메뉴 건너뛰기




Volumn 109, Issue 2, 2010, Pages 548-557

Generation of a mutagenized organophosphorus hydrolase for the biodegradation of the organophosphate pesticides malathion and demeton-S

Author keywords

bioremediation; biotechnology; environmental health; pesticides; pollutants

Indexed keywords

BIODEGRADATION; BIOTECHNOLOGY; DETOXIFICATION; EFFICIENCY; ESCHERICHIA COLI; GENE ENCODING; HYDROLASES; HYDROLYSIS; PESTICIDES; SUBSTRATES;

EID: 77954504321     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2010.04672.x     Document Type: Article
Times cited : (55)

References (37)
  • 2
    • 0013208747 scopus 로고    scopus 로고
    • Progress on the road to new nerve agent treatments
    • Broomfield, C.A. Kirby, S.D. (2001) Progress on the road to new nerve agent treatments. J Appl Toxicol 21 (Suppl 1 S43 S46.
    • (2001) J Appl Toxicol , vol.21 , Issue.SUPPL. 1
    • Broomfield, C.A.1    Kirby, S.D.2
  • 3
    • 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. Raushel, F.M. (2001) Structural determinants of the substrate and stereochemical specificity of phosphotriesterase. Biochemistry 40, 1325 1331.
    • (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
  • 4
    • 0036208056 scopus 로고    scopus 로고
    • Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents
    • Cho, C.M., Mulchandani, A. Chen, W. (2002) Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents. Appl Environ Microbiol 68, 2026 2030.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 2026-2030
    • Cho, C.M.1    Mulchandani, A.2    Chen, W.3
  • 5
    • 4143066086 scopus 로고    scopus 로고
    • Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos
    • Cho, C.M., Mulchandani, A. Chen, W. (2004) Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos. Appl Environ Microbiol 70, 4681 4685.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 4681-4685
    • Cho, C.M.1    Mulchandani, A.2    Chen, W.3
  • 7
    • 0033032010 scopus 로고    scopus 로고
    • Rational design of organophosphorus hydrolase for altered substrate specificities
    • Di Sioudi, B.D., Miller, C.E., Lai, K., Grimsley, J.K. Wild, J.R. (1999) Rational design of organophosphorus hydrolase for altered substrate specificities. Chem Biol Interact 119-120, 211 223.
    • (1999) Chem Biol Interact , vol.119-120 , pp. 211-223
    • Di Sioudi, B.D.1    Miller, C.E.2    Lai, K.3    Grimsley, J.K.4    Wild, J.R.5
  • 10
    • 34547742504 scopus 로고    scopus 로고
    • Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX
    • Ghanem, E., Yingchun, L., Chengfu, X. Raushel, F.M. (2007) Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX. Biochemistry 46, 9032 9040.
    • (2007) Biochemistry , vol.46 , pp. 9032-9040
    • Ghanem, E.1    Yingchun, L.2    Chengfu, X.3    Raushel, F.M.4
  • 11
    • 0034694836 scopus 로고    scopus 로고
    • Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX
    • Gopal, S., Rastogi, V., Ashman, W. Mulbry, W. (2000) Mutagenesis of organophosphorus hydrolase to enhance hydrolysis of the nerve agent VX. Biochem Biophys Res Commun 279, 516 519.
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 516-519
    • Gopal, S.1    Rastogi, V.2    Ashman, W.3    Mulbry, W.4
  • 12
    • 0041866683 scopus 로고    scopus 로고
    • Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site
    • Hill, C.M., Li, W.S., Thoden, J.B., Holden, H.M. Raushel, F.M. (2003) Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site. J Am Chem Soc 125, 8990 8991.
    • (2003) J Am Chem Soc , vol.125 , pp. 8990-8991
    • Hill, C.M.1    Li, W.S.2    Thoden, J.B.3    Holden, H.M.4    Raushel, F.M.5
  • 13
    • 0030918117 scopus 로고    scopus 로고
    • Malathion as a model for the enzymatic hydrolysis of the neurotoxic agent, VX
