{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T00:25:41Z","timestamp":1789431941342,"version":"build-2803163510"},"reference-count":51,"publisher":"American Chemical Society (ACS)","issue":"51","license":[{"start":{"date-parts":[[2015,12,16]],"date-time":"2015-12-16T00:00:00Z","timestamp":1450224000000},"content-version":"vor","delay-in-days":14,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000774","name":"Defense Threat Reduction Agency","doi-asserted-by":"publisher","award":["HDTRA1-14-1-0004"],"award-info":[{"award-number":["HDTRA1-14-1-0004"]}],"id":[{"id":"10.13039\/100000774","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,12,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The most familiar organophosphorus compounds are the neurotoxic insecticides and nerve agents. A related group of organophosphorus compounds, the phosphotriester plasticizers and flame retardants, has recently become widely used. Unlike the neurotoxic phosphotriesters, the plasticizers and flame retardants lack an easily hydrolyzable bond. While the hydrolysis of the neurotoxic organophosphates by phosphotriesterase enzymes is well-known, the lack of a labile bond in the flame retardants and plasticizers renders them inert to typical phosphotriesterases. A phosphotriesterase from Sphingobium sp. strain TCM1 (Sb-PTE) has recently been reported to catalyze the hydrolysis of organophosphorus flame retardants. This enzyme has now been expressed in Escherichia coli, and the activity with a wide variety of organophosphorus substrates has been characterized and compared to the activity of the well-known phosphotriesterase from Pseudomonas diminuta (Pd-PTE). Structure prediction suggests that Sb-PTE has a \u03b2-propeller fold, and homology modeling has identified a potential mononuclear manganese binding site. Sb-PTE exhibits catalytic activity against typical phosphotriesterase substrates such as paraoxon, but unlike Pd-PTE, Sb-PTE is also able to effectively hydrolyze flame retardants, plasticizers, and industrial solvents. Sb-PTE can hydrolyze both phosphorus\u2013oxygen bonds and phosphorus\u2013sulfur bonds, but not phosphorus\u2013nitrogen bonds. The best substrate for Sb-PTE is the flame retardant triphenyl phosphate with a kcat\/Km of 1.7 \u00d7 106 M\u20131 s\u20131. Quite remarkably, Sb-PTE is also able to hydrolyze phosphotriesters with simple alcohol leaving groups such as tributyl phosphate (kcat\/Km = 40 M\u20131 s\u20131), suggesting that this enzyme could be useful for the bioremediation of a wide variety of organophosphorus compounds.<\/jats:p>","DOI":"10.1021\/acs.biochem.5b01144","type":"journal-article","created":{"date-parts":[[2015,12,2]],"date-time":"2015-12-02T11:53:28Z","timestamp":1449057208000},"page":"7539-7549","source":"Crossref","is-referenced-by-count":36,"title":["Interrogation of the Substrate Profile and Catalytic\nProperties of the Phosphotriesterase from\n                    <i>Sphingobium<\/i>\n                    sp. Strain TCM1: An Enzyme Capable of Hydrolyzing Organophosphate\nFlame Retardants and Plasticizers"],"prefix":"10.1021","volume":"54","author":[{"given":"Dao Feng","family":"Xiang","sequence":"first","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew N.","family":"Bigley","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhongjie","family":"Ren","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haoran","family":"Xue","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth G.","family":"Hull","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Romo","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Frank M.","family":"Raushel","sequence":"additional","affiliation":[{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]},{"name":"Texas A&M University , , , ,","place":["College Station, Texas, United States, 77843"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2015,12,2]]},"reference":[{"key":"2026090401114188700_cit1","doi-asserted-by":"publisher","first-page":"756","DOI":"10.1007\/s00204-006-0120-2","article-title":"Acetylcholinesterase\ninhibition: does it explain the toxicity of organophosphorus compounds?","volume":"80","author":"Maxwell","year":"2006","journal-title":"Arch. Toxicol."