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

Bioorganic and Medicinal Chemistry Letters

Volumn 10, Issue 11, 2000, Pages 1285-1288

  Hill, Craig M ^a   Wu, Feiyue ^a   Cheng, Tu Chen ^b   Defrank, Joseph J ^b   Raushel, Frank M ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b US Army Edgewood Res Devmt E   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ORGANOPHOSPHATE; PHOSPHOTRIESTERASE;

ARTICLE; DETOXIFICATION; ENANTIOMER; ENZYME SPECIFICITY; HYDROLYSIS; NONHUMAN; STEREOCHEMISTRY;

ALTEROMONAS; ARYLDIALKYLPHOSPHATASE; ESTERASES; ESTERS; ORGANOPHOSPHORUS COMPOUNDS; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

ALTEROMONAS SP.; BACTERIA (MICROORGANISMS);

EID: 0034608454     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(00)00213-4     Document Type: Article

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10. 4 at 65% saturation and then dialyzed against buffer A.
11. m values makes their precise measurement difficult. The more reliable estimate of the specificity ratio is obtained from the progress curves.
12. The substrates were synthesized as described in 9. The enantiomeric purity for each isomer was greater than 95%. The toxic properties of these compounds have not been determined.
13. Benschop H.P., Konings C.A.G., Van Genderen J., De Jong L.P.A. Toxicol. Appl. Pharmacol. 72:1984;61.