메뉴 건너뛰기




Volumn 22, Issue 2, 2006, Pages 406-410

Enhanced biodegradation of toxic organophosphate compounds using recombinant Escherichia coli with sec pathway-driven periplasmic secretion of organophosphorus hydrolase

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; DIFFUSION; ENZYMES; ESCHERICHIA COLI; GENETIC ENGINEERING; SUBSTRATES; TOXIC MATERIALS;

EID: 33646042541     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp050356k     Document Type: Article
Times cited : (48)

References (37)
  • 1
    • 0032795933 scopus 로고    scopus 로고
    • Bacteria designed for bioremediation
    • Timmis, K. N.; Pieper, D. H. Bacteria designed for bioremediation. Trends Biotechnol. 1999, 17, 201-204.
    • (1999) Trends Biotechnol. , vol.17 , pp. 201-204
    • Timmis, K.N.1    Pieper, D.H.2
  • 2
    • 0034029016 scopus 로고    scopus 로고
    • Field applications of genetically engineered microorganisms for bioremediation processes
    • Sayler, G. S.; Ripp, S. Field applications of genetically engineered microorganisms for bioremediation processes. Curr. Opin. Biotechnol. 2000, 11, 268-289.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 268-289
    • Sayler, G.S.1    Ripp, S.2
  • 3
    • 0035988030 scopus 로고    scopus 로고
    • Enhanced-rate biodegradation of organophosphate neurotoxins by immobilized nongrowing bacteria
    • Kim, J. W.; Rainina, E. I.; Mulbry, W. W.; Engler, C. R.; Wild, J. R. Enhanced-rate biodegradation of organophosphate neurotoxins by immobilized nongrowing bacteria. Biotechnol. Prog. 2002, 18, 429-436.
    • (2002) Biotechnol. Prog. , vol.18 , pp. 429-436
    • Kim, J.W.1    Rainina, E.I.2    Mulbry, W.W.3    Engler, C.R.4    Wild, J.R.5
  • 4
    • 0032008124 scopus 로고    scopus 로고
    • The use of live biocatalysts for pesticide detoxification
    • Chen, W.; Mulchandani, A. The use of live biocatalysts for pesticide detoxification. Trends Biotechnol. 1998, 16, 71-76.
    • (1998) Trends Biotechnol. , vol.16 , pp. 71-76
    • Chen, W.1    Mulchandani, A.2
  • 5
    • 0031949586 scopus 로고    scopus 로고
    • Recombinant DNA techniques for bioremediation and environmentally friendly synthesis
    • Keasling, J. D.; Bang, S. W. Recombinant DNA techniques for bioremediation and environmentally friendly synthesis. Curr. Opin. Biotechnol. 1998, 9, 135-140.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 135-140
    • Keasling, J.D.1    Bang, S.W.2
  • 6
    • 0036276694 scopus 로고    scopus 로고
    • Enhanced detoxification of organophosphates using recombinant Escherichia coli with coexpression of organophosphorus hydrolase and bacterial hemoglobin
    • Kang, D. G.; Kim, J. Y. H.; Cha, H. J. Enhanced detoxification of organophosphates using recombinant Escherichia coli with coexpression of organophosphorus hydrolase and bacterial hemoglobin. Biotechnol. Lett. 2002, 24, 879-883.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 879-883
    • Kang, D.G.1    Kim, J.Y.H.2    Cha, H.J.3
  • 7
    • 0003242424 scopus 로고    scopus 로고
    • The development of a new biosensor based on recombinant E. coli for the detection of organophosphorus neurotoxins
    • Rainina, E.; Efremenco, E.; Varfolomeyev, S.; Simonian, A. L.; Wild, J. The development of a new biosensor based on recombinant E. coli for the detection of organophosphorus neurotoxins. Biosens. Bioelectron. 1996, 11, 991-1000.
    • (1996) Biosens. Bioelectron. , vol.11 , pp. 991-1000
    • Rainina, E.1    Efremenco, E.2    Varfolomeyev, S.3    Simonian, A.L.4    Wild, J.5
  • 8
    • 0029687854 scopus 로고    scopus 로고
    • Effects of ultraviolet light irradiation in biotreatment of organophosphates
    • Hung, S. C.; Liao, J. C. Effects of ultraviolet light irradiation in biotreatment of organophosphates. Appl. Biochem. Biotechnol. 1996, 56, 37-47.
    • (1996) Appl. Biochem. Biotechnol. , vol.56 , pp. 37-47
    • Hung, S.C.1    Liao, J.C.2
  • 9
    • 0035344055 scopus 로고    scopus 로고
    • Export of cytochrome P450 105D1 to the periplasmic space of Escherichia coli
    • Kaderbhai, M. A.; Ugochukwu, C. C.; Kelly, S. L.; Lamb, D. C. Export of cytochrome P450 105D1 to the periplasmic space of Escherichia coli. Appl. Environ. Microbiol. 2001, 67, 2136-2138.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2136-2138
    • Kaderbhai, M.A.1    Ugochukwu, C.C.2    Kelly, S.L.3    Lamb, D.C.4
  • 10
    • 0020107851 scopus 로고
    • Permeabilized cells
    • Felix, H. R. Permeabilized cells. Anal. Biochem. 1982, 120, 710-715.
    • (1982) Anal. Biochem. , vol.120 , pp. 710-715
    • Felix, H.R.1