},{"key":"2026090401114188700_cit2","doi-asserted-by":"publisher","first-page":"727","DOI":"10.1016\/j.trac.2008.07.002","article-title":"Organophosphorus flame retardants and plasticizers\nin water and air I. Occurrence and fate","volume":"27","author":"Reemtsma","year":"2008","journal-title":"TrAC,\nTrends Anal. Chem."},{"key":"2026090401114188700_cit3","doi-asserted-by":"publisher","first-page":"1119","DOI":"10.1016\/j.chemosphere.2012.03.067","article-title":"Phosphorus flame retardants: properties,\nproduction, environmental occurrence, toxicity and analysis","volume":"88","author":"van der Veen","year":"2012","journal-title":"Chemosphere"},{"key":"2026090401114188700_cit4","doi-asserted-by":"publisher","first-page":"2394","DOI":"10.1021\/cb4004892","article-title":"Engineering\nV-type nerve agents detoxifying enzymes using computationally focused\nlibraries","volume":"8","author":"Cherny","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"2026090401114188700_cit5","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1016\/j.jhazmat.2007.12.099","article-title":"Degradation of nerve\nagents by an organophosphate-degrading agent (OpdA)","volume":"157","author":"Dawson","year":"2008","journal-title":"J. Hazard. Mater."},{"key":"2026090401114188700_cit6","doi-asserted-by":"crossref","first-page":"19659","DOI":"10.1016\/S0021-9258(19)47164-0","article-title":"Purification\nand\nproperties of the phosphotriesterase from Pseudomonas diminuta","volume":"264","author":"Dumas","year":"1989","journal-title":"J. Biol. Chem."},{"key":"2026090401114188700_cit7","doi-asserted-by":"publisher","first-page":"10904","DOI":"10.1021\/bi960663m","article-title":"Metal-substrate\ninteractions facilitate the catalytic\nactivity of the bacterial phosphotriesterase","volume":"35","author":"Hong","year":"1996","journal-title":"Biochemistry"},{"key":"2026090401114188700_cit8","doi-asserted-by":"publisher","first-page":"6463","DOI":"10.1021\/bi300811t","article-title":"Enzymes for the\nhomeland defense: optimizing phosphotriesterase\nfor the hydrolysis of organophosphate nerve agents","volume":"51","author":"Tsai","year":"2012","journal-title":"Biochemistry"},{"key":"2026090401114188700_cit9","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1093\/proeng\/gzg013","article-title":"Evolution of an organophosphate-degrading enzyme: a\ncomparison of natural and directed evolution","volume":"16","author":"Yang","year":"2003","journal-title":"Protein Eng., Des. Sel."},{"key":"2026090401114188700_cit10","doi-asserted-by":"publisher","first-page":"5866","DOI":"10.1128\/AEM.01845-14","article-title":"Haloalkylphosphorus hydrolases purified\nfrom Sphingomonas sp. strain TDK1 and Sphingobium sp. strain TCM1","volume":"80","author":"Abe","year":"2014","journal-title":"Appl. Environ. Microbiol."},{"key":"2026090401114188700_cit11","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1021\/bi001548l","article-title":"Structural\ndeterminants of the substrate and stereochemical specificity of phosphotriesterase","volume":"40","author":"Chen-Goodspeed","year":"2001","journal-title":"Biochemistry"},{"key":"2026090401114188700_cit12","doi-asserted-by":"publisher","first-page":"371","DOI":"10.1016\/j.bbrc.2007.01.186","article-title":"Dialkyl phenyl phosphates as novel selective inhibitors\nof butyrylcholinesterase","volume":"355","author":"Law","year":"2007","journal-title":"Biochem. Biophys.\nRes. Commun."},{"key":"2026090401114188700_cit13","doi-asserted-by":"publisher","first-page":"10426","DOI":"10.1021\/ja402832z","article-title":"Enzymatic neutralization\nof the chemical warfare agent VX: evolution of phosphotriesterase\nfor phosphorothiolate hydrolysis","volume":"135","author":"Bigley","year":"2013","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090401114188700_cit14","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1016\/S0968-0896(01)00306-6","article-title":"A pH sensitive colorometric\nassay for the high-throughput\nscreening of enzyme inhibitors and substrates: a case study using\nkinases","volume":"10","author":"Chapman","year":"2002","journal-title":"Bioorg. Med. Chem."