{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T01:24:05Z","timestamp":1792718645148,"version":"4.5.0"},"reference-count":95,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2013,1,1]],"date-time":"2013-01-01T00:00:00Z","timestamp":1356998400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2013,1]]},"DOI":"10.1016\/j.bbapap.2012.04.004","type":"journal-article","created":{"date-parts":[[2012,4,26]],"date-time":"2012-04-26T04:33:33Z","timestamp":1335414813000},"page":"443-453","source":"Crossref","is-referenced-by-count":231,"title":["Catalytic mechanisms for phosphotriesterases"],"prefix":"10.1016","volume":"1834","author":[{"given":"Andrew N.","family":"Bigley","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank M.","family":"Raushel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2012.04.004_bb0005","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1016\/S1369-5274(02)00314-4","article-title":"Bacterial detoxification of organophosphate nerve agents","volume":"5","author":"Raushel","year":"2002","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0010","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1002\/med.20192","article-title":"Design, evaluation and structure\u2013Activity relationship studies of the AChE reactivators against organophosphorus pesticides","volume":"31","author":"Musilek","year":"2011","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0015","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1289\/ehp.9410218","article-title":"Toxicity of the organophosphate chemical warfare agents GA, GB, and VX: Implications for public protection","volume":"102","author":"Munro","year":"1994","journal-title":"Environ. Health Perspect."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0020","doi-asserted-by":"crossref","first-page":"2586","DOI":"10.1128\/AEM.54.10.2586-2589.1988","article-title":"Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes","volume":"54","author":"Harper","year":"1988","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0025","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1107\/S0907444904005669","article-title":"Crystalization and preliminary X-ray studies of methyl parathion hydrolase from Pseudomonas sp. WBC-3","volume":"60","author":"Sun","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0030","doi-asserted-by":"crossref","first-page":"4922","DOI":"10.1128\/AEM.67.10.4922-4925.2001","article-title":"Isolation of methyl parathion-degrading strain M6 and cloning of the methyl parathion hydrolase gene","volume":"67","author":"Zhongli","year":"2001","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0035","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1139\/m94-160","article-title":"Degradation of methyl parathion by Pseudomonas putida","volume":"40","author":"Rani","year":"1994","journal-title":"Can. J. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0040","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1128\/jb.173.6.1938-1943.1991","article-title":"Purification and properties of an organophophorus acid anhydrase from a halophilic bacterial isolate","volume":"173","author":"DeFrank","year":"1991","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0045","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/sj.jim.2900358","article-title":"Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis","volume":"18","author":"Cheng","year":"1997","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0050","doi-asserted-by":"crossref","first-page":"3371","DOI":"10.1128\/AEM.68.7.3371-3376.2002","article-title":"Identification of an opd (organophosphate degradation) gene in an Agrobacterium isolate","volume":"68","author":"Horne","year":"2002","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0055","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/0003-9861(72)90073-2","article-title":"Purification of a DFP-hydrolyzing enzyme from squid head ganglion","volume":"150","author":"Hoskin","year":"1972","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0060","doi-asserted-by":"crossref","first-page":"10133","DOI":"10.1021\/bi00106a009","article-title":"Purification of rabbit and human serum paraoxonase","volume":"30","author":"Furlong","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0065","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.jmb.2008.04.022","article-title":"Structural basis for natural lactonase and promiscuous phosphotriesterase activities","volume":"379","author":"Elias","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0070","doi-asserted-by":"crossref","first-page":"12728","DOI":"10.1021\/bi051021e","article-title":"Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily","volume":"44","author":"Roodveldt","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0075","doi-asserted-by":"crossref","first-page":"2237","DOI":"10.1021\/bi802274f","article-title":"Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily","volume":"48","author":"Xiang","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0080","doi-asserted-by":"crossref","first-page":"6371","DOI":"10.1021\/bi047440d","article-title":"Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase","volume":"44","author":"Khersonsky","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0085","doi-asserted-by":"crossref","first-page":"3472","DOI":"10.1073\/pnas.95.7.3472","article-title":"Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli","volume":"95","author":"Wilce","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0090","doi-asserted-by":"crossref","first-page":"7973","DOI":"10.1021\/bi00025a002","article-title":"Three-dimensional