Chemical Mechanism of the Phosphotriesterase from Sphingobium sp. Strain TCM1, an Enzyme Capable of Hydrolyzing Organophosphate Flame Retardants. Academic Article

abstract

• The mechanism of action of the manganese-dependent phosphotriesterase from Sphingobium sp. strain TCM1 that is capable of hydrolyzing organophosphate flame retardants was determined. The enzyme was shown to hydrolyze the RP-enantiomer of O-methyl O-cyclohexyl p-nitrophenyl thiophosphate with net inversion of configuration and without the formation of a covalent reaction intermediate. These results demonstrate that the enzyme catalyzes the hydrolysis of substrates by activation of a nucleophilic water molecule for direct attack at the phosphorus center.

authors

• Raushel, Frank

published proceedings

• J Am Chem Soc

author list (cited authors)

• Bigley, A. N., Xiang, D. F., Ren, Z., Xue, H., Hull, K. G., Romo, D., & Raushel, F. M.

citation count

• 22

complete list of authors

• Bigley, Andrew N||Xiang, Dao Feng||Ren, Zhongjie||Xue, Haoran||Hull, Kenneth G||Romo, Daniel||Raushel, Frank M

publication date

• February 2016

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Bacterial Proteins
• Flame Retardants
• Hydrolysis
• Kinetics
• Organophosphates
• Phosphoric Triester Hydrolases
• Sphingomonadaceae
• Stereoisomerism

PubMed Central ID

• 26907457

Digital Object Identifier (DOI)

• 10.1021/jacs.5b12739

start page

• 2921

end page

• 2924

volume

• 138

issue

• 9