메뉴 건너뛰기




Volumn 58, Issue 1, 2014, Pages 53-59

Improving methyl parathion hydrolase to enhance its chlorpyrifos-hydrolysing efficiency

Author keywords

Chlorpyrifos; Hydrolysis; Improve; Methyl parathion hydrolase; pH stability; Random mutagenesis; Thermostability

Indexed keywords

BACTERIOLOGY; EFFICIENCY; HYDROLASES; MUTAGENESIS; PH EFFECTS; PHOSPHORUS COMPOUNDS; STABILITY; SUBSTRATES;

EID: 84890225408     PISSN: 02668254     EISSN: 1472765X     Source Type: Journal    
DOI: 10.1111/lam.12155     Document Type: Article
Times cited : (27)

References (34)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus sublilis
    • Anagnostopoulos, C. and Spizizen, J. (1960) Requirements for transformation in Bacillus sublilis. J Bacteriol 81, 741-746.
    • (1960) J Bacteriol , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 2
    • 33645961330 scopus 로고    scopus 로고
    • Flexible protein-protein docking
    • Bonvin, A.M. (2006) Flexible protein-protein docking. Curr Opin Struct Biol 16, 194-200.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 194-200
    • Bonvin, A.M.1
  • 3
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R.C. and Joyce, G.F. (1992) Randomization of genes by PCR mutagenesis. Genome Res 2, 28-33.
    • (1992) Genome Res , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 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. and 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. and 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
  • 6
    • 0035490893 scopus 로고    scopus 로고
    • Isolation of methyl parathion-degrading strain M6 and cloning of the methyl parathion hydrolase gene
    • Cui, Z., Li, S. and Fu, G. (2001) Isolation of methyl parathion-degrading strain M6 and cloning of the methyl parathion hydrolase gene. Appl Environ Microbiol 67, 4922-4925.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4922-4925
    • Cui, Z.1    Li, S.2    Fu, G.3
  • 7
    • 33744807436 scopus 로고    scopus 로고
    • Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures
    • Damm, K.L. and Carlson, H.A. (2006) Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures. Biophys J 90, 4558-4573.
    • (2006) Biophys J , vol.90 , pp. 4558-4573
    • Damm, K.L.1    Carlson, H.A.2
  • 8
    • 78650192378 scopus 로고    scopus 로고
    • Evaluation of pesticides residues in Greek peaches during 2002-2007 after the implementation of integrated crop management
    • Danis, T.G., Karagiozoglou, D.T., Tsakiris, I.N., Alegakis, A.K. and Tsatsakis, A.M. (2011) Evaluation of pesticides residues in Greek peaches during 2002-2007 after the implementation of integrated crop management. Food Chem 126, 97-103.
    • (2011) Food Chem , vol.126 , pp. 97-103
    • Danis, T.G.1    Karagiozoglou, D.T.2    Tsakiris, I.N.3    Alegakis, A.K.4    Tsatsakis, A.M.5
  • 9
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deléage, G. and Geourjon, C. (1993) An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput Appl Biosci 92, 197-199.
    • (1993) Comput Appl Biosci , vol.92 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 10
    • 0024340489 scopus 로고
    • Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski, W.J., Dumas, D.P., Heitmeyer, D.P., Lewis, V.E. and Raushel, F.M. (1989) Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 28, 4650-4655.
    • (1989) Biochemistry , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 11
    • 26244457622 scopus 로고    scopus 로고
    • Crystal structure of methyl parathion hydrolase from Pseudomonas sp. WBC-3
    • Dong, Y., Mark, B., Sun, L., Zhou, Y., Zhang, Z., Zhang, C., Rao, Z. and Zhang, X. (2005) Crystal structure of methyl parathion hydrolase from Pseudomonas sp. WBC-3. J Mol Biol 353, 655-663.
    • (2005) J Mol Biol , vol.353 , pp. 655-663
    • Dong, Y.1    Mark, B.2    Sun, L.3    Zhou, Y.4    Zhang, Z.5    Zhang, C.6    Rao, Z.7    Zhang, X.8
  • 12
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P., Caldwell, S.R., Wild, J.R. and Raushel, R.M. (1989) Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J Biol Chem 261, 19659-19665.
    • (1989) J Biol Chem , vol.261 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, R.M.4
