Erratum: Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase (Biochemistry (2010) 49 (547) DOI: 10.1021/bi9011989));Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase

Biochemistry

Volumn 49, Issue 3, 2010, Pages 547-559

  Vyas, Nand K ^a   Nickitenko, Alexei ^a   Rastogi, Vipin K ^b   Shah, Saumil S ^b   Quiocho, Florante A ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b EDGEWOOD CHEMICAL BIOLOGICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBOXYLATION; HYDROGEN BONDS; HYDROLYSIS; LIGANDS; PHOSPHORUS COMPOUNDS;

ACETYLCHOLINESTERASE; ACTIVE SITE RESIDUES; CHEMICAL NERVE AGENTS; NONPOLAR INTERACTIONS; ORGANOPHOSPHORUS COMPOUNDS; ORGANOPHOSPHORUS HYDROLASE; TETRAHEDRAL PHOSPHATES; X-RAY STRUCTURE DETERMINATIONS;

CATALYST ACTIVITY;

ACETYLCHOLINESTERASE; CARBOXYLIC ACID; DIPEPTIDE DERIVATIVE; FLUORINE; FLUORINE DERIVATIVE; GLYCINE; GLYCOLIC ACID; LIGAND; MANGANESE; N,N' DIISOPROPYLDIAMIDOFLUOROPHOSPHATE; N,N' DIISOPROPYLDIAMIDOPHOSPHATE; NERVE GAS; ORGANOPHOSPHATE ANHYDROLASE; ORGANOPHOSPHORUS COMPOUND; PHOSPHATE; PROLINE DIPEPTIDASE; UNCLASSIFIED DRUG;

ALTEROMONAS; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; DENSITY; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROGEN BOND; HYDROLYSIS; LIGAND BINDING; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY;

ALTEROMONAS SP.;

EID: 74949127023     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100138q     Document Type: Erratum

References (51)

