B. K. Singh, Organophosphorus-degrading bacteria: ecology and industrial applications, Nature Reviews Microbiology, vol.150, issue.2, pp.156-64, 2009.
DOI : 10.1099/mic.0.26977-0

F. M. Raushel, Bacterial detoxification of organophosphate nerve agents, Current Opinion in Microbiology, vol.5, issue.3, pp.288-95, 2002.
DOI : 10.1016/S1369-5274(02)00314-4

K. E. Lejeune, J. R. Wild, and A. J. Russell, Nerve agents degraded by enzymatic foams, Nature, vol.395, issue.6697, pp.27-35, 1998.
DOI : 10.1038/25634

D. P. Dumas, S. R. Caldwell, J. R. Wild, and F. M. Raushel, Purification and properties of the phosphotriesterase from Pseudomonas diminuta, J Biol Chem, vol.264, issue.33, pp.19659-65, 1989.

F. M. Raushel, Catalytic detoxification, Nature, vol.101, issue.7330, pp.310-311, 2011.
DOI : 10.1073/pnas.2536901100

P. C. Tsai, Stereoselective Hydrolysis of Organophosphate Nerve Agents by the Bacterial Phosphotriesterase, Biochemistry, vol.49, issue.37, pp.7978-87, 2010.
DOI : 10.1021/bi101056m

E. Ghanem and F. M. Raushel, Detoxification of organophosphate nerve agents by bacterial phosphotriesterase, Toxicology and Applied Pharmacology, vol.207, issue.2, pp.459-70, 2005.
DOI : 10.1016/j.taap.2005.02.025

L. Merone, L. Mandrich, M. Rossi, and G. Manco, A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties, Extremophiles, vol.185, issue.4, pp.297-305, 2005.
DOI : 10.1042/bj3320203

D. Vecchio and P. , Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus, Extremophiles, vol.4, issue.3, pp.461-70, 2009.
DOI : 10.1016/j.bbapap.2005.06.008

C. Vieille and G. J. Zeikus, Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability, Microbiology and Molecular Biology Reviews, vol.65, issue.1, pp.1-43, 2001.
DOI : 10.1128/MMBR.65.1.1-43.2001

URL : http://mmbr.asm.org/content/65/1/1.full.pdf

D. C. Demirjian, F. Moris-varas, and . Cassidy, Enzymes from extremophiles, Current Opinion in Chemical Biology, vol.5, issue.2, pp.144-51, 2001.
DOI : 10.1016/S1367-5931(00)00183-6

L. Merone, Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase, Bioresource Technology, vol.101, issue.23, pp.9204-9216, 2010.
DOI : 10.1016/j.biortech.2010.06.102

M. Elias, Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities, Journal of Molecular Biology, vol.379, issue.5, pp.1017-1045, 2008.
DOI : 10.1016/j.jmb.2008.04.022

M. Elias, Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase, Acta crystallographica, vol.63, pp.553-558, 2007.

F. S. Ng, D. M. Wright, and S. Seah, Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for quorum quenching, Appl Environ Microbiol, 2010.

R. Popat, S. A. Crusz, and S. P. Diggle, The social behaviours of bacterial pathogens, British Medical Bulletin, vol.187, issue.5, pp.63-75, 2008.
DOI : 10.1128/JB.187.5.1799-1814.2005

Y. H. Dong, Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase, Nature, vol.17, issue.6839, pp.813-820, 2001.
DOI : 10.1038/8643

M. Elias and D. S. Tawfik, Divergence and Convergence in Enzyme Evolution: Parallel Evolution of Paraoxonases from Quorum-quenching Lactonases, Journal of Biological Chemistry, vol.267, issue.1, pp.11-20, 2012.
DOI : 10.1074/jbc.R111.240945

R. D. Gupta, Directed evolution of hydrolases for prevention of G-type nerve agent intoxication, Nature Chemical Biology, vol.28, issue.158, pp.120-125, 2011.
DOI : 10.1038/nbt.1609

E. Porzio, L. Merone, L. Mandrich, M. Rossi, and G. Manco, A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus, Biochimie, vol.89, issue.5, pp.625-661, 2007.
DOI : 10.1016/j.biochi.2007.01.007

R. Hawwa, J. Aikens, R. J. Turner, B. D. Santarsiero, and A. D. Mesecar, Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus, Archives of Biochemistry and Biophysics, vol.488, issue.2, pp.109-129, 2009.
DOI : 10.1016/j.abb.2009.06.005

