:metabolism*; D004952:Esters / Q000378:metabolism; D009943:Organophosphorus Compounds / Q000378:metabolism*; D013237:Stereoisomerism; D013379:Substrate Specificity
D004952:Esters; D009943:Organophosphorus Compounds; D004950:Esterases; D043303:Aryldialkylphosphatase