  • 15
    • 3142609729 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a novel methyl parathion hydrolase
    • Fu, G., Cui, Z., Huang, T. and Li, S. (2004) Expression, purification, and characterization of a novel methyl parathion hydrolase. Protein Expr Purif 36, 170-176. Http://www.epa.gov/oppfead1/cb/csb_page/updates/2012/chlorpyrifos.html
    • (2004) Protein Expr Purif , vol.36 , pp. 170-176
    • Fu, G.1    Cui, Z.2    Huang, T.3    Li, S.4
  • 16
    • 84862785138 scopus 로고    scopus 로고
    • Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic residues
    • Huang, L., Wang, P., Tian, J., Jiang, H., Wu, N., Yang, P., Yao, B. and Fan, Y. (2012) Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic residues. Biotechnol Lett 34, 1115-1121.
    • (2012) Biotechnol Lett , vol.34 , pp. 1115-1121
    • Huang, L.1    Wang, P.2    Tian, J.3    Jiang, H.4    Wu, N.5    Yang, P.6    Yao, B.7    Fan, Y.8
  • 17
    • 77950164392 scopus 로고    scopus 로고
    • Random mutagenesis methods for in vitro directed enzyme evolution
    • Labrou, N.E. (2010) Random mutagenesis methods for in vitro directed enzyme evolution. Curr Protein Pept Sci 11, 91-100.
    • (2010) Curr Protein Pept Sci , vol.11 , pp. 91-100
    • Labrou, N.E.1
  • 18
    • 33847381188 scopus 로고    scopus 로고
    • Isolation of a chlorpyrifos-degrading bacterium, Sphingomonas sp. strain Dsp-2, and cloning of the mpd gene
    • Li, X., He, J. and Li, S. (2007) Isolation of a chlorpyrifos-degrading bacterium, Sphingomonas sp. strain Dsp-2, and cloning of the mpd gene. Res Microbiol 158, 143-149.
    • (2007) Res Microbiol , vol.158 , pp. 143-149
    • Li, X.1    He, J.2    Li, S.3
  • 19
    • 63149152073 scopus 로고    scopus 로고
    • Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment
    • Rasila, T.S., Pajunen, M.I. and Savilahti, H. (2009) Critical evaluation of random mutagenesis by error-prone polymerase chain reaction protocols, Escherichia coli mutator strain, and hydroxylamine treatment. Anal Biochem 388, 71-80.
    • (2009) Anal Biochem , vol.388 , pp. 71-80
    • Rasila, T.S.1    Pajunen, M.I.2    Savilahti, H.3
  • 20
    • 84966188998 scopus 로고
    • Enzymatic hydrolysis of organophosphates: cloning and expression of a parathion hydrolase gene from Pseudomonas diminuta
    • Serdar, C.M. and Gibson, D.T. (1985) Enzymatic hydrolysis of organophosphates: cloning and expression of a parathion hydrolase gene from Pseudomonas diminuta. Nat Biotechnol 3, 567-571.
    • (1985) Nat Biotechnol , vol.3 , pp. 567-571
    • Serdar, C.M.1    Gibson, D.T.2
  • 21
    • 33645472653 scopus 로고    scopus 로고
    • Microbial degradation of organophosphorus compounds
    • Singh, B.K. and 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
  • 22
    • 81355149258 scopus 로고    scopus 로고
    • Characterization of a novel PTEN mutation in MDA-MB-453 breast carcinoma cell line
    • Singh, G., Odriozola, L., Guan, H., Kennedy, C.R. and Chan, A.M. (2011) Characterization of a novel PTEN mutation in MDA-MB-453 breast carcinoma cell line. BMC Cancer 11, 490.
    • (2011) BMC Cancer , vol.11 , pp. 490
    • Singh, G.1    Odriozola, L.2    Guan, H.3    Kennedy, C.R.4    Chan, A.M.5
  • 23
    • 79551680693 scopus 로고    scopus 로고
    • Quantification of organophosphate insecticides in drinking water in urban areas using lyophilisation and high-performance liquid chromatography-electrospray ionization-mass spectrometry techniques
    • Sinha, S.N., Vasudev, K., Rao, M. and Odetokun, M. (2011) Quantification of organophosphate insecticides in drinking water in urban areas using lyophilisation and high-performance liquid chromatography-electrospray ionization-mass spectrometry techniques. Int J Mass Spectrom 300, 12-20.
    • (2011) Int J Mass Spectrom , vol.300 , pp. 12-20
    • Sinha, S.N.1    Vasudev, K.2    Rao, M.3    Odetokun, M.4
  • 24
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody, R.W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287, 252-260.
    • (2000) Anal Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 25