R. Hawwa, S. D. Larsen, K. Ratia, and A. Mesecar, Structure-Based and Random Mutagenesis Approaches Increase the Organophosphate-Degrading Activity of a Phosphotriesterase Homologue from Deinococcus radiodurans, Journal of Molecular Biology, vol.393, issue.1, pp.36-57, 2009.
DOI : 10.1016/j.jmb.2009.06.083

G. A. Omburo, J. M. Kuo, L. S. Mullins, and F. M. Raushel, Characterization of the zinc binding site of bacterial phosphotriesterase, The Journal of biological chemistry, vol.267, pp.13278-83, 1992.

Y. Ashani, Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers, Chemico-Biological Interactions, vol.187, issue.1-3, pp.1-3, 2010.
DOI : 10.1016/j.cbi.2010.02.039

C. J. Jackson, J. W. Liu, M. L. Coote, and D. L. Ollis, The effects of substrate orientation on the mechanism of a phosphotriesterase, Organic & Biomolecular Chemistry, vol.94, issue.24, pp.4343-50, 2005.
DOI : 10.1042/bj1040369

C. J. Jackson, phosphotriesterase: the prominent role of iron in the heterobinuclear active site, Biochemical Journal, vol.397, issue.3, pp.501-509, 2006.
DOI : 10.1042/BJ20060276

M. Ben-david, Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1, Journal of Molecular Biology, vol.418, issue.3-4, pp.181-96, 2012.
DOI : 10.1016/j.jmb.2012.02.042

M. M. Benning, S. B. Hong, F. M. Raushel, and H. M. Holden, The Binding of Substrate Analogs to Phosphotriesterase, Journal of Biological Chemistry, vol.74, issue.39, pp.30556-60, 2000.
DOI : 10.1021/bi960663m

L. Afriat-jurnou, C. J. Jackson, and D. S. Tawfik, Reconstructing a Missing Link in the Evolution of a Recently Diverged Phosphotriesterase by Active-Site Loop Remodeling, Biochemistry, vol.51, issue.31, 2012.
DOI : 10.1021/bi300694t

F. W. Studier, Protein production by auto-induction in high-density shaking cultures, Protein Expression and Purification, vol.41, issue.1, pp.207-241, 2005.
DOI : 10.1016/j.pep.2005.01.016

H. A. Walsh, K. C. O-'shea, and N. P. Botting, Comparative inhibition by substrate analogues 3-methoxy-and 3-hydroxydesaminokynurenine and an improved 3 step purification of recombinant human kynureninase, BMC Biochemistry, vol.4, issue.1, p.13, 2003.
DOI : 10.1186/1471-2091-4-13

W. Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants, Journal of Applied Crystallography, vol.26, issue.6, pp.795-800, 1993.
DOI : 10.1107/S0021889893005588

A. Vagin and A. Teplyakov, An approach to multi-copy search in molecular replacement, Acta Crystallographica Section D Biological Crystallography, vol.56, issue.12, pp.1622-1626, 2000.
DOI : 10.1107/S0907444900013780

URL : http://journals.iucr.org/d/issues/2000/12/00/li0360/li0360.pdf

P. Emsley and K. Cowtan, : model-building tools for molecular graphics, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2126-2158, 2004.
DOI : 10.1107/S0907444904019158

URL : http://journals.iucr.org/d/issues/2004/12/01/ba5070/ba5070.pdf

G. N. Murshudov, A. A. Vagin, and E. J. Dodson, Refinement of Macromolecular Structures by the Maximum-Likelihood Method, Acta Crystallographica Section D Biological Crystallography, vol.53, issue.3, pp.240-55, 1997.
DOI : 10.1107/S0907444996012255

V. S. Lamzin and K. S. Wilson, Automated refinement of protein models, Acta Crystallographica Section D Biological Crystallography, vol.49, issue.1, pp.129-176, 1993.
DOI : 10.1107/S0907444992008886

V. B. Chen, : all-atom structure validation for macromolecular crystallography, Acta Crystallographica Section D Biological Crystallography, vol.285, issue.1, pp.12-21, 2010.
DOI : 10.1107/S0907444909042073

W. L. Delano, The PyMOL Molecular Graphics System, DeLano Scientific, 2002.