},{"key":"2026090401114188700_cit15","doi-asserted-by":"publisher","first-page":"2237","DOI":"10.1021\/bi802274f","article-title":"Functional annotation\nand three-dimensional structure\nof Dr0930 from Deinococcus radiodurans, a close relative\nof phosphotriesterase in the amidohydrolase superfamily","volume":"48","author":"Xiang","year":"2009","journal-title":"Biochemistry"},{"key":"2026090401114188700_cit16","first-page":"333","article-title":"Die Kinetik der Invertinwirkung","volume":"49","author":"Michaelis","year":"1913","journal-title":"Biochemische Zeitschrift"},{"key":"2026090401114188700_cit17","doi-asserted-by":"publisher","first-page":"735","DOI":"10.1002\/prac.19873290426","article-title":"Direct conversion of alcohols into phosphorothiolates","volume":"329","author":"Mlotkowska","year":"1987","journal-title":"J. Prakt. Chem."},{"key":"2026090401114188700_cit18","doi-asserted-by":"publisher","first-page":"4189","DOI":"10.1021\/jo200522w","article-title":"Electrophilic trifluoromethylation\nof S-hydrogen phosphorothioates","volume":"76","author":"Santschi","year":"2011","journal-title":"J. Org. Chem."},{"key":"2026090401114188700_cit19","doi-asserted-by":"publisher","first-page":"2225","DOI":"10.1021\/ja00188a042","article-title":"Acetylenic esters -\npreparation and characterization of alkynyl dialkyl phosphates, RC\n= COPO(OR\u2032)2","volume":"111","author":"Stang","year":"1989","journal-title":"J. Am. Chem.\nSoc."},{"key":"2026090401114188700_cit20","doi-asserted-by":"publisher","first-page":"5078","DOI":"10.1021\/ol301675v","article-title":"Oxidative cleavage of alpha-aryl aldehydes using iodosylbenzene","volume":"14","author":"Havare","year":"2012","journal-title":"Org. Lett."},{"key":"2026090401114188700_cit21","unstructured":"Smith, N. D., Kahraman, M., Govek, S. P., Nagasawa, J. Y., and Lai, A. G. (2012) Estrogen receptor modulators and use thereof. U.K.\nPatent Application GB 2,483,736 (A)."},{"key":"2026090401114188700_cit22","doi-asserted-by":"publisher","first-page":"2856","DOI":"10.1038\/nprot.2006.468","article-title":"In-gel digestion\nfor mass spectrometric characterization of proteins and proteomes","volume":"1","author":"Shevchenko","year":"2007","journal-title":"Nat. Protoc."},{"key":"2026090401114188700_cit23","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.jsb.2008.04.003","article-title":"The leptospiral\nantigen Lp49 is a two-domain protein with putative protein binding\nfunction","volume":"163","author":"Giuseppe","year":"2008","journal-title":"J. Struct. Biol."},{"key":"2026090401114188700_cit24","doi-asserted-by":"publisher","first-page":"W38","DOI":"10.1093\/nar\/gkr441","article-title":"FFAS server: novel\nfeatures and applications","volume":"39","author":"Jaroszewski","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2026090401114188700_cit25","doi-asserted-by":"publisher","first-page":"363","DOI":"10.1038\/nprot.2009.2","article-title":"Protein\nstructure prediction on the Web: a case study\nusing the Phyre server","volume":"4","author":"Kelley","year":"2009","journal-title":"Nat. Protoc."},{"key":"2026090401114188700_cit26","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a\nvisualization system\nfor exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput.\nChem."},{"key":"2026090401114188700_cit27","volume-title":"Mechanism Based Enzyme Inactivation: Chemistry and Enzymology","author":"Silverman","year":"1988"},{"key":"2026090401114188700_cit28","first-page":"1890","article-title":"Cloning and expression\nof a parathion hydrolase gene from a soil bacterium, Burkholderia sp. JBA3","volume":"17","author":"Kim","year":"2007","journal-title":"J. Microbiol. Biotechnol."