메뉴 건너뛰기




Volumn 109, Issue 5, 2012, Pages 1101-1108

Immobilization of organophosphohydrolase OpdA from Agrobacterium radiobacter by overproduction at the surface of polyester inclusions inside engineered Escherichia coli

Author keywords

Bioremediation; Immobilization; Insecticides; Organophosphohydrolase; Pesticides

Indexed keywords

AGROBACTERIUM RADIOBACTER; APPLICATION PERFORMANCE; C-TERMINUS; COEXPRESSED; CONTAMINATED ENVIRONMENT; FUSION PROTEINS; INCREASED TEMPERATURE; LINKER REGION; ORGANOPHOSPHOHYDROLASE; ORGANOPHOSPHORUS PESTICIDE; RALSTONIA EUTROPHA; STEADY-STATE KINETICS;

EID: 84858448799     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24402     Document Type: Article
Times cited : (37)

References (44)
  • 1
    • 0041328584 scopus 로고    scopus 로고
    • Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa mediated synthesis of a new polyoxoester: Identification of catalytic residues
    • Amara A, Rehm BHA. 2003. Replacement of the catalytic nucleophile cysteine-296 by serine in class II polyhydroxyalkanoate synthase from Pseudomonas aeruginosa mediated synthesis of a new polyoxoester: Identification of catalytic residues. Biochem J 374: 413-421.
    • (2003) Biochem J , vol.374 , pp. 413-421
    • Amara, A.1    Rehm, B.H.A.2
  • 3
    • 0035814923 scopus 로고    scopus 로고
    • High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • Benning MM, Shim H, Raushel FM, Holden HM. 2001. High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry 40: 2712-2722.
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 4
    • 42749086354 scopus 로고    scopus 로고
    • OpdA, a bacterial organophosphorus hydrolase, prevents lethality in rats after poisoning with highly toxic organophosphorus pesticides
    • Bird SB, Sutherland TD, Gresham C, Oakeshott J, Scott C, Eddleston M. 2008. OpdA, a bacterial organophosphorus hydrolase, prevents lethality in rats after poisoning with highly toxic organophosphorus pesticides. Toxicology 247: 88-92.
    • (2008) Toxicology , vol.247 , pp. 88-92
    • Bird, S.B.1    Sutherland, T.D.2    Gresham, C.3    Oakeshott, J.4    Scott, C.5    Eddleston, M.6
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0023749235 scopus 로고
    • Pseudomonas oleovorans as a source of poly(beta-hydroxyalkanoates) for potential applications as biodegradable polyesters
    • Brandl H, Gross RA, Lenz RW, Fuller RC. 1988. Pseudomonas oleovorans as a source of poly(beta-hydroxyalkanoates) for potential applications as biodegradable polyesters. Appl Environ Microbiol 54: 1977-1982.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1977-1982
    • Brandl, H.1    Gross, R.A.2    Lenz, R.W.3    Fuller, R.C.4
  • 7
    • 0026071672 scopus 로고
    • Detoxification of organophosphate pesticides using an immobilized phosphotriesterase from Pseudomonas diminuta
    • Caldwell SR, Raushel FM. 1991. Detoxification of organophosphate pesticides using an immobilized phosphotriesterase from Pseudomonas diminuta. Biotechnol Bioeng 37: 103-109.
    • (1991) Biotechnol Bioeng , vol.37 , pp. 103-109
    • Caldwell, S.R.1    Raushel, F.M.2
  • 8
    • 46449100353 scopus 로고    scopus 로고
    • Degradation of nerve agents by an organophosphate-degrading agent (OpdA)
    • Dawson RM, Pantelidis S, Rose HR, Kotsonis SE. 2008. Degradation of nerve agents by an organophosphate-degrading agent (OpdA). J Hazard Mater 157: 308-314.
    • (2008) J Hazard Mater , vol.157 , pp. 308-314
    • Dawson, R.M.1    Pantelidis, S.2    Rose, H.R.3    Kotsonis, S.E.4
  • 9
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas DP, Caldwell SR, Wild JR, Raushel FM. 1989. Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J Biol Chem 264: 19659-19665.
    • (1989) J Biol Chem , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 10