structure of the binuclear metal center of phosphotriesterase","volume":"34","author":"Benning","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0095","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/j.jmb.2005.08.057","article-title":"Crystal structure of methyl parathion hydrolase from Pseudomonas sp. WBC-3","volume":"353","author":"Dong","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0100","doi-asserted-by":"crossref","first-page":"1744","DOI":"10.1107\/S0907444903016135","article-title":"Statistical analysis of crystallographic data obtained from squid ganglion DFPase at 0.85 \u00c5 resolution","volume":"59","author":"Koepke","year":"2003","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0105","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1073\/pnas.0807842106","article-title":"Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement","volume":"106","author":"Blum","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0110","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1021\/bi9011989","article-title":"Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase\/prolidase","volume":"49","author":"Vyas","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0115","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1038\/nsmb767","article-title":"Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes","volume":"11","author":"Harel","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0120","doi-asserted-by":"crossref","first-page":"13278","DOI":"10.1016\/S0021-9258(18)42207-7","article-title":"Characterization of the zinc binding site of bacterial phosphotriesterase","volume":"267","author":"Omburo","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0125","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1042\/0264-6021:3530579","article-title":"Role of calcium ions in the structure and function of the di-isopropylfluorophosphatase from Loligo vulgaris","volume":"353","author":"Hartleib","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0130","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1021\/bi001548l","article-title":"Stuctural determinants of the substrate and stereochemical specificity of phosphotriesterase","volume":"40","author":"Chen-Goodspeed","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0135","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1002\/prot.22264","article-title":"In silico analyses of substrate interactions with human serum paraoxonase 1","volume":"75","author":"Hu","year":"2009","journal-title":"Proteins"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0140","doi-asserted-by":"crossref","first-page":"9022","DOI":"10.1021\/bi0500675","article-title":"Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme","volume":"44","author":"Katsemi","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0145","doi-asserted-by":"crossref","first-page":"12750","DOI":"10.1021\/ja061887n","article-title":"Binding of a designed substrate analogue to diisopropyl fluorophosphatase: Implications for the phosphotriesterase mechanism","volume":"128","author":"Blum","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0150","doi-asserted-by":"crossref","first-page":"5707","DOI":"10.1021\/bi0497805","article-title":"Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase","volume":"43","author":"Aubert","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0155","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444910034013","article-title":"Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase)","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0160","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1128\/AEM.44.1.246-249.1982","article-title":"Plasmid involvement in parathion hydrolysis by Pseudomonas diminuta","volume":"44","author":"Serdar","year":"1982","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0165","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1128\/AEM.51.5.926-930.1986","article-title":"Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by Southern hybridization with opd form Pseudomonas diminuta","volume":"51","author":"Mulbry","year":"1986","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0170","first-page":"627","article-title":"Plasmid mediated organophosphate pesticide degradation by Flavobacterium balustinum","volume":"36","author":"Somara","year":"1995","journal-title":"Biochem. Mol. Biol. Int."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0175","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1093\/proeng\/gzg013","article-title":"Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution","volume":"16","author":"Yang","year":"2003","journal-title":"Protein Eng."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0180","doi-asserted-by":"crossref","first-page":"6020","DOI":"10.1021\/bi960325l","article-title":"Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analong diethyl 4-methylbenzylphosphonate","volume":"35","author":"Vanhooke","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0185","doi-asserted-by":"crossref","first-page":"9497","DOI":"10.1021\/bi800971v","article-title":"Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase","volume":"47","author":"Kim","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0190","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.bbapap.2005.06.008","article-title":"The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism","volume":"1752","author":"Jackson","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0195","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/j.jmb.2007.10.061","article-title":"In crystallo capture