    • Hoskin, F.C. Walker, J.E. (1997) Malathion as a model for the enzymatic hydrolysis of the neurotoxic agent, VX. Bull Environ Contam Toxicol 59, 9 13.
    • (1997) Bull Environ Contam Toxicol , vol.59 , pp. 9-13
    • Hoskin, F.C.1    Walker, J.E.2
  • 14
    • 0028946531 scopus 로고
    • Hydrolysis of tetriso by an enzyme derived from Pseudomonas diminuta as a model for the detoxication of O-ethyl S-(2-diisopropylaminoethyl) methylphosphonothiolate (VX)
    • Hoskin, F.C., Walker, J.E., Dettbarn, W.D. Wild, J.R. (1995) Hydrolysis of tetriso by an enzyme derived from Pseudomonas diminuta as a model for the detoxication of O-ethyl S-(2-diisopropylaminoethyl) methylphosphonothiolate (VX). Biochem Pharmacol 49, 711 715.
    • (1995) Biochem Pharmacol , vol.49 , pp. 711-715
    • Hoskin, F.C.1    Walker, J.E.2    Dettbarn, W.D.3    Wild, J.R.4
  • 15
    • 0033001855 scopus 로고    scopus 로고
    • Degradation of nerve gases by CLECS and cells: Kinetics of heterogenous systems
    • Hoskin, F.C., Walker, J.E. Stote, R. (1999) Degradation of nerve gases by CLECS and cells: kinetics of heterogenous systems. Chem Biol Interact 119-120, 439 444.
    • (1999) Chem Biol Interact , vol.119-120 , pp. 439-444
    • Hoskin, F.C.1    Walker, J.E.2    Stote, R.3
  • 16
    • 0025120049 scopus 로고
    • Acute pesticide poisoning: A major global health problem
    • Jeyaratnam, J. (1990) Acute pesticide poisoning: a major global health problem. World Health Stat Q 43, 139 144.
    • (1990) World Health Stat Q , vol.43 , pp. 139-144
    • Jeyaratnam, J.1
  • 17
    • 0028933772 scopus 로고
    • Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase
    • Lai, K., Stolowich, N.J. Wild, J.R. (1995) Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch Biochem Biophys 318, 59 64.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 59-64
    • Lai, K.1    Stolowich, N.J.2    Wild, J.R.3
  • 18
    • 0001169024 scopus 로고
    • Turnover time of acetylcholinesterase
    • Lawler, H.C. (1961) Turnover time of acetylcholinesterase. J Biol Chem 236, 2296 2301.
    • (1961) J Biol Chem , vol.236 , pp. 2296-2301
    • Lawler, H.C.1
  • 19
    • 33644984271 scopus 로고    scopus 로고
    • Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides
    • Mee-Hie Cho, C., Mulchandani, A. Chen, W. (2006) Functional analysis of organophosphorus hydrolase variants with high degradation activity towards organophosphate pesticides. Protein Eng Des Sel 19, 99 105.
    • (2006) Protein Eng des Sel , vol.19 , pp. 99-105
    • Mee-Hie Cho, C.1    Mulchandani, A.2    Chen, W.3
  • 21
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry, W.W. Karns, J.S. (1989) Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J Bacteriol 171, 6740 6746.
    • (1989) J Bacteriol , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 22
    • 0033586803 scopus 로고    scopus 로고
    • Detoxification of organophosphate nerve agents by immobilized Escherichia coli with surface-expressed organophosphorus hydrolase
    • DOI 10.1002/(SICI)1097-0290(19990420)63:2<216::AID-BIT10>3.0.CO;2-0
    • Mulchandani, A., Kaneva, I. Chen, W. (1999) Detoxification of organophosphate nerve agents by immobilized Escherichia coli with surface-expressed organophosphorus hydrolase. Biotechnol Bioeng 63, 216 223. (Pubitemid 29095631)
    • (1999) Biotechnology and Bioengineering , vol.63 , Issue.2 , pp. 216-223
    • Mulchandani, A.1    Kaneva, I.2    Chen, W.3
  • 23
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G.A., Kuo, J.M., Mullins, L.S. Raushel, F.M. (1992) Characterization of the zinc binding site of bacterial phosphotriesterase. J Biol Chem 267, 13278 13283.
    • (1992) J Biol Chem , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 24
    • 33845282579 scopus 로고
    • Acetylcholinesterase: Enzyme structure, reaction dynamics, and virtual transition states