    • 0034694203 scopus 로고    scopus 로고
    • Degradation of organophosphorous nerve agents by enzyme-polymer nanocomposites: Efficient biocatalytic materials for personal protection and large-scale detoxification
    • Gill I, Ballesteros A. 2000. Degradation of organophosphorous nerve agents by enzyme-polymer nanocomposites: Efficient biocatalytic materials for personal protection and large-scale detoxification. Biotechnol Bioeng 70: 400-410.
    • (2000) Biotechnol Bioeng , vol.70 , pp. 400-410
    • Gill, I.1    Ballesteros, A.2
  • 11
    • 75649140553 scopus 로고    scopus 로고
    • The role of nonbonded interactions in the conformational dynamics of organophosphorous hydrolase adsorbed onto functionalized mesoporous silica surfaces
    • Gomes DE, Lins RD, Pascutti PG, Lei C, Soares TA. 2010. The role of nonbonded interactions in the conformational dynamics of organophosphorous hydrolase adsorbed onto functionalized mesoporous silica surfaces. J Physic Chem 114: 531-540.
    • (2010) J Physic Chem , vol.114 , pp. 531-540
    • Gomes, D.E.1    Lins, R.D.2    Pascutti, P.G.3    Lei, C.4    Soares, T.A.5
  • 12
    • 70350469039 scopus 로고    scopus 로고
    • Organophosphate hydrolase in Brevundimonas diminuta is targeted to the periplasmic face of the inner membrane by the twin arginine translocation pathway
    • Gorla P, Pandey JP, Parthasarathy S, Merrick M, Siddavattam D. 2009. Organophosphate hydrolase in Brevundimonas diminuta is targeted to the periplasmic face of the inner membrane by the twin arginine translocation pathway. J Bacteriol 191: 6292-6299.
    • (2009) J Bacteriol , vol.191 , pp. 6292-6299
    • Gorla, P.1    Pandey, J.P.2    Parthasarathy, S.3    Merrick, M.4    Siddavattam, D.5
  • 13
    • 38949135957 scopus 로고    scopus 로고
    • In vivo production of scFv-displaying biopolymer beads using a self-assembly-promoting fusion partner
    • Grage K, Rehm BH. 2008. In vivo production of scFv-displaying biopolymer beads using a self-assembly-promoting fusion partner. Bioconj Chem 19: 254-262.
    • (2008) Bioconj Chem , vol.19 , pp. 254-262
    • Grage, K.1    Rehm, B.H.2
  • 14
    • 65249103916 scopus 로고    scopus 로고
    • Bacterial polyhydroxyalkanoate granules: Biogenesis, structure, and potential use as nano-/micro-beads in biotechnological and biomedical applications
    • Grage K, Jahns AC, Parlane N, Palanisamy R, Rasiah IA, Atwood JA, Rehm BH. 2009. Bacterial polyhydroxyalkanoate granules: Biogenesis, structure, and potential use as nano-/micro-beads in biotechnological and biomedical applications. Biomacromolecules 10: 660-669.
    • (2009) Biomacromolecules , vol.10 , pp. 660-669
    • Grage, K.1    Jahns, A.C.2    Parlane, N.3    Palanisamy, R.4    Rasiah, I.A.5    Atwood, J.A.6    Rehm, B.H.7
  • 17
    • 0034850374 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition and the extrapyramidal syndrome: A review of the neurotoxicity of organophosphate
    • Hsieh BH, Deng JF, Ger J, Tsai WJ. 2001. Acetylcholinesterase inhibition and the extrapyramidal syndrome: A review of the neurotoxicity of organophosphate. Neurotoxicology 22: 423-427.
    • (2001) Neurotoxicology , vol.22 , pp. 423-427
    • Hsieh, B.H.1    Deng, J.F.2    Ger, J.3    Tsai, W.J.4
  • 19
    • 33746934144 scopus 로고    scopus 로고
    • Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: The prominent role of iron in the heterobinuclear active site
    • Jackson CJ, Carr PD, Kim HK, Liu JW, Herrald P, Mitic N, Schenk G, Smith CA, Ollis DL. 2006. Anomalous scattering analysis of Agrobacterium radiobacter phosphotriesterase: The prominent role of iron in the heterobinuclear active site. Biochem J 397: 501-508.
    • (2006) Biochem J , vol.397 , pp. 501-508
