Characterisation of the organophosphate hydrolase catalytic activity of SsoPox

Scientific Reports

Volumn 2, Issue , 2012, Pages

  Hiblot, Julien ^a   Gotthard, Guillaume ^a   Chabriere, Eric ^a   Elias, Mikael ^b  

^a CNRS   (France)

^b WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; FENSULFOTHION; ORGANOPHOSPHORUS COMPOUND; PARAOXON; PHOSPHATASE; PHOSPHOROTHIOIC ACID DERIVATIVE; PHOSPHORYLPHOSPHATASE;

ARTICLE; BINDING SITE; BIOCATALYSIS; CHEMISTRY; DRUG ANTAGONISM; ENZYME ACTIVE SITE; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR DOCKING; SULFOLOBUS SOLFATARICUS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DETERGENTS; KINETICS; MOLECULAR DOCKING SIMULATION; ORGANOPHOSPHORUS COMPOUNDS; ORGANOTHIOPHOSPHORUS COMPOUNDS; PARAOXON; PHOSPHORIC MONOESTER HYDROLASES; SULFOLOBUS SOLFATARICUS;

EID: 84869155211     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00779     Document Type: Article

References (42)

1. Singh, B. K. Organophosphorus-degrading bacteria: ecology and industrial applications. Nat Rev Microbiol 7 (2), 156-64 (2009).
2. Raushel, F. M. Bacterial detoxification of organophosphate nerve agents. Current opinion in microbiology 5(3), 288-95 (2002). (Pubitemid 34614941)
3. LeJeune, K. E., Wild, J. R. & Russell, A. J. Nerve agents degraded by enzymatic foams. Nature 395 (6697), 27-8 (1998). (Pubitemid 28420218)
4. Seibert, C. M. & Raushel, F. M. Structural and catalytic diversity within the amidohydrolase superfamily. Biochemistry 44 (17), 6383-91 (2005). (Pubitemid 40593789)
5. Dumas, D. P., Caldwell, S. R., Wild, J. R. & Raushel, F. M. Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J Biol Chem 264 (33), 19659-65 (1989). (Pubitemid 20008072)
6. Raushel, F. M. Chemical biology: Catalytic detoxification. Nature 469 (7330), 310-1 (2011).
7. Tsai, P. C. et al. Stereoselective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase. Biochemistry 49 (37), 7978-87 (2010).
8. Ghanem, E. & Raushel, F. M. Detoxification of organophosphate nerve agents by bacterial phosphotriesterase. Toxicology and applied pharmacology 207 (2 Suppl), 459-70 (2005).
9. Merone, L., Mandrich, L., Rossi, M. & Manco, G. A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles 9 (4), 297-305 (2005). (Pubitemid 41187698)
10. Del Vecchio, P. et al. Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles 13 (3), 461-70 (2009).
11. Vieille, C. & Zeikus, G. J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65 (1), 1-43 (2001). (Pubitemid 32204286)
12. Demirjian, D. C., Moris-Varas, F. & Cassidy, C. S. Enzymes from extremophiles. Current opinion in chemical biology 5 (2), 144-51 (2001). (Pubitemid 32245674)
13. Merone, L. et al. Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase. Bioresour Technol 101 (23), 9204-12 (2010).
14. Afriat, L., Roodveldt, C., Manco, G. & Tawfik, D. S. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry 45 (46), 13677-86 (2006). (Pubitemid 44788738)
15. Elias, M. et al. Structural basis for natural lactonase and promiscuous phosphotriesterase activities. Journal of molecular biology 379 (5), 1017-28 (2008).
16. Elias, M. et al. Crystallization and preliminary X-ray diffraction analysis of the hyperthermophilic Sulfolobus solfataricus phosphotriesterase. Acta crystallographica 63 (Pt 7), 553-5 (2007). (Pubitemid 47052198)
17. Ng, F. S., Wright, D. M. & Seah, S. Y. Characterization of a phosphotriesterase-like lactonase from Sulfolobus solfataricus and its immobilization for quorum quenching. Appl Environ Microbiol (2010).
18. Popat, R., Crusz, S. A. & Diggle, S. P. The social behaviours of bacterial pathogens. Br Med Bull 87, 63-75 (2008).
