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Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase
Abstract
The reaction mechanism for the phosphotriesterase from Pseudomonas diminuta has been examined. When paraoxon (diethyl 4-nitrophenyl phosphate) is hydrolyzed by this enzyme in oxygen-18-labeled water, the oxygen-18 label is found exclusively in the diethyl phosphate product. The absolute configurations for the (+) and (-) enantiomers of O-ethyl phenylphosphonothioic acid have been determined by X-ray diffraction structural determination of the individual crystalline 1-phenylethylamine salts. The (+) enantiomer of the free acid corresponds to the RP configuration. The RP enantiomer of O-ethyl phenylphosphonothioic acid has been converted to the SP enantiomer of EPN [O-ethyl O-(4-nitrophenyl) phenylphosphonothioate]. (SP)-EPN is hydrolyzed by the phosphotriesterase to the SP enantiomer of O-ethyl phenylphosphonothioic acid. The enzymatic reaction therefore proceeds with inversion of configuration. These results have been interpreted as an indication of a single in-line displacement by an activated water molecule directly at the phosphorus center of the phosphotriester substrate. (RP)-EPN is not hydrolyzed by the enzyme at an appreciable rate.
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Cited by
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Kim, K., Tsay, O. G., Atwood, D. A., & Churchill, D. G. (2011) · Chemical Reviews · doi:10.1021/cr100193y · Cited by 1,011
Purification and Properties of the Phosphotriesterase from Pseudomonas diminuta
Dumas, D. P., Caldwell, S. R., Wild, J. R., & Raushel, F. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47164-0 · Cited by 498
Self-citationKatz, M. J., Moon, S.-Y., Mondloch, J. E., Beyzavi, M. H., Stephenson, C. J., Hupp, J. T., & Farha, O. K. (2015) · Chemical Science · doi:10.1039/c4sc03613a · Cited by 334
Metadata
- Authors
- Lewis, V. E., Donarski, W. J., Wild, J. R., & Raushel, F. M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1988-03-08
- Volume
- 27
- Issue
- 5
- Pages
- 1591-1597
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2080120578
- Cited by
- 181
- References
- 0
- FWCI
- 5.91
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lewis, V. E., Donarski, W. J., Wild, J. R., & Raushel, F. M. (1988). Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase. Biochemistry. https://doi.org/10.1021/bi00405a030
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