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Volumn 15, Issue 1, 2013, Pages 218-225

A modified pathway for the production of acetone in Escherichia coli

Author keywords

Acetone; E. coli; Thioesterase

Indexed keywords

ACETYL-COA; BACILLUS SUBTILIS; CLOSTRIDIUM ACETOBUTYLICUM; DECARBOXYLASES; E. COLI; FED-BATCH CULTURES; GENETIC BACKGROUNDS; HAEMOPHILUS INFLUENZAE; HOST STRAIN; RECOMBINANT PLASMID; THIOESTERASES;

EID: 84872394631     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2012.08.001     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 0036191545 scopus 로고    scopus 로고
    • Identification of an acetoacetyl coenzyme A synthetase-dependent pathway for utilization of l-(+)-3-hydroxybutyrate in Sinorhizobium meliloti
    • Aneja P., Dziak R., Cai G.Q., Charles T.C. Identification of an acetoacetyl coenzyme A synthetase-dependent pathway for utilization of l-(+)-3-hydroxybutyrate in Sinorhizobium meliloti. J. Bacteriol. 2002, 184:1571-1577.
    • (2002) J. Bacteriol. , vol.184 , pp. 1571-1577
    • Aneja, P.1    Dziak, R.2    Cai, G.Q.3    Charles, T.C.4
  • 2
    • 0001243611 scopus 로고
    • Segregation of new lysogenic types during growth of a doubly lysogenic strain derived from Escherichia coli K12
    • Appleyard R.K. Segregation of new lysogenic types during growth of a doubly lysogenic strain derived from Escherichia coli K12. Genetics 1954, 39:440-452.
    • (1954) Genetics , vol.39 , pp. 440-452
    • Appleyard, R.K.1
  • 6
    • 0031886572 scopus 로고    scopus 로고
    • Expression of Clostridium acetobutylicum ATCC 824 genes in Escherichia coli for acetone production and acetate detoxification
    • Bermejo L.L., Welker N.E., Papoutsakis E.T. Expression of Clostridium acetobutylicum ATCC 824 genes in Escherichia coli for acetone production and acetate detoxification. Appl. Environ. Microbiol. 1998, 64:1079-1085.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1079-1085
    • Bermejo, L.L.1    Welker, N.E.2    Papoutsakis, E.T.3
  • 8
    • 0014674485 scopus 로고
    • A complementation analysis of the restriction and modification of DNA in Escherichia coli
    • Boyer H.W., Roulland-Dussoix D. A complementation analysis of the restriction and modification of DNA in Escherichia coli. J. Mol. Biol. 1969, 41:459-472.
    • (1969) J. Mol. Biol. , vol.41 , pp. 459-472
    • Boyer, H.W.1    Roulland-Dussoix, D.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with Β-galactosidase selection
    • Bullock W.O., Fernandez J.M., Short J.M.S. XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with Β-galactosidase selection. BioTechniques 1987, 5:376-379.
    • (1987) BioTechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.S.3
  • 11
    • 0032721968 scopus 로고    scopus 로고
    • Acetate metabolism in a pta mutant of Escherichia coli W3110: importance of maintaining acetyl coenzyme A flux for growth and survival
    • Chang D.-E., Shin S., Rhee J.-S., Pan J.-G. Acetate metabolism in a pta mutant of Escherichia coli W3110: importance of maintaining acetyl coenzyme A flux for growth and survival. J. Bacteriol. 1999, 181:6656-6663.
    • (1999) J. Bacteriol. , vol.181 , pp. 6656-6663
    • Chang, D.-E.1    Shin, S.2    Rhee, J.-S.3    Pan, J.-G.4
  • 12
    • 0032534048 scopus 로고    scopus 로고
    • Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step
    • Chong S., Montello G.E., Zhang A., Cantor E.J., Liao W., Xu M.Q., Benner J. Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 1998, 26:5109-5115.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5109-5115
    • Chong, S.1    Montello, G.E.2    Zhang, A.3    Cantor, E.J.4    Liao, W.5    Xu, M.Q.6    Benner, J.7
  • 14
    • 33749571961 scopus 로고    scopus 로고
    • Overcoming acetate in Escherichia coli recombinant protein fermentations
    • Eiteman M.A., Altman A. Overcoming acetate in Escherichia coli recombinant protein fermentations. Trends Biotechnol. 2006, 24:530-536.
    • (2006) Trends Biotechnol. , vol.24 , pp. 530-536
    • Eiteman, M.A.1    Altman, A.2
  • 15
    • 57049150206 scopus 로고    scopus 로고
    • Selection and optimization of microbial hosts for biofuel production
    • Fischer C.R., Klein-Marcuschamer D., Stephanopolous G. Selection and optimization of microbial hosts for biofuel production. Metab. Eng. 2008, 10:295-304.
    • (2008) Metab. Eng. , vol.10 , pp. 295-304
    • Fischer, C.R.1    Klein-Marcuschamer, D.2    Stephanopolous, G.3
  • 17
    • 37349093415 scopus 로고    scopus 로고
    • Engineered synthetic pathway for isopropanol production in Escherichia coli
    • Hanai T., Atsumi S., Liao J.C. Engineered synthetic pathway for isopropanol production in Escherichia coli. Appl. Environ. Microbiol. 2007, 73:7814-7818.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7814-7818