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., Venyaminov, S.Y. and Woody, R.W. (2000) Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal Biochem 287, 243-251.
    • (2000) Anal Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 26
    • 81355149809 scopus 로고    scopus 로고
    • Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface
    • Su, Y., Tian, J., Wang, P., Chu, X., Liu, G., Wu, N. and Fan, Y. (2011) Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface. Appl Biochem Biotechnol 165, 989-997.
    • (2011) Appl Biochem Biotechnol , vol.165 , pp. 989-997
    • Su, Y.1    Tian, J.2    Wang, P.3    Chu, X.4    Liu, G.5    Wu, N.6    Fan, Y.7
  • 27
    • 78449306754 scopus 로고    scopus 로고
    • Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation
    • Tian, J., Wang, P., Gao, S., Chu, X., Wu, N. and Fan, Y. (2010) Enhanced thermostability of methyl parathion hydrolase from Ochrobactrum sp. M231 by rational engineering of a glycine to proline mutation. FEBS J 277, 4901-4908.
    • (2010) FEBS J , vol.277 , pp. 4901-4908
    • Tian, J.1    Wang, P.2    Gao, S.3    Chu, X.4    Wu, N.5    Fan, Y.6
  • 28
    • 0036307716 scopus 로고    scopus 로고
    • Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production
    • Wu, S.C., Yeung, J.C., Duan, Y., Ye, R., Szarka, S.J., Habibi, H.R. and Wong, S.L. (2002) Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: effects of molecular chaperones and a wall-bound protease on antibody fragment production. Appl Environ Microbiol 68, 3261-3269.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3261-3269
    • Wu, S.C.1    Yeung, J.C.2    Duan, Y.3    Ye, R.4    Szarka, S.J.5    Habibi, H.R.6    Wong, S.L.7
  • 30
    • 24944469147 scopus 로고    scopus 로고
    • Isolation and characterization of a chlorpyrifos and 3,5,6-trichloro-2-pyridinol degrading bacterium
    • Yang, L., Zhao, Y., Zhang, B., Yang, C. and Zhang, X. (2005) Isolation and characterization of a chlorpyrifos and 3, 5, 6-trichloro-2-pyridinol degrading bacterium. FEMS Microbiol Lett 251, 67-73.
    • (2005) FEMS Microbiol Lett , vol.251 , pp. 67-73
    • Yang, L.1    Zhao, Y.2    Zhang, B.3    Yang, C.4    Zhang, X.5
  • 31
    • 33750804116 scopus 로고    scopus 로고
    • Cloning of mpd gene from a chlorpyrifos-degrading bacterium and use of this strain in bioremediation of contaminated soil
    • Yang, C., Liu, N., Guo, X. and Qiao, C. (2006) Cloning of mpd gene from a chlorpyrifos-degrading bacterium and use of this strain in bioremediation of contaminated soil. FEMS Microbiol Lett 265, 118-125.
    • (2006) FEMS Microbiol Lett , vol.265 , pp. 118-125
    • Yang, C.1    Liu, N.2    Guo, X.3    Qiao, C.4
  • 32
    • 52549092769 scopus 로고    scopus 로고
    • Overexpression of methyl parathion hydrolase and its application in detoxification of organophosphates
    • Yang, J., Yang, C., Jiang, H. and Qiao, C. (2008) Overexpression of methyl parathion hydrolase and its application in detoxification of organophosphates. Biodegradation 19, 831-839.
    • (2008) Biodegradation , vol.19 , pp. 831-839
    • Yang, J.1    Yang, C.2    Jiang, H.3    Qiao, C.4
  • 33
    • 33748665267 scopus 로고    scopus 로고
    • Characterization of a fungal strain capable of degrading chlorpyrifos and its use in detoxification of the insecticide on vegetables
    • Yu, Y., Fang, H., Wang, X., Wu, X., Shan, M. and Yu, J. (2006) Characterization of a fungal strain capable of degrading chlorpyrifos and its use in detoxification of the insecticide on vegetables. Biodegradation 17, 487-494.
    • (2006) Biodegradation , vol.17 , pp. 487-494
    • Yu, Y.1    Fang, H.2    Wang, X.3    Wu, X.4    Shan, M.5    Yu, J.6
  • 34
    • 22144475150 scopus 로고    scopus 로고
    • High-level expression and secretion of methyl parathion hydrolase in Bacillus subtilis WB800
    • Zhang, X., Cui, Z., Hong, Q. and Li, S. (2005) High-level expression and secretion of methyl parathion hydrolase in Bacillus subtilis WB800. Appl Environ Microbiol 71, 4101-4103.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4101-4103
    • Zhang, X.1    Cui, Z.2    Hong, Q.3    Li, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.