},{"key":"2026090401114188700_cit29","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1263\/jbb.101.80","article-title":"Purification and characterization\nof fenitrothion hydrolase\nfrom Burkholderia sp. NF100","volume":"101","author":"Tago","year":"2006","journal-title":"J. Biosci. Bioeng."},{"key":"2026090401114188700_cit30","doi-asserted-by":"publisher","first-page":"1453","DOI":"10.1016\/S0969-2126(02)00840-7","article-title":"Archaeal surface\nlayer proteins contain beta propeller, PKD, and beta helix domains\nand are related to metazoan cell surface proteins","volume":"10","author":"Jing","year":"2002","journal-title":"Structure"},{"key":"2026090401114188700_cit31","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1016\/j.jmb.2012.02.042","article-title":"Catalytic versatility\nand backups\nin enzyme active sites: the case of serum paraoxonase 1","volume":"418","author":"Ben-David","year":"2012","journal-title":"J. Mol. Biol."},{"key":"2026090401114188700_cit32","doi-asserted-by":"publisher","first-page":"12750","DOI":"10.1021\/ja061887n","article-title":"Binding of a designed substrate analogue to diisopropyl\nfluorophosphatase: implications for the phosphotriesterase mechanism","volume":"128","author":"Blum","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"2026090401114188700_cit33","doi-asserted-by":"publisher","first-page":"7649","DOI":"10.1074\/jbc.M512594200","article-title":"The histidine 115-histidine 134 dyad mediates the lactonase\nactivity of mammalian serum paraoxonases","volume":"281","author":"Khersonsky","year":"2006","journal-title":"J.\nBiol. Chem."},{"key":"2026090401114188700_cit34","doi-asserted-by":"publisher","first-page":"S15","DOI":"10.1186\/1471-2105-9-S12-S15","article-title":"Flanking signal and mature peptide residues influence\nsignal peptide cleavage","volume":"9","author":"Choo","year":"2008","journal-title":"BMC Bioinf."},{"key":"2026090401114188700_cit35","doi-asserted-by":"publisher","first-page":"10368","DOI":"10.3390\/ijms130810368","article-title":"Macromolecule-assisted de novo protein folding","volume":"13","author":"Choi","year":"2012","journal-title":"Int. J. Mol.\nSci."},{"key":"2026090401114188700_cit36","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/S0090-9556(25)06732-7","article-title":"Comparison\nof purified human and rabbit serum paraoxonases","volume":"23","author":"Kuo","year":"1995","journal-title":"Drug Metab. Dispos."},{"key":"2026090401114188700_cit37","doi-asserted-by":"publisher","first-page":"15892","DOI":"10.1021\/ja0658618","article-title":"Resolution of chiral\nphosphate, phosphonate, and phosphinate esters by an enantioselective\nenzyme library","volume":"128","author":"Nowlan","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"2026090401114188700_cit38","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1080\/009841099157638","article-title":"Comparison\nof neurotoxic effects and potential risks from oral administration\nor ingestion of tricresyl phosphate and jet engine oil containing\ntricresyl phosphate","volume":"57","author":"Mackerer","year":"1999","journal-title":"J. Toxicol. Environ. Health,\nPart A"},{"key":"2026090401114188700_cit39","volume-title":"International\nprogramme on chemical safety-environmental heath criteria 112-tri-n-butyl\nphosphate","author":"Nakamura","year":"1991"},{"key":"2026090401114188700_cit40","doi-asserted-by":"publisher","first-page":"2180","DOI":"10.2134\/jeq2003.2180","article-title":"Cotton defoliant\nrunoff as a function of active ingredient and tillage","volume":"32","author":"Potter","year":"2003","journal-title":"J. Environ. Qual."},{"key":"2026090401114188700_cit41","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1021\/bi00003a006","article-title":"Mechanism-based inactivation of phosphotriesterase\nby reaction of a critical histidine with a ketene intermediate","volume":"34","author":"Banzon","year":"1995","journal-title":"Biochemistry"},{"key":"2026090401114188700_cit42","doi-asserted-by":"publisher","first-page":"4597","DOI":"10.1021\/ja00948a035","article-title":"Steric\nEffects in hydrolysis of N-acylimidazoles and esters of p-nitrophenol","volume":"87","author":"Fife","year":"1965","journal-title":"J. Am. Chem. Soc."