of a Mchaelis complex and product-binding modes of a bacterial phosphotriesterase","volume":"375","author":"Jackson","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0200","doi-asserted-by":"crossref","first-page":"2712","DOI":"10.1021\/bi002661e","article-title":"High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta","volume":"40","author":"Benning","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0205","doi-asserted-by":"crossref","first-page":"9148","DOI":"10.1021\/bi00086a021","article-title":"Structural characterization of the divalent cation sites of bacterial phosphotriesterase by 113Cd NMR Spectroscopy","volume":"32","author":"Omburo","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0210","doi-asserted-by":"crossref","first-page":"7438","DOI":"10.1021\/bi00244a010","article-title":"Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta","volume":"30","author":"Caldwell","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0215","doi-asserted-by":"crossref","first-page":"15892","DOI":"10.1021\/ja0658618","article-title":"Resolution of chiral phosphate, phosphonate, and phosphineate esters by an enantioselective enzyme library","volume":"128","author":"Nowlan","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0220","doi-asserted-by":"crossref","first-page":"25596","DOI":"10.1074\/jbc.272.41.25596","article-title":"Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase","volume":"272","author":"Watkins","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0225","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1016\/S0960-894X(01)80516-3","article-title":"Stereospecific enzymatic hydrolysis of phosphorus-sulfur bonds in chiral organophosphate triesters","volume":"4","author":"Chae","year":"1994","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0230","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1006\/abbi.1995.1204","article-title":"Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase","volume":"318","author":"Lai","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0235","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1006\/bbrc.1997.7569","article-title":"Enzymatic hydrolysis of Russian-VX by organophosphorus hydrolase","volume":"241","author":"Rastogi","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0240","doi-asserted-by":"crossref","first-page":"430","DOI":"10.2533\/chimia.1996.430","article-title":"Rational enzyme design: Computer modeling and site-directed mutagenesis for the modification of catalytic specificity in organophosphorus hydrolase","volume":"50","author":"Lai","year":"1996","journal-title":"Chimia"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0245","doi-asserted-by":"crossref","first-page":"17445","DOI":"10.1074\/jbc.273.28.17445","article-title":"Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase","volume":"273","author":"Shim","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0250","doi-asserted-by":"crossref","first-page":"4681","DOI":"10.1128\/AEM.70.8.4681-4685.2004","article-title":"Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos","volume":"70","author":"Cho","year":"2004","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0255","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1093\/protein\/gzj007","article-title":"Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides","volume":"19","author":"Cho","year":"2006","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0260","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1111\/j.1365-2672.2010.04672.x","article-title":"Generation of a mutagenized organophosphorus hydrolase for the biodegradation of the organophosphate pesticides malathion and demeton-S","volume":"109","author":"Schofield","year":"2010","journal-title":"J. Appl. Microbiol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0265","doi-asserted-by":"crossref","first-page":"10904","DOI":"10.1021\/bi960663m","article-title":"Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase","volume":"35","author":"Hong","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0270","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1021\/bi982204m","article-title":"Stereochmical constraints on the substrate specificity of phosphotriesterase","volume":"38","author":"Hong","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0275","doi-asserted-by":"crossref","first-page":"7978","DOI":"10.1021\/bi101056m","article-title":"Selective hydrolysis of organophosphate nerve agents by the bacterial phosphotriesterase","volume":"49","author":"Tsai","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0280","doi-asserted-by":"crossref","first-page":"2083","DOI":"10.1016\/S0968-0896(01)00113-4","article-title":"Stereoselective detoxification of chiral sarin and soman analogues by phosphotriesterase","volume":"9","author":"Li","year":"2001","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0285","doi-asserted-by":"crossref","first-page":"1332","DOI":"10.1021\/bi001549d","article-title":"Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues","volume":"40","author":"Chen-Goodspeed","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0290","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1021\/ja017840d","article-title":"Enzymatic synthesis of chiral organophosphothioates from prochiral precursors","volume":"124","author":"Li","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0295","doi-asserted-by":"crossref","first-page":"7526","DOI":"10.1021\/ja035625m","article-title":"Operational control of stereoselectivity during the enzymatic hydrolysis of racemic organophosphorus