    • Jackson, C.J.1    Carr, P.D.2    Kim, H.K.3    Liu, J.W.4    Herrald, P.5    Mitic, N.6    Schenk, G.7    Smith, C.A.8    Ollis, D.L.9
  • 21
    • 69449086810 scopus 로고    scopus 로고
    • Tolerance of the Ralstonia eutropha class I polyhydroxyalkanoate synthase for translational fusions to its C terminus reveals a new mode of functional display
    • Jahns AC, Rehm BHA. 2009. Tolerance of the Ralstonia eutropha class I polyhydroxyalkanoate synthase for translational fusions to its C terminus reveals a new mode of functional display. Appl Environ Microbiol 75: 5461-5466.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5461-5466
    • Jahns, A.C.1    Rehm, B.H.A.2
  • 22
    • 55249108919 scopus 로고    scopus 로고
    • Multifunctional inorganic-binding beads self-assembled inside engineered bacteria
    • Jahns AC, Haverkamp RG, Rehm BH. 2008. Multifunctional inorganic-binding beads self-assembled inside engineered bacteria. Bioconj Chem 19: 2072-2080.
    • (2008) Bioconj Chem , vol.19 , pp. 2072-2080
    • Jahns, A.C.1    Haverkamp, R.G.2    Rehm, B.H.3
  • 23
    • 0031257974 scopus 로고    scopus 로고
    • The removal of pesticide residues from wool wax by solvent extraction
    • Jones FW. 1997. The removal of pesticide residues from wool wax by solvent extraction. J Am Oil Chem Soc 74: 1241-1245.
    • (1997) J Am Oil Chem Soc , vol.74 , pp. 1241-1245
    • Jones, F.W.1
  • 24
    • 0033151438 scopus 로고    scopus 로고
    • Removal of wool wax, nonylphenol ethoxylates and pesticide residues from wool scour effluent
    • Jones FW, Westmoreland DJ. 1999. Removal of wool wax, nonylphenol ethoxylates and pesticide residues from wool scour effluent. Water Res 33: 1775-1780.
    • (1999) Water Res , vol.33 , pp. 1775-1780
    • Jones, F.W.1    Westmoreland, D.J.2
  • 26
    • 28644434174 scopus 로고    scopus 로고
    • Detoxification of the organophosphate nerve agent coumaphos using organophosphorus hydrolase immobilized on cellulose materials
    • Mansee AH, Chen W, Mulchandani A. 2005. Detoxification of the organophosphate nerve agent coumaphos using organophosphorus hydrolase immobilized on cellulose materials. J Ind Microbiol Biotech 32: 554-560.
    • (2005) J Ind Microbiol Biotech , vol.32 , pp. 554-560
    • Mansee, A.H.1    Chen, W.2    Mulchandani, A.3
  • 27
    • 0024501620 scopus 로고
    • Purification and characterization of three parathion hydrolases from gram-negative bacterial strains
    • Mulbry WW, Karns JS. 1989. Purification and characterization of three parathion hydrolases from gram-negative bacterial strains. Appl Environ Microbiol 55: 289-293.
    • (1989) Appl Environ Microbiol , vol.55 , pp. 289-293
    • Mulbry, W.W.1    Karns, J.S.2
  • 28
    • 0022479569 scopus 로고
    • Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta
    • Mulbry WW, Karns JS, Kearney PC, Nelson JO, McDaniel CS, Wild JR. 1986. Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by southern hybridization with opd from Pseudomonas diminuta. Appl Environ Microbiol 51: 926-930.
    • (1986) Appl Environ Microbiol , vol.51 , pp. 926-930
    • Mulbry, W.W.1    Karns, J.S.2    Kearney, P.C.3    Nelson, J.O.4    McDaniel, C.S.5    Wild, J.R.6
  • 30
    • 20444498924 scopus 로고    scopus 로고
    • In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases
    • Peters V, Rehm BH. 2005. In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases. FEMS Microbiol Lett 248: 93-100.
    • (2005) FEMS Microbiol Lett , vol.248 , pp. 93-100
    • Peters, V.1    Rehm, B.H.2
  • 31
    • 33644961915 scopus 로고    scopus 로고
    • In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase
    • Peters V, Rehm BH. 2006. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl Environ Microbiol 72: 1777-1783.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 1777-1783