},{"key":"2026090401114188700_cit43","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1107\/S1744309106008402","article-title":"Structure\nof the manganese superoxide dismutase from Deinococcus radiodurans\nin two crystal forms","volume":"62","author":"Dennis","year":"2006","journal-title":"Acta Crystallogr., Sect.\nF: Struct. Biol. Cryst. Commun."},{"key":"2026090401114188700_cit44","doi-asserted-by":"publisher","first-page":"19867","DOI":"10.1074\/jbc.M313820200","article-title":"A closed conformation of Bacillus\nsubtilis oxalate\ndecarboxylase OxdC provides evidence for the true identity of the\nactive site","volume":"279","author":"Just","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2026090401114188700_cit45","doi-asserted-by":"publisher","first-page":"2330","DOI":"10.1107\/S0907444913021665","article-title":"Structural\ninsight into L-ribulose 3-epimerase from Mesorhizobium loti","volume":"69","author":"Uechi","year":"2013","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"key":"2026090401114188700_cit46","doi-asserted-by":"publisher","first-page":"443","DOI":"10.1016\/j.jmb.2007.09.033","article-title":"Crystal structures\nof D-tagatose 3-epimerase from Pseudomonas cichorii and its complexes with D-tagatose and\nD-fructose","volume":"374","author":"Yoshida","year":"2007","journal-title":"J. Mol. Biol."},{"key":"2026090401114188700_cit47","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.jsb.2014.12.003","article-title":"Structure of inorganic\npyrophosphatase from Staphylococcus aureus reveals conformational\nflexibility of the active site","volume":"189","author":"Gajadeera","year":"2015","journal-title":"J. Struct. Biol."},{"key":"2026090401114188700_cit48","doi-asserted-by":"publisher","first-page":"1020","DOI":"10.1002\/cmdc.201200076","article-title":"Hydroxamic acids as potent inhibitors\nof Fe(II) and Mn(II) E. coli methionine aminopeptidase:\nbiological activities and X-ray structures of oxazole hydroxamate-EcMetAP-Mn\ncomplexes","volume":"7","author":"Huguet","year":"2012","journal-title":"ChemMedChem"},{"key":"2026090401114188700_cit49","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1016\/j.jsb.2011.05.002","article-title":"Crystal\nstructures of Pseudomonas aeruginosa guanidinobutyrase\nand guanidinopropionase, members of the ureohydrolase superfamily","volume":"175","author":"Lee","year":"2011","journal-title":"J. Struct. Biol."},{"key":"2026090401114188700_cit50","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1107\/S1744309113002674","article-title":"Organophosphorus acid\nanhydrolase\nfrom Alteromonas macleodii: structural study and\nfunctional relationship to prolidases","volume":"69","author":"Stepankova","year":"2013","journal-title":"Acta\nCrystallogr., Sect. F: Struct. Biol. Cryst. Commun."},{"key":"2026090401114188700_cit51","doi-asserted-by":"publisher","first-page":"1591","DOI":"10.1021\/bi00405a030","article-title":"Mechanism and stereochemical\ncourse at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase","volume":"27","author":"Lewis","year":"1988","journal-title":"Biochemistry"}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.5b01144","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/54\/51\/7539\/67277856\/acs.biochem.5b01144.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/54\/51\/7539\/67277856\/acs.biochem.5b01144.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T14:09:13Z","timestamp":1788790153000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/54\/51\/7539\/1477234\/Interrogation-of-the-Substrate-Profile-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,12,2]]},"references-count":51,"journal-issue":{"issue":"51","published-online":{"date-parts":[[2015,12,2]]},"published-print":{"date-parts":[[2015,12,29]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.5b01144","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12,2]]}}}