compounds","volume":"125","author":"Li","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0300","doi-asserted-by":"crossref","first-page":"8990","DOI":"10.1021\/ja0358798","article-title":"Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site","volume":"125","author":"Hill","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0305","doi-asserted-by":"crossref","first-page":"8888","DOI":"10.1021\/ja048457m","article-title":"Enzymatic resolution of chiral phosphinate esters","volume":"126","author":"Li","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0310","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1093\/protein\/gzn019","article-title":"Balancing the stability and the catalytic specificities of OP hydrolase with enhanced V-agent activities","volume":"21","author":"Reeves","year":"2008","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0315","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1021\/bi00405a030","article-title":"Mechanism and stereochemical course at the phosphorus of the reaction catalyzed by a bacterial phosphotriesterase","volume":"27","author":"Lewis","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0320","doi-asserted-by":"crossref","first-page":"11005","DOI":"10.1021\/bi0506270","article-title":"Protonation of the binuclear metal center within the active site of phosphotriesterase","volume":"44","author":"Samples","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0325","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s00775-011-0779-6","article-title":"Electronic and geometric structures of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA)","volume":"16","author":"Ely","year":"2011","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0330","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1042\/BJ20101054","article-title":"The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis","volume":"432","author":"Ely","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0335","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1021\/bi061951d","article-title":"Activation of the binuclear metal center through formation of phosphotriesterase-inhibitor complexes","volume":"46","author":"Samples","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0340","doi-asserted-by":"crossref","first-page":"7444","DOI":"10.1021\/bi00244a011","article-title":"Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis","volume":"30","author":"Caldwell","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0345","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1021\/jp068500n","article-title":"Theoretical study of the phosphotriesterase reaction mechanism","volume":"111","author":"Chen","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0350","doi-asserted-by":"crossref","first-page":"13352","DOI":"10.1021\/bi700460c","article-title":"The reaction mechanism of paraoxon hydrolysis by phosphotriesterase from combined QM\/MM simulations","volume":"46","author":"Wong","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0355","doi-asserted-by":"crossref","first-page":"2388","DOI":"10.1002\/jcc.21238","article-title":"Molecular dynamics simulations of the detoxification of paraoxon catalyzed by phosphotriesterase","volume":"30","author":"Zhang","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0360","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.molcatb.2003.09.002","article-title":"Hydrolysis of organophosphate triesters by Escherichia coli aminopeptidase P","volume":"27","author":"Jao","year":"2004","journal-title":"J. Mol. Catal. B: Enzym."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0365","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1006\/abbi.1994.1204","article-title":"Substrate specificity of aminopeptidase P from Escherichia coli: Comparison with membrane-bound forms from rat and bovine lung","volume":"311","author":"Yoshimoto","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0370","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1021\/bi0518904","article-title":"Kinetic and crystallographic analyis of mutant Escherichia coli aminopeptidase P: Insites into substrate recognition and mechanism of catalysis","volume":"45","author":"Graham","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0375","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/S0960-894X(00)00213-4","article-title":"Substrate and stereochemical specificity of the organophosphorus acid anhydrolase from Alteromonas sp. JD6.5 toward p-nitrophenyl phosphotriesters","volume":"10","author":"Hill","year":"2000","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0380","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1006\/bioo.2000.1189","article-title":"Stereochemical Specificity of organophorus acid anhydrolase toward p-nitrophenyl analogs of soman and sarin","volume":"29","author":"Hill","year":"2001","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0385","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1002\/cbic.200500412","article-title":"Aminopeptidase P mediated detoxification of organophosphonate analogues of sarin: mechanistic and stereochemical study at the phosphorus atom of the substrate","volume":"7","author":"Huang","year":"2006","journal-title":"ChemBioChem"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0390","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1073\/pnas.2536901100","article-title":"Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization","volume":"101","author":"Aharoni","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0395","doi-asserted-by":"crossref","first-page":"347","DOI":"10.2478\/v10004-007-0028-0","article-title":"3-D structure