    • Hanai, T.1    Atsumi, S.2    Liao, J.C.3
  • 18
    • 0022970603 scopus 로고
    • Acetone-butanol fermentation revisited
    • Jones D.T., Woods D.R. Acetone-butanol fermentation revisited. Microbiol. Rev. 1986, 50:484-524.
    • (1986) Microbiol. Rev. , vol.50 , pp. 484-524
    • Jones, D.T.1    Woods, D.R.2
  • 19
    • 2142710129 scopus 로고    scopus 로고
    • Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis
    • Linne U., Schwarzer D., Schroeder G.N., Marahiel M.A. Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis. Eur. J. Biochem. 2004, 271:1536-1545.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1536-1545
    • Linne, U.1    Schwarzer, D.2    Schroeder, G.N.3    Marahiel, M.A.4
  • 20
    • 0020422133 scopus 로고
    • Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase
    • Lorowitz W., Clark D. Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase. J. Bacteriol. 1982, 152:935-938.
    • (1982) J. Bacteriol. , vol.152 , pp. 935-938
    • Lorowitz, W.1    Clark, D.2
  • 21
    • 80052625837 scopus 로고    scopus 로고
    • Metabolic engineering of Clostridium acetobutylicum: recent advances to improve butanol production
    • Lütke-Eversloh T., Bahl H. Metabolic engineering of Clostridium acetobutylicum: recent advances to improve butanol production. Curr. Opin. Biotechnol. 2011, 22:1-14.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 1-14
    • Lütke-Eversloh, T.1    Bahl, H.2
  • 22
    • 0027477171 scopus 로고
    • In vivo methylation in Escherichia coli by the Bacillus subtilis phage Φ3TI to protect plasmids from restriction upon transformation of Clostridium acetobutylicum ATCC 824
    • Mermelstein L.D., Papoutsakis E.T. In vivo methylation in Escherichia coli by the Bacillus subtilis phage Φ3TI to protect plasmids from restriction upon transformation of Clostridium acetobutylicum ATCC 824. Appl. Environ. Microbiol. 1993, 59:1077-1081.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1077-1081
    • Mermelstein, L.D.1    Papoutsakis, E.T.2
  • 23
    • 77953022341 scopus 로고    scopus 로고
    • A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: from biofuels and chemical, to biocatalysis and bioremediation
    • Nicolaou S.A., Gaida S.M., Papoutsakis E.T. A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: from biofuels and chemical, to biocatalysis and bioremediation. Metab. Eng. 2010, 12:307-331.
    • (2010) Metab. Eng. , vol.12 , pp. 307-331
    • Nicolaou, S.A.1    Gaida, S.M.2    Papoutsakis, E.T.3
  • 27
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer D., Mootz H.D., Linne U., Marahiel M.A. Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl. Acad. Sci. USA 2002, 99:14083-14088.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14083-14088
    • Schwarzer, D.1    Mootz, H.D.2    Linne, U.3    Marahiel, M.A.4
  • 29
    • 57049169148 scopus 로고    scopus 로고
    • Metabolic Engineering of the non-sporulating, non-solventogenic Clostridium acetobutylicum strain M5 to produce butanol without acetone demonstrate the robustness of the acid-formation pathways and the importance of the electron balance
    • Sillers R., Chow A., Tracy B., Papoutsakis E.F. Metabolic Engineering of the non-sporulating, non-solventogenic Clostridium acetobutylicum strain M5 to produce butanol without acetone demonstrate the robustness of the acid-formation pathways and the importance of the electron balance. Metab. Eng. 2008, 10:321-332.
    • (2008) Metab. Eng. , vol.10 , pp. 321-332
    • Sillers, R.1    Chow, A.2    Tracy, B.3    Papoutsakis, E.F.4
  • 30
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffat B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 1986, 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 31
    • 0024616857 scopus 로고
    • Coenzyme A transferase from Clostridium acetobutylicum ATCC 824 and its role in the uptake of acids
    • Wiesenborn D.P., Rudolph F.B., Papoutsakis E.T. Coenzyme A transferase from Clostridium acetobutylicum ATCC 824 and its role in the uptake of acids. Appl. Environ. Microbiol. 1989, 55:323-329.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 323-329
    • Wiesenborn, D.P.1    Rudolph, F.B.2    Papoutsakis, E.T.3
  • 32
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 1985, 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 33
    • 0037051944 scopus 로고    scopus 로고
    • The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis
    • Zhuang Z., Song F., Martin B.M., Dunaway-Mariano D. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett. 2002, 516:161-163.
    • (2002) FEBS Lett. , vol.516 , pp. 161-163
    • Zhuang, Z.1    Song, F.2    Martin, B.M.3    Dunaway-Mariano, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.