메뉴 건너뛰기




Volumn 54, Issue 35, 2015, Pages 5502-5512

Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; CHEMICAL WARFARE; DETOXIFICATION; ENZYMES; HAZARDOUS MATERIALS; HYDROGEN BONDS; HYDROLYSIS; METAL IONS; METALS; STEREOCHEMISTRY; STEREOSELECTIVITY;

EID: 84941116942     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00629     Document Type: Article
Times cited : (56)

References (34)
  • 1
    • 0000737686 scopus 로고
    • Nerve agent stereoisomers: Analysis, isolation and toxicology
    • Benschop, H. P. and De Jong, L. P. A. (1988) Nerve agent stereoisomers: analysis, isolation and toxicology Acc. Chem. Res. 21, 368-374 10.1021/ar00154a003
    • (1988) Acc. Chem. Res. , vol.21 , pp. 368-374
    • Benschop, H.P.1    De Jong, L.P.A.2
  • 2
    • 84900449846 scopus 로고    scopus 로고
    • Lessons Learned from the Syrian Sarin Attack: Evaluation of a Clinical Syndrome Through Social MediaLessons Learned from the Syrian Sarin Attack
    • Rosman, Y., Eisenkraft, A., Milk, N., Shiyovich, A., Ophir, N., Shrot, S., Kreiss, Y., and Kassirer, M. (2014) Lessons Learned From the Syrian Sarin Attack: Evaluation of a Clinical Syndrome Through Social MediaLessons Learned From the Syrian Sarin Attack Ann. Intern. Med. 160, 644-648 10.7326/M13-2799
    • (2014) Ann. Intern. Med. , vol.160 , pp. 644-648
    • Rosman, Y.1    Eisenkraft, A.2    Milk, N.3    Shiyovich, A.4    Ophir, N.5    Shrot, S.6    Kreiss, Y.7    Kassirer, M.8
  • 3
    • 0036798853 scopus 로고    scopus 로고
    • A review of nerve agent exposure for the critical care physician
    • Leikin, J. B., Thomas, R. G., Walter, F. G., Klein, R., and Meislin, H. W. (2002) A review of nerve agent exposure for the critical care physician Crit. Care Med. 30, 2346-2354 10.1097/00003246-200210000-00026
    • (2002) Crit. Care Med. , vol.30 , pp. 2346-2354
    • Leikin, J.B.1    Thomas, R.G.2    Walter, F.G.3    Klein, R.4    Meislin, H.W.5
  • 5
    • 78549267772 scopus 로고    scopus 로고
    • Prophylaxis with human serum butyrylcholinesterase protects Guinea pigs exposed to multiple lethal doses of soman or VX
    • Saxena, A., Sun, W., Fedorko, J. M., Koplovitz, I., and Doctor, B. P. (2011) Prophylaxis with human serum butyrylcholinesterase protects guinea pigs exposed to multiple lethal doses of soman or VX Biochem. Pharmacol. 81, 164-169 10.1016/j.bcp.2010.09.007
    • (2011) Biochem. Pharmacol. , vol.81 , pp. 164-169
    • Saxena, A.1    Sun, W.2    Fedorko, J.M.3    Koplovitz, I.4    Doctor, B.P.5
  • 6
    • 84941075595 scopus 로고    scopus 로고
    • FLIR Systems Threat Detection Technologies: Enzymes, FLIR Systems, Wilsonville, OR, (accessed 8/4/15)
    • FLIR Systems Threat Detection Technologies: Enzymes, FLIR Systems, Wilsonville, OR, http://www.flir.com/threatdetection/display/?id=63297 (accessed 8/4/15).
  • 7
    • 84880392305 scopus 로고    scopus 로고
    • Enzymatic neutralization of the chemical warfare agent VX: Evolution of phosphotriesterase for phosphorothiolate hydrolysis
    • Bigley, A. N., Xu, C., Henderson, T. J., Harvey, S. P., and Raushel, F. M. (2013) Enzymatic neutralization of the chemical warfare agent VX: evolution of phosphotriesterase for phosphorothiolate hydrolysis J. Am. Chem. Soc. 135, 10426-10432 10.1021/ja402832z
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 10426-10432
    • Bigley, A.N.1    Xu, C.2    Henderson, T.J.3    Harvey, S.P.4    Raushel, F.M.5
  • 8
    • 0030901409 scopus 로고    scopus 로고
    • Nucleotide sequence of a gene encoding an organophosphorus nerve agent degrading enzyme from Alteromonas haloplanktis
    • Cheng, T., Liu, L., Wang, B., Wu, J., DeFrank, J. J., Anderson, D. M., 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 10.1038/sj.jim.2900358
    • (1997) J. Ind. Microbiol. Biotechnol. , vol.18 , pp. 49-55
    • Cheng, T.1    Liu, L.2    Wang, B.3    Wu, J.4    DeFrank, J.J.5    Anderson, D.M.6    Rastogi, V.K.7    Hamilton, A.B.8
  • 10
    • 84875811941 scopus 로고    scopus 로고
    • Human paraoxonase double mutants hydrolyze v and G class organophosphorus nerve agents
    • Kirby, S. D., Norris, J. R., Richard Smith, J., Bahnson, B. J., and Cerasoli, D. M. (2013) Human paraoxonase double mutants hydrolyze V and G class organophosphorus nerve agents Chem.-Biol. Interact. 203, 181-185 10.1016/j.cbi.2012.10.023
    • (2013) Chem.-Biol. Interact. , vol.203 , pp. 181-185
    • Kirby, S.D.1    Norris, J.R.2    Richard Smith, J.3    Bahnson, B.J.4    Cerasoli, D.M.5
  • 11
    • 72249111746 scopus 로고    scopus 로고
    • Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design
    • Melzer, M., Chen, J. C., Heidenreich, A., Gab, J., Koller, M., Kehe, K., and Blum, M. M. (2009) Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design J. Am. Chem. Soc. 131, 17226-17232 10.1021/ja905444g
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17226-17232
    • Melzer, M.1    Chen, J.C.2    Heidenreich, A.3    Gab, J.4    Koller, M.5    Kehe, K.6    Blum, M.M.7
  • 12
    • 84865146694 scopus 로고    scopus 로고
    • Enzymes for the homeland defense: Optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents
    • Tsai, P. C., Fox, N., Bigley, A. N., Harvey, S. P., Barondeau, D. P., and Raushel, F. M. (2012) Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents Biochemistry 51, 6463-6475 10.1021/bi300811t
    • (2012) Biochemistry , vol.51 , pp. 6463-6475
    • Tsai, P.C.1    Fox, N.2    Bigley, A.N.3    Harvey, S.P.4    Barondeau, D.P.5    Raushel, F.M.6
  • 15
    • 0033586351 scopus 로고    scopus 로고
    • Biocatalytic nerve agent detoxification in fire fighting foams
    • LeJeune, K. E. and Russell, A. J. (1999) Biocatalytic nerve agent detoxification in fire fighting foams Biotechnol. Bioeng. 62, 659-665 10.1002/(SICI)1097-0290(19990320)62:6<659::AID-BIT5>3.0.CO;2-N
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 659-665
    • LeJeune, K.E.1    Russell, A.J.2
  • 17
    • 33644984271 scopus 로고    scopus 로고
    • Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides
    • Mee-Hie Cho, C., Mulchandani, A., and Chen, W. (2006) Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides Protein Eng., Des. Sel. 19, 99-105 10.1093/protein/gzj007
    • (2006) Protein Eng., Des. Sel. , vol.19 , pp. 99-105
    • Mee-Hie Cho, C.1    Mulchandani, A.2    Chen, W.3
  • 18
    • 17144364646 scopus 로고    scopus 로고
    • Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state
    • Roodveldt, C. and Tawfik, D. S. (2005) Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state Protein Eng., Des. Sel. 18, 51-58 10.1093/protein/gzi005
    • (2005) Protein Eng., Des. Sel. , vol.18 , pp. 51-58
    • Roodveldt, C.1    Tawfik, D.S.2
  • 19
    • 0031577717 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Russian-VX by organophosphorus hydrolase
    • Rastogi, V. K., DeFrank, J. J., Cheng, T. C., and Wild, J. R. (1997) Enzymatic hydrolysis of Russian-VX by organophosphorus hydrolase Biochem. Biophys. Res. Commun. 241, 294-296 10.1006/bbrc.1997.7569
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 294-296
    • Rastogi, V.K.1    DeFrank, J.J.2    Cheng, T.C.3    Wild, J.R.4
  • 21
    • 84919784933 scopus 로고    scopus 로고
    • In vitro and in vivo toxicological studies of v nerve agents: Molecular and stereoselective aspects
    • Reiter, G., Muller, S., Hill, I., Weatherby, K., Thiermann, H., Worek, F., and Mikler, J. (2015) In vitro and in vivo toxicological studies of V nerve agents: molecular and stereoselective aspects Toxicol. Lett. 232, 438-448 10.1016/j.toxlet.2014.11.010
    • (2015) Toxicol. Lett. , vol.232 , pp. 438-448
    • Reiter, G.1    Muller, S.2    Hill, I.3    Weatherby, K.4    Thiermann, H.5    Worek, F.6    Mikler, J.7
  • 22
    • 0017115171 scopus 로고
    • Synthesis and properties of 2-S-(N,N-dialkylamino)ethyl)thio-1,3,2-dioxaphosphorinane 2-oxide and of the corresponding quaternary derivatives as potential nontoxic antiglaucoma agents
    • Amitai, G., Ashani, Y., Grunfeld, Y., Kalir, A., and Cohen, S. (1976) Synthesis and properties of 2-S-(N,N-dialkylamino)ethyl)thio-1,3,2-dioxaphosphorinane 2-oxide and of the corresponding quaternary derivatives as potential nontoxic antiglaucoma agents J. Med. Chem. 19, 810-813 10.1021/jm00228a600
    • (1976) J. Med. Chem. , vol.19 , pp. 810-813
    • Amitai, G.1    Ashani, Y.2    Grunfeld, Y.3    Kalir, A.4    Cohen, S.5
  • 23
    • 0000870544 scopus 로고
    • Die Kinetik der Invertinwirkung
    • Michaelis, L. and Menten, M. L. (1913) Die Kinetik der Invertinwirkung Biochem. Z. 49, 333-369
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2
  • 24
    • 2442496666 scopus 로고    scopus 로고
    • Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase
    • Aubert, S. D., Li, Y., and Raushel, F. M. (2004) Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase Biochemistry 43, 5707-5715 10.1021/bi0497805
    • (2004) Biochemistry , vol.43 , pp. 5707-5715
    • Aubert, S.D.1    Li, Y.2    Raushel, F.M.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, M. W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276A, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.M.W.1
  • 27
  • 28
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O. and Olson, A. J. (2010) AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J. Comput. Chem. 31, 455-461 10.1002/jcc.21334
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 29
    • 0035814818 scopus 로고    scopus 로고
    • Structural determinants of the substrate and stereochemical specificity of phosphotriesterase
    • Chen-Goodspeed, M., Sogorb, M. A., Wu, F., Hong, S. B., and Raushel, F. M. (2001) Structural determinants of the substrate and stereochemical specificity of phosphotriesterase Biochemistry 40, 1325-1331 10.1021/bi001548l
    • (2001) Biochemistry , vol.40 , pp. 1325-1331
    • Chen-Goodspeed, M.1    Sogorb, M.A.2    Wu, F.3    Hong, S.B.4    Raushel, F.M.5
  • 30
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Caldwell, S. R., Newcomb, J. R., Schlecht, K. A., and Raushel, F. M. (1991) Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta Biochemistry 30, 7438-7444 10.1021/bi00244a010
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 31
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • Hong, S. B. and Raushel, F. M. (1996) Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase Biochemistry 35, 10904-10912 10.1021/bi960663m
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.B.1    Raushel, F.M.2
  • 32
    • 0035912842 scopus 로고    scopus 로고
    • Molecular Structure of Dihydroorotase: A Paradigm for Catalysis through the Use of a Binuclear Metal Center
    • Thoden, J. B., Phillips, G. N., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular Structure of Dihydroorotase: A Paradigm for Catalysis through the Use of a Binuclear Metal Center Biochemistry 40, 6989-6997 10.1021/bi010682i
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips, G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 33
    • 0025833708 scopus 로고
    • Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis
    • Caldwell, S. R., Raushel, F. M., Weiss, P. M., and Cleland, W. W. (1991) Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis Biochemistry 30, 7444-7450 10.1021/bi00244a011
    • (1991) Biochemistry , vol.30 , pp. 7444-7450
    • Caldwell, S.R.1    Raushel, F.M.2    Weiss, P.M.3    Cleland, W.W.4
  • 34
    • 0029993512 scopus 로고    scopus 로고
    • Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with the Bound Substrate Analog Diethyl 4-Methylbenzylphosphonate
    • 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-Methylbenzylphosphonate Biochemistry 35, 6020-6025 10.1021/bi960325l
    • (1996) Biochemistry , vol.35 , pp. 6020-6025
    • Vanhooke, J.L.1    Benning, M.M.2    Raushel, F.M.3    Holden, H.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.