of serum paraoxonase 1 sheds light on its activity, stability, soulubility and crystallizability","volume":"58","author":"Harel","year":"2007","journal-title":"Arh. Hig. Rada Toksikol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0400","first-page":"653","article-title":"Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity","volume":"26","author":"Kuo","year":"1998","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0405","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1006\/prep.2000.1360","article-title":"High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris","volume":"21","author":"Hartleib","year":"2001","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0410","doi-asserted-by":"crossref","first-page":"5216","DOI":"10.1021\/bi702222x","article-title":"Inhibitory potency against human acetylcholinesterase and enzymatic hydrolysis of fluorogenic nerve agent mimics by human paraoxonase 1 and squid diisopropyl fluorophosphatase","volume":"47","author":"Blum","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0415","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1080\/10408360802610878","article-title":"The paraoxonases: role in human diseases and methodological difficulties in measurement","volume":"46","author":"Camps","year":"2009","journal-title":"Crit. Rev. Clin. Lab. Sci."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0420","doi-asserted-by":"crossref","first-page":"2816","DOI":"10.1021\/bi982281h","article-title":"Identification of residues essential for human paraoxonase (PON1) arylesterase\/organophosphatase activities","volume":"38","author":"Josse","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0425","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.1111\/j.1742-4658.2006.05198.x","article-title":"Enhanced stereoselective hydrolysis of toxic organophosphates by directly evolved variants of mammalian serum paraoxonase","volume":"273","author":"Amitai","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0430","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/nchembio.510","article-title":"Directed evolution of hydrolases for prevention of G-type nerve agent intoxication","volume":"7","author":"Gupta","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0435","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.bbrc.2010.10.125","article-title":"Efficient hydrolysis of the chemical warfare nerve agent tabun by recombinant and purified human and rabbit serum paraoxonase 1","volume":"403","author":"Valiyaveettil","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0440","doi-asserted-by":"crossref","first-page":"e20335","DOI":"10.1371\/journal.pone.0020335","article-title":"VX hydrolysis by human serum paraoxonase 1: A comparison of experimental and computational results","volume":"6","author":"Peterson","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0445","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1038\/ng1196-334","article-title":"The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin","volume":"14","author":"Davies","year":"1996","journal-title":"Nat. Genet."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0450","doi-asserted-by":"crossref","first-page":"17226","DOI":"10.1021\/ja905444g","article-title":"Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design","volume":"131","author":"Melzer","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0455","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.bbapap.2004.08.002","article-title":"Structure\/function analysis of human serum paraoxonase (HuPON1) mutants designed from a DFPase-like homology model","volume":"1702","author":"Yeung","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0460","doi-asserted-by":"crossref","first-page":"7649","DOI":"10.1074\/jbc.M512594200","article-title":"The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases","volume":"281","author":"Khersonsky","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0465","doi-asserted-by":"crossref","first-page":"7657","DOI":"10.1074\/jbc.M512595200","article-title":"The catalytic histidine dyad of high density lipoprotein-associated serum paraxonase-1 (PON1) is essential for PON1-mediated inhibition of low density lipoprotein oxidation and stimulation of macrophage cholesterol efflux","volume":"281","author":"Rosenblat","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2012.04.004_bb0470","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/S0167-4838(01)00153-4","article-title":"Insites into the reaction mechanism of the diisopropyl fluorophosphatase from Loligo vulgaris by means of kinetic studies, chemical modification and site-directed mutagenesis","volume":"1546","author":"Hartleib","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2012.04.004_bb0475","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0969-2126(01)00610-4","article-title":"Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris","volume":"9","author":"Scharff","year":"2001","journal-title":"Structure"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963912000660?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963912000660?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,6,22]],"date-time":"2023-06-22T05:07:54Z","timestamp":1687410474000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963912000660"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,1]]},"references-count":95,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2013,1]]}},"alternative-id":["S1570963912000660"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2012.04.004","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2013,1]]}}}