  • 11
    • 4043119792 scopus 로고    scopus 로고
    • Periplasmic expression as a basis for whole cell kinetic screening of unnatural enzyme reactivities
    • Sroga, G. E.; Dordick, J. S. Periplasmic expression as a basis for whole cell kinetic screening of unnatural enzyme reactivities. Methods Enzymol. 2004, 388, 145-156.
    • (2004) Methods Enzymol. , vol.388 , pp. 145-156
    • Sroga, G.E.1    Dordick, J.S.2
  • 12
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins, R. D.; Kaneva, I.; Mulchandani, A.; Chen, W. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nat. Biotechnol. 1997, 15, 984-987.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 13
    • 0035125229 scopus 로고    scopus 로고
    • Cell surface display of organophosphorus hydrolase using ice nucleation protein
    • Shimazu, M.; Mulchandani, A.; Chen, W. Cell surface display of organophosphorus hydrolase using ice nucleation protein. Biotechnol. Prog. 2001, 17, 76-80.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 76-80
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 14
    • 0942297855 scopus 로고    scopus 로고
    • Functional display of foreign protein on cell surface of Escherichia coli using N-terminal domain of ice nucleation protein
    • Li, L.; Kang, D. G.; Cha, H. J. Functional display of foreign protein on cell surface of Escherichia coli using N-terminal domain of ice nucleation protein. Biotechnol. Bioeng. 2004, 85, 214-221.
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 214-221
    • Li, L.1    Kang, D.G.2    Cha, H.J.3
  • 15
    • 0024340489 scopus 로고
    • Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski, W. J.; Dumas, D. P.; Heitmeyer, D. P.; Lewis, V. E.; Raushel, F. M. Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 1989, 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
  • 16
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase
    • McDaniel, C. S.; Harper, L. L.; Wild, J. R. Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. J. Bacteriol. 1988, 170, 2306-2311.
    • (1988) J. Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 17
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry, W. W.; Karns, J. S. Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J. Bacteriol. 1989, 171, 6740-6746.
    • (1989) J. Bacteriol. , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 18
    • 0030711517 scopus 로고    scopus 로고
    • Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
    • Grimsley, J. K.; Scholtz, J. M.; Pace, C. N.; Wild, J. R. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry 1997, 36, 14366-14374.
    • (1997) Biochemistry , vol.36 , pp. 14366-14374
    • Grimsley, J.K.1    Scholtz, J.M.2    Pace, C.N.3    Wild, J.R.4
  • 19
    • 0028933772 scopus 로고
    • Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase
    • Lai, K.; Stolowich, N. J.; Wild, J. R. Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch. Biochem. Biophys. 1995, 318, 59-64.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 59-64
    • Lai, K.1    Stolowich, N.J.2    Wild, J.R.3
  • 20
    • 0024281297 scopus 로고
    • Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase
    • Lewis, V. E.; Donarski, W. J.; Wild, J. R.; Raushel, F. M. Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase. Biochemistry 1988, 27, 1591-1597.
    • (1988) Biochemistry , vol.27 , pp. 1591-1597
    • Lewis, V.E.1    Donarski, W.J.2    Wild, J.R.3    Raushel, F.M.4
  • 21
    • 84966188998 scopus 로고
    • Enzymatic hydrolysis of organophosphates: Cloning and expression of a parathion hydrolase gene from Pseudomonas diminuta
    • Serdar, C. M.; Gibson, D. T. Enzymatic hydrolysis of organophosphates: cloning and expression of a parathion hydrolase gene from Pseudomonas diminuta. BioTechnology 1985, 3, 567-571.
    • (1985) BioTechnology , vol.3 , pp. 567-571
    • Serdar, C.M.1    Gibson, D.T.2
  • 22
    • 0035812940 scopus 로고    scopus 로고
    • Enhancement of organophosphorus hydrolase yield in Escherichia coli using multiple gene fusions
    • Wu, C. F.; Valdes, J. J.; Rao, G.; Bentley, W. E. Enhancement of organophosphorus hydrolase yield in Escherichia coli using multiple gene fusions. Biotechnol. Bioeng. 2001, 75, 100-103.
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 100-103
    • Wu, C.F.1    Valdes, J.J.2    Rao, G.3    Bentley, W.E.4
  • 23
    • 0001154861 scopus 로고    scopus 로고
    • Observations of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: Monitoring protein expression and solubility