1. Mazur, A., and Bodansky, O. (1945) The mechanism of in vitro and in vivo inhibition of cholinesterase activity by diisopropyl fluorophosphate. J. Biol. Chem. 163, 261-276.
2. Mazur, A. (1946) An enzyme in animal tissues capable of hydrolyzing the phosphorus-fluorine bond of alkyl fluorophosphate. J. Biol. Chem. 164, 271-286.
3. Hoskins, F. C. G., Kirkish, M. A., and Steinmann, K. E. (1984) Two enzymes for the detoxification of organophosphorus compoounds: Sources, similarities, and significance. Fundam. Appl. Toxicol. 4, 165-172.
4. DeFrank, J. J., and Cheng, T.-C. (1991) Purification and properties of an organophosphorus acid anhydrolase from a halophilic bacterial isolate. J. Bacteriol. 173, 1938-1943.
5. Cheng, T.-C., Harvey, S. P., and Stroup, A. N. (1993) Purification and properties of a highly active organophosphorus acid anhydrolase from Alteromonas undina. Appl. Environ. Microbiol. 59, 3138-3140.
6. Cheng, T.-C., Liu, L., Wang, B., DeFrank, J. J., Rastogi, V. K., and Hamilton, A. B. (1997) Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis. J. Ind. Microbiol. Biotechnol. 18, 49-55.
7. Sutherland, T. D., Horne, I., Weir, K. M., Coppin, C. W., Williams, M. R., Selleck, M., Russell, R. J., and Oakeshott, J. G. (2004) Enzymatic bioremediation: From enzyme discovery to applications. Clin. Exp. Pharmacol. Physiol. 31, 817-821.
8. LeJeune, K. E., Dravis, B. C., Yang, F., Hetro, A. D., Doctor, B. P., and Russell, A. J. (1998) Fighting nerve agent chemical weapons with enzyme technology. Ann. N.Y. Acad. Sci. 864, 153-170.
9. LeJeune, K. E., Wild, J. R., and Russell, A. J. (1998) Nerve agents degraded by enzymatic foams. Nature 395, 27-28.
10. Kropp, T. J., and Richardson, R. J. (2006) Aging of mipafox-inhibited human acetylcholinesterase proceeds by displacement of both isopropylamine groups to yield a phosphate adduct. Chem. Res. Toxicol. 19, 334-339.
11. Glynn, P., Read, D. J., Lush, M. J., Li, Y., and Atkins, J. (1999) Molecular cloning of neuropathy target esterase (NTE). Chem.-Biol. Interact. 119-120, 513-517.
12. Akassoglou, K., Malester, B., Xu, J., Tessarollo, L., Rosenbluth, J., and Chao, M. V. (2004) Brain-specific deletion of neuropathy target esterase/swisscheese results in neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 101, 5075-5080.
13. Kropp, T. J., Glynn, P., and Richardson, R. J. (2004) The mipafox-inhibited catalytic domain of human neuropathy target esterase ages by reversible proton loss. Biochemistry 43, 3716-3722.
14. Cheng, T.-C., Harvey, S. P., and Chen, G. L. (1996) Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme. Appl. Environ. Microbiol. 62, 1636-1641.
15. Maher, M. J., Ghosh, M., Grunden, A. M., Menon, A. L., Adams, M. W., Freeman, H. C., and Guss, J. M. (2004) Structure of the prolidase from Pyrococcus furiosus. Biochemistry 43, 2771-2783.
16. Yaron, A., and Mlynar, D. (1968) Aminopeptidase-P. Biochem. Biophys. Res. Commun. 32, 658-663.
17. Kurien, B. T., Patel, N. C., Porter, A. C., D'Souza, A., Miller, D., Matsumoto, H., Wang, H., and Scofield, R. H. (2006) Prolidase deficiency and the biochemical assays used in its diagnosis. Anal. Biochem. 349, 165-175.
18. Cheng, T.-C., DeFrank, J. J., and Rastogi, V. K. (1999) Alteromonas prolidase for organophosphorus G-agent decontamination. Chem.- Biol. Interact. 119-120, 455-462.
19. Leslie, A. (1992) Recent changes to the MOSFLM package for processing film and image plate data, Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography, Vol. 26.
20. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
21. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve,R.W., Jiang, J. S.,Kuszewski, J., Nilges,M., Pannu, N. S.,Read, R. J.,Rice, L. M., Simonson, T., andWarren,G. L. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905-921.
22. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaad, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
23. Sack, J., and Quiocho, F. (1997) CHAIN: A crystallographic modelling program. Methods Enzymol. 277, 158-173.
24. Lawskowski, R. A., McArthur, M. W., Moss, D. S., and Thorton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 282-291.
25. Kraulis, P. (1991) MOLSCRIPT:Aprogram to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
26. Wallace, A. C., Laskowski, R. A., and Thornton, J. M. (1995) LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134.
27. Bahadur, R. P., and Zacharias, M. (2008) The interface of protein-protein complexes: Analysis of contacts and prediction interactions. Cell. Mol. Life Sci. 65, 1059-1072.