19. Dong, Y. H. et al.Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 411 (6839), 813-7 (2001).
20. Elias, M. & Tawfik, D. S. Divergence and Convergence in Enzyme Evolution: Parallel Evolution of Paraoxonases from Quorum-quenching Lactonases. The Journal of biological chemistry 287 (1), 11-20 (2012).
21. Gupta, R. D. et al. Directed evolution of hydrolases for prevention of G-type nerve agent intoxication. Nat Chem Biol 7 (2), 120-5 (2011).
22. Porzio, E., Merone, L., Mandrich, L., Rossi, M. & Manco, G. A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus. Biochimie 89 (5), 625-36 (2007). (Pubitemid 46669781)
23. Hawwa, R., Aikens, J., Turner, R. J., Santarsiero, B. D. &Mesecar, A. D. Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. Arch Biochem Biophys 488 (2), 109-20 (2009).
24. Hawwa, R., Larsen, S. D., Ratia, K. &Mesecar, A. D. Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans. Journal of molecular biology 393 (1), 36-57 (2009).
25. Omburo, G. A., Kuo, J. M., Mullins, L. S. & Raushel, F. M. Characterization of the zinc binding site of bacterial phosphotriesterase. The Journal of biological chemistry 267 (19), 13278-83 (1992).
26. Ashani, Y. et al. Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of paraoxonase (PON1) catalytic scavengers. Chemico-biological interactions 187 (1-3), 362-9 (2010).
27. Jackson, C. J., Liu, J. W., Coote, M. L. & Ollis, D. L. The effects of substrate orientation on the mechanism of a phosphotriesterase. Org Biomol Chem 3 (24), 4343-50 (2005). (Pubitemid 43035618)
28. Jackson, C. J. et al. Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site. The Biochemical journal 397 (3), 501-8 (2006). (Pubitemid 44187508)
29. Ben-David, M. et al. Catalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1. Journal of molecular biology 418 (3-4), 181-96 (2012).
30. Benning, M. M., Hong, S. B., Raushel, F. M. & Holden, H. M. The binding of substrate analogs to phosphotriesterase. The Journal of biological chemistry 275 (39), 30556-60 (2000).
31. Momb, J. et al. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations. Biochemistry 47 (29), 7715-25 (2008). (Pubitemid 352019502)
32. Afriat-Jurnou, L., Jackson, C. J. & Tawfik, D. S. Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling. Biochemistry (2012).
33. Studier, F. W. Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41 (1), 207-34 (2005).
34. Walsh, H. A., O'Shea, K. C. & Botting, N. P. Comparative inhibition by substrate analogues 3-methoxy-and 3-hydroxydesaminokynurenine and an improved 3 step purification of recombinant human kynureninase. BMC Biochem 4, 13 (2003).
35. Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry land cell constants. Journal of Applied Crystalography 26, 795-800 (1993).
36. Collaborative Computational Project Number 4, The CCP4 suite: programs for protein crystallography. Acta crystallographica 50, 760-3 (1994).
37. Vagin, A. & Teplyakov, A. An approach to multi-copy search in molecular replacement. Acta Crystallogr D Biol Crystallogr 56 (Pt 12), 1622-4 (2000). (Pubitemid 32040020)
38. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 (Pt 12 Pt 1), 2126-32 (2004). (Pubitemid 41742764)
39. Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53 (Pt 3), 240-55 (1997). (Pubitemid 27235885)
40. Lamzin, V. S. & Wilson, K. S. Automated refinement of protein models. Acta crystallographica. Section D, Biological crystallography 49 (Pt 1), 129-47 (1993).
41. Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta crystallographica. Section D, Biological crystallography 66 (Pt1), 12-21 (2010).
42. DeLano, W. L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA (2002).