    • Peters, V.1    Rehm, B.H.2
  • 32
    • 41549140412 scopus 로고    scopus 로고
    • Protein engineering of streptavidin for in vivo assembly of streptavidin beads
    • Peters V, Rehm BH. 2008. Protein engineering of streptavidin for in vivo assembly of streptavidin beads. J Biotechnol 134: 266-274.
    • (2008) J Biotechnol , vol.134 , pp. 266-274
    • Peters, V.1    Rehm, B.H.2
  • 33
    • 63849236826 scopus 로고    scopus 로고
    • One-step production of immobilized alpha-amylase in recombinant Escherichia coli
    • Rasiah IA, Rehm BH. 2009. One-step production of immobilized alpha-amylase in recombinant Escherichia coli. Appl Environ Microbiol 75: 2012-2016.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2012-2016
    • Rasiah, I.A.1    Rehm, B.H.2
  • 34
    • 0033658178 scopus 로고    scopus 로고
    • Phosphotriesterase: An enzyme in search of its natural substrate
    • Raushel FM, Holden HM. 2000. Phosphotriesterase: An enzyme in search of its natural substrate. Adv Enzymol Relat Area Mol Biol 74: 51-93.
    • (2000) Adv Enzymol Relat Area Mol Biol , vol.74 , pp. 51-93
    • Raushel, F.M.1    Holden, H.M.2
  • 35
    • 79953844432 scopus 로고    scopus 로고
    • Immobilization of organophosphate hydrolase on an amyloid fibril nanoscaffold: Towards bioremediation and chemical detoxification
    • Raynes JK, Pearce FG, Meade SJ, Gerrard JA. 2011. Immobilization of organophosphate hydrolase on an amyloid fibril nanoscaffold: Towards bioremediation and chemical detoxification. Biotechnol Prog 27: 360-367.
    • (2011) Biotechnol Prog , vol.27 , pp. 360-367
    • Raynes, J.K.1    Pearce, F.G.2    Meade, S.J.3    Gerrard, J.A.4
  • 36
    • 33846457905 scopus 로고    scopus 로고
    • Biogenesis of microbial polyhydroxyalkanoate granules: A platform technology for the production of tailor-made bioparticles
    • Rehm BH. 2007. Biogenesis of microbial polyhydroxyalkanoate granules: A platform technology for the production of tailor-made bioparticles. Curr Issues Mol Biol 9: 41-62.
    • (2007) Curr Issues Mol Biol , vol.9 , pp. 41-62
    • Rehm, B.H.1
  • 37
    • 77954757413 scopus 로고    scopus 로고
    • Bacterial polymers: Biosynthesis, modifications and applications
    • Rehm BH. 2010. Bacterial polymers: Biosynthesis, modifications and applications. Nat Rev Microbiol 8: 578-592.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 578-592
    • Rehm, B.H.1
  • 38
    • 0035882164 scopus 로고    scopus 로고
    • Matrix-assisted in vitro refolding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli
    • Rehm BH, Qi Q, Beermann BB, Hinz HJ, Steinbuchel A. 2001. Matrix-assisted in vitro refolding of Pseudomonas aeruginosa class II polyhydroxyalkanoate synthase from inclusion bodies produced in recombinant Escherichia coli. Biochem. J 358: 263-268.
    • (2001) Biochem. J , vol.358 , pp. 263-268
    • Rehm, B.H.1    Qi, Q.2    Beermann, B.B.3    Hinz, H.J.4    Steinbuchel, A.5
  • 39
    • 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
    • Roodvelt C, Tawfik DS. 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
    • Roodvelt, C.1    Tawfik, D.S.2
  • 43
    • 57149098782 scopus 로고    scopus 로고
    • Organophosphate degrading microorganisms and enzymes as biocatalysts in environmental and personal decontamination applications
    • Yair S, Ofer B, Arik E, Shai S, Yossi R, Tzvika D, Amir K. 2008. Organophosphate degrading microorganisms and enzymes as biocatalysts in environmental and personal decontamination applications. Crit Rev Biotechnol 28: 265-275.
    • (2008) Crit Rev Biotechnol , vol.28 , pp. 265-275
    • Yair, S.1    Ofer, B.2    Arik, E.3    Shai, S.4    Yossi, R.5    Tzvika, D.6    Amir, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.