28. Roderick, S. L., and Matthews, B. W. (1993) Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: A new type of proteolytic enzyme. Biochemistry 32, 3907-3912.
29. Carrel, J. C., Carrel, H. L., Erlebacher, J., and Glusker, J. P. (1988) Structural aspects of metal ion-carboxylate interactions. J. Am. Chem. Soc. 110, 8651-8656.
30. Christianson, D. W. (1997) Structural chemistry and biology of manganese metalloenzymes. Prog. Biophys. Mol. Biol. 67, 217-252.
31. Wilce, M. C., Bond, C. S., Dixon, N. E., Freeman, H. C., Guss, J. M., Lilley, P. E., and Wilce, J. A. (1998) Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 95, 3472-3477.
32. Levitt, M., and Perutz, M. F. (1988) Aromatic rings act as hydrogen bond acceptors. J. Mol. Biol. 201, 751-754.
33. Hoskins, F. C. G. (1985) Inhibition of a soman- and diisopropylphosphorofluorodate (DFP)-detoxifying enzyme by mipafox. Biochem. Pharmacol. 34, 2069-2072.
34. Johnson, M. K. (1977) Improved assay of neurotoxic esterase for screening organophosphates for delayed neurotoxicity potential. Arch. Toxicol. 37, 113-115.
35. Graham, S. C., and Guss, J. M. (2008) Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Arch. Biochem. Biophys. 469, 200-208.
36. Zheng, J., Constantine, C. A., Zhao, L., Rastogi, V. K., Cheng, T. C., Defrank, J. J., and Leblanc, R. M. (2005) Molecular interaction between organophosphorus acid anhydrolase and diisopropylfluorophosphate. Biomacromolecules 6, 1555-1560.
37. Graham, S. C., Maher, M. J., Simmons, W. H., Freeman, H. C., and Guss, J. M. (2004) Structure of Escherichia coli aminopeptidase P in the complex with the inhibitor apstatin. Acta Crystallogr. D60, 1770-1779.
38. Graham, S. C., Bond, C. S., Freeman, H. C., and Guss, J. M. (2005) Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center. Biochemistry 44, 13820-13836.
39. Graham, S. C., Lilley, P. E., Lee, M., Schaeffer, P. M., Kralicek, A. V., Dixon, N. E., and Guss, J. M. (2006) Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: Insights into substrate recognition and the mechanism of catalysis. Biochemistry 45, 964-975.
40. Ghanem, E., and Raushel, F. M. (2005) Detoxification of organophosphate nerve agents by bacterial phosphotriesterase. Toxicol. Appl. Pharmacol. 207, S459-S470.
41. Kim, J., Tsai, P.-C., Chen, S.-L., Himo, F., Almo, S. C., and Raushel, F. M. (2008) Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase. Biochemistry 47, 9497-9504.
42. Aubert, S. D., Li, Y., and Raushel, F. M. (2004) Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase. Biochemistry 43, 5707-5715.
43. Hill, C. M., Wu, F., Cheng, T.-C., DeFrank, J. J., and Raushel, F. M. (2000) Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteronomonas sp. JD6.5 toward p-nitrophenyl phosphotriesters. Bioorg. Med. Chem. Lett. 10, 1285-1288.
44. Hill, C. M., Li, W. S., Cheng, T.-C., DeFrank, J. J., and Raushel, F. M. (2001) Stereochemical specificity of organophosphorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin. Bioorg. Chem. 29, 27-35.
45. Vanhooke, J. L., Benning, M. M., Raushel, F. M., and Holden,H.M. (1996) Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzyl-phosphonate. Biochemistry 35, 6020-6025.
46. Lewis, V. E., Donarski, W. J., Wild, J. R., and Raushel, F. M. (1988) Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase. Biochemistry 27, 1591-1597.
47. Huang, L.-F., Su, B., Jao, S.-C., Liu, K.-T., and Li, W.-S. (2006) Aminopeptidase P mediated detoxification of organophosphonate analogues of sarin: Mechanistic and stereochemical study at the phosphorus atom of the substrate. ChemBioChem 7, 506-514.
48. Benning, M. M., Hong, S.-B., Raushel, F. M., and Holden, H. M. (2000) The binding of substrate analogs to phosphotriesterase. J. Biol. Chem. 275, 30556-30560.
49. Lowther, T. W., Zhang, Y., Sampson, P. B., Honek, J. F., and Matthews, B. W. (1999) Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structure analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry 38, 14810-14819.
50. Copik, A. J., Nocek, G. P., Swierczek, S. I., Ruebush, S., Jang, S. B., Meng, L., D'Souza, V. M., Peters, J. W., Bennett, B., and Holz, R. C. (2005) EPR and X-ray crystallographic characterization of the product-bound form of the MnII-loaded methionyl aminopeptidase from Pyrococcus furiosus. Biochemistry 44, 121-129.
51. Harding, M. M. (2006) Small revisions to predicted distances around metal sites in proteins. Acta Crystallogr. D62, 678-682.