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

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

• Raushel, Frank

published proceedings

• Bioorg Med Chem Lett

author list (cited authors)

• Hill, C. M., Wu, F., Cheng, T. C., DeFrank, J. J., & Raushel, F. M.

citation count

• 33

complete list of authors

• Hill, CM||Wu, F||Cheng, TC||DeFrank, JJ||Raushel, FM

publication date

• January 2000

publisher

• Elsevier  Publisher

published in

• Bioorganic and Medicinal Chemistry Letters  Journal

keywords

• Alteromonas
• Aryldialkylphosphatase
• Esterases
• Esters
• Organophosphorus Compounds
• Stereoisomerism
• Substrate Specificity

Digital Object Identifier (DOI)

• 10.1016/s0960-894x(00)00213-4

start page

• 1285

end page

• 1288

volume

• 10

issue

• 11

URL

• http://dx.doi.org/10.1016/s0960-894x(00)00213-4