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

Full Text: HTML

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.

Related Articles:

Vibrational spectra and normal coordinate analysis of barium dimethyl, diethyl and ethyl methyl phosphates

[Taga, Keijiro; Miyagai, Kiyotaka; Hirabayashi, Noriaki; Yoshida, Tadayoshi; Okabayashi, Hirofumi Journal of Molecular Structure, 1991 , vol. 245, # 1/2 p. 1 - 11]

Spezielle praktische Geologie und Begwirtschaff

[Jentzsch,R. et al. Journal fuer Praktische Chemie (Leipzig), 1975 , vol. 317, p. 733 - 744]

Phosphorylation of alcohols through the acid-catalysed fragmentation of α-oxyiminophosphonates

[Breuer, Eli; Karaman, Rafik; Leader, Haim; Goldblum, Amiram Journal of the Chemical Society, Chemical Communications, 1987 , p. 671 - 672]

Fragmentation of methyl hydrogen α-hydroxyiminobenzylphosphonates—kinetics, mechanism and the question of metaphosphate formation

[Katzhendler, Jehoshua; Schneider, Hava; Ta-Shma, Rachel; Breuer, Eli Journal of the Chemical Society. Perkin Transactions 2, 2000 , # 9 p. 1961 - 1968]

Fragmentation of methyl hydrogen α-hydroxyiminobenzylphosphonates—kinetics, mechanism and the question of metaphosphate formation

[Katzhendler, Jehoshua; Schneider, Hava; Ta-Shma, Rachel; Breuer, Eli Journal of the Chemical Society. Perkin Transactions 2, 2000 , # 9 p. 1961 - 1968]

More Articles...