    • Quinn, D.M. (1987) Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem Rev 87, 955 979.
    • (1987) Chem Rev , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 25
    • 0036273082 scopus 로고    scopus 로고
    • Bacterial detoxification of organophosphate nerve agents
    • Raushel, F.M. (2002) Bacterial detoxification of organophosphate nerve agents. Curr Opin Microbiol 5, 288 295.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 288-295
    • Raushel, F.M.1
  • 26
    • 44649197217 scopus 로고    scopus 로고
    • Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities
    • Reeves, T.E., Wales, M.E., Grimsley, J.K., Li, P., Cerasoli, D.M. Wild, J.R. (2008) Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities. Protein Eng Des Sel 21, 405 412.
    • (2008) Protein Eng des Sel , vol.21 , pp. 405-412
    • Reeves, T.E.1    Wales, M.E.2    Grimsley, J.K.3    Li, P.4    Cerasoli, D.M.5    Wild, J.R.6
  • 27
    • 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. 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.
    • (2005) Protein Eng des Sel , vol.18 , pp. 51-58
    • Roodveldt, C.1    Tawfik, D.S.2
  • 29
    • 0037979019 scopus 로고    scopus 로고
    • Development of a thermally regulated broad-spectrum promoter system for use in pathogenic gram-positive species
    • Schofield, D.A., Westwater, C., Hoel, B.D., Werner, P.A., Norris, J.S. Schmidt, M.G. (2003) Development of a thermally regulated broad-spectrum promoter system for use in pathogenic gram-positive species. Appl Environ Microbiol 69, 3385 3392.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 3385-3392
    • Schofield, D.A.1    Westwater, C.2    Hoel, B.D.3    Werner, P.A.4    Norris, J.S.5    Schmidt, M.G.6
  • 30
    • 34648824667 scopus 로고    scopus 로고
    • Development of a yeast biosensor-biocatalyst for the detection and biodegradation of the organophosphate paraoxon
    • Schofield, D.A., Westwater, C., Barth, J.L. DiNovo, A.A. (2007) Development of a yeast biosensor-biocatalyst for the detection and biodegradation of the organophosphate paraoxon. Appl Microbiol Biotechnol 76, 1383 1394.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1383-1394
    • Schofield, D.A.1    Westwater, C.2    Barth, J.L.3    Dinovo, A.A.4
  • 31
    • 33645472653 scopus 로고    scopus 로고
    • Microbial degradation of organophosphorus compounds
    • Singh, B.K. Walker, A. (2006) Microbial degradation of organophosphorus compounds. FEMS Microbiol Rev 30, 428 471.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 428-471
    • Singh, B.K.1    Walker, A.2
  • 32
    • 0033537687 scopus 로고    scopus 로고
    • Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity
    • diSioudi, B., Grimsley, J.K., Lai, K. Wild, J.R. (1999) Modification of near active site residues in organophosphorus hydrolase reduces metal stoichiometry and alters substrate specificity. Biochemistry 38, 2866 2872.
    • (1999) Biochemistry , vol.38 , pp. 2866-2872
    • Disioudi, B.1    Grimsley, J.K.2    Lai, K.3    Wild, J.R.4
  • 33
    • 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. Holden, H.M. (1996) Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate. Biochemistry 35, 6020 6025.
    • (1996) Biochemistry , vol.35 , pp. 6020-6025
    • Vanhooke, J.L.1    Benning, M.M.2    Raushel, F.M.3    Holden, H.M.4
  • 34
    • 0030754819 scopus 로고    scopus 로고
    • Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase
    • Watkins, L.M., Mahoney, H.J., McCulloch, J.K. Raushel, F.M. (1997) Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase. J Biol Chem 272, 25596 25601.
    • (1997) J Biol Chem , vol.272 , pp. 25596-25601
    • Watkins, L.M.1    Mahoney, H.J.2    McCulloch, J.K.3    Raushel, F.M.4
  • 35
  • 37


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.