Mn2+ modulates the kinetic properties of an archaeal member of the PLL family

Chemico-Biological Interactions

Volumn 203, Issue 1, 2013, Pages 251-256

  Porzio, Elena ^a   Di Gennaro, Spartaco ^b   Palma, Achille ^b   Manco, Giuseppe ^a  

^a INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^b Metapontum Agrobios ^*  (Italy)

Author keywords

Kinetic parameters; Metals; Organophosphates; Phosphotriesterase like lactonases; Stability

Indexed keywords

AMIDASE; CADMIUM; MANGANESE; METAL; PARAOXON; PHOSPHOTRIESTERASE LIKE LACTONASE; UNCLASSIFIED DRUG; APOENZYME; ARCHAEAL PROTEIN; CARBOXYLESTERASE; HOLOENZYME; PHOSPHOTRIESTERASE; RECOMBINANT PROTEIN;

ANALYTIC METHOD; ARCHAEON; BINDING AFFINITY; CATALYSIS; CHEMICAL REACTION KINETICS; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; INDUCTIVE PLASMA COUPLED MASS SPECTROMETRY; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FAMILY; SULFOLOBUS ACIDOCALDARIUS; ARCHAEAL GENE; ARTICLE; CHEMISTRY; DRUG EFFECT; ENZYME SPECIFICITY; ENZYMOLOGY; GENE EXPRESSION; GENETICS; KINETICS; MASS SPECTROMETRY; METABOLISM; PH; TEMPERATURE;

ARCHAEA; SULFOLOBUS ACIDOCALDARIUS;

APOENZYMES; ARCHAEAL PROTEINS; CADMIUM; CARBOXYLIC ESTER HYDROLASES; ENZYME STABILITY; GENE EXPRESSION; GENES, ARCHAEAL; HOLOENZYMES; HYDROGEN-ION CONCENTRATION; KINETICS; MANGANESE; MASS SPECTROMETRY; PARAOXON; PHOSPHORIC TRIESTER HYDROLASES; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SULFOLOBUS ACIDOCALDARIUS; TEMPERATURE;

MLCS; MLOWN;

EID: 84875812059     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2012.11.003     Document Type: Conference Paper

References (25)

1. B.K. Singh Organophosphorus-degrading bacteria: ecology and industrial applications Nat. Rev. Microbiol. 7 2009 156 164
2. P. Masson, F. Nachon, and D. Rochu Engineering of catalytic bioscavengers of organophosphorus compounds Bull. Acad. Natl. Med. 191 2007 95 111
3. K.E. LeJeune, J.R. Wild, and A.J. Russell Nerve agents degraded by enzymatic foams Nature 395 1998 27 28
4. D.M. Munnecke Enzymatic hydrolysis of organophosphate insecticides, a possible pesticide disposal method Appl. Environ. Microbiol. 32 1976 7 13
5. N. Sethunathan, and T. Yoshida A Flavobacterium sp. that degrades diazinon and parathion Can. J. Microbiol. 19 1973 873 875
6. I. Horne, T.D. Sutherland, R.L. Harcourt, R.J. Russell, and J.G. Oakeshott Identification of an opd (organophosphate degradation) gene in an Agrobacterium isolate Appl. Environ. Microbiol. 68 2002 3371 3376
7. R.D. Gupta, M. Goldsmith, Y. Ashani, Y. Simo, G. Mullokandov, H. Bar, M. Ben-David, H. Leader, R. Margalit, I. Silman, J.L. Sussman, and D.S. Tawfik Directed evolution of hydrolases for prevention of G-type nerve agent intoxication Nat. Chem. Biol. 7 2011 120 125
8. P.C. Tsai, A. Bigley, E. Ghanem, C.L. Cadieux, S.A. Kasten, T.E. Reeves, D.M. Cerasoli, and F.M. Raushel Stereoselective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase Biochemistry 49 2010 7978 7987
9. L. Afriat, C. Roodveldt, G. Manco, and D.S. Tawfik The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase Biochemistry 45 2006 13677 13686
10. L. Merone, L. Mandrich, M. Rossi, and G. Manco A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties Extremophiles 9 2005 297 305
11. D.F. Xiang, P. Kolb, A.A. Fedorov, M. Meier, L.V. Fedorov, T.T. Nguyen, R. Sterner, S.C. Almo, B.K. Shoichet, and F.M. Raushel Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily Biochemistry 48 2009 2237 2247
12. R. Hawwa, S.D. Larsen, K. Ratia, and A.D. Mesecar Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans J. Mol. Biol. 393 2009 36 57
13. L. Mandrich, S. Di Gennaro, A. Palma, G. Manco, A further biochemical characterization of DrPLL the thermophilic lactonase from Deinococcus radiodurans, Protein Pept. Lett. (2012).
14. 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 Arch. Biochem. Biophys. 488 2009 109 120
15. D.F. Xiang, P. Kolb, A.A. Fedorov, M.M. Meier, L.V. Fedorov, T.T. Nguyen, R. Sterner, S.C. Almo, B.K. Shoichet, and F.M. Raushel Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily Biochemistry 48 2009 2237 2247
16. M. Elias, J. Dupuy, L. Merone, L. Mandrich, E. Porzio, S. Moniot, D. Rochu, C. Lecomte, M. Rossi, P. Masson, G. Manco, and E. Chabriere Structural basis for natural lactonase and promiscuous phosphotriesterase activities J. Mol. Biol. 379 2008 1017 1028
17. 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. 264 1989 9659 9666
18. M.M. Benning, H. Shim, F.M. Raushel, and H.M. Holden High-resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta Biochemistry 40 2001 2712 2722
19. H. Shim, and F.M. Raushel Self-assembly of the binuclear center of phosphotriesterase Biochemistry 39 2000 7357 7364
20. L. Merone, L. Mandrich, E. Porzio, M. Rossi, S. Muller, G. Reiter, F. Worek, and G. Manco Improving the promiscuous nerve agent hydrolase activity of a thermostable archaeal lactonase Bioresour. Technol. 101 2010 9204 9212
21. 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 89 2007 625 636
22. D. Rochu, N. Viguie, F. Renault, D. Crouzier, M.T. Froment, and P. Masson Contribution of the active site metal cation to catalytic activity and to conformational stability of phosphotriesterase: a thermo- and pH-dependence study Biochem. J. 380 2004 627 633
23. C.J. Jackson, P.D. Carr, H.K. Kim, J.W. Liu, P. Herrald, N. Mitic, G. Schenk, C.A. Smith, and D.L. Ollis Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: the prominent role of iron in the heterobinuclear active site Biochem. J. 397 2006 501 508
24. J.Y. Chow, B. Xue, K.H. Lee, A. Tung, L. Wu, R.C. Robinson, and W.S. Yew Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily J. Biol. Chem. 285 2010 40911 40920
25. D.D. Perrin, and B. Dempsey Buffer for pH and Metal Ion Control 1974 Chapman and Hall London