메뉴 건너뛰기




Volumn 10, Issue 6, 2008, Pages 312-320

Metabolic engineering of Escherichia coli for 1-butanol and 1-propanol production via the keto-acid pathways

Author keywords

Alcohols; Biofuels; Butanol; Metabolic engineering