    • Cha, H. J.; Wu, C. F.; Valdes, J. J.; Rao, G.; Bentley, W. E. Observations of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: Monitoring protein expression and solubility. Biotechnol. Bioeng. 2000, 67, 565-574.
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 565-574
    • Cha, H.J.1    Wu, C.F.2    Valdes, J.J.3    Rao, G.4    Bentley, W.E.5
  • 24
    • 0035829836 scopus 로고    scopus 로고
    • Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase
    • Shimazu, M.; Mulchandani, A.; Chen, W. Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase. Biotechnol. Bioeng. 2001, 76, 318-324.
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 318-324
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 25
    • 0141977171 scopus 로고    scopus 로고
    • Cell surface display of organophosphorus hydrolase in Pseudomonas putida using an ice-nucleation protein anchor
    • Shimazu, M.; Nguyen, A.; Mulchandani, A.; Chen, W. Cell surface display of organophosphorus hydrolase in Pseudomonas putida using an ice-nucleation protein anchor. Biotechnol. Prog. 2003, 19, 1612-1614.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1612-1614
    • Shimazu, M.1    Nguyen, A.2    Mulchandani, A.3    Chen, W.4
  • 26
    • 0034632872 scopus 로고    scopus 로고
    • Making membranes in bacteria
    • Stuart, R. A.; Neupert, W. Making membranes in bacteria. Nature 2000, 406, 637-41.
    • (2000) Nature , vol.406 , pp. 637-641
    • Stuart, R.A.1    Neupert, W.2
  • 27
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 1993, 57, 50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 28
    • 0030271490 scopus 로고    scopus 로고
    • Secretion of recombinant proteins by gram-negative bacteria
    • Sandkvist, M.; Bagdasarian, M. Secretion of recombinant proteins by gram-negative bacteria. Curr. Opin. Biotechnol. 1996, 7, 505-511.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 505-511
    • Sandkvist, M.1    Bagdasarian, M.2
  • 29
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
    • Danese, P. N.; Silhavy, T. J. Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli. Annu. Rev. Genet. 1998, 32, 59-94.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 30
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G.; Dobberstein, B. Common principles of protein translocation across membranes. Science 1996, 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 31
    • 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.; Raushel, F. M. Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 1991, 30, 7438-7444.
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 32
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx, F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10, 411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 33
    • 0033532176 scopus 로고    scopus 로고
    • Cotranslocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway
    • Rodrigue, A.; Chanal, A.; Beck, K.; Muller, M.; Wu, L. Cotranslocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway. J. Biol. Chem. 1999, 274, 13223-13228.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Muller, M.4    Wu, L.5
  • 34
    • 0035793148 scopus 로고    scopus 로고
    • Display of green fluorescent protein on Escherichia coli cell surface
    • Shi, H.; Su, W. W. Display of green fluorescent protein on Escherichia coli cell surface. Enzyme Microbial. Technol. 2001, 28, 25-34.
    • (2001) Enzyme Microbial. Technol. , vol.28 , pp. 25-34
    • Shi, H.1    Su, W.W.2
  • 35
    • 0344560614 scopus 로고    scopus 로고
    • Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif
    • Xu, Z.; Lee, S. Y. Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif. Appl. Environ. Microbiol. 1999, 65, 5142-5147.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 5142-5147
    • Xu, Z.1    Lee, S.Y.2
  • 36
    • 0034736407 scopus 로고    scopus 로고
    • Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA
    • Winter, J.; Neubauer, P.; Glockshuber, R.; Rudolph, R. Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA. J. Biotechnol. 2000, 84, 175-185.
    • (2000) J. Biotechnol. , vol.84 , pp. 175-185
    • Winter, J.1    Neubauer, P.2    Glockshuber, R.3    Rudolph, R.4
  • 37
    • 0032747644 scopus 로고    scopus 로고
    • SecA: The ubiquitous component of preprotein translocase in prokaryotes
    • Schmidt, M. G.; Kiser, K. B. SecA: the ubiquitous component of preprotein translocase in prokaryotes. Microb. Infect. 1999, 1, 993-1004.
    • (1999) Microb. Infect. , vol.1 , pp. 993-1004
    • Schmidt, M.G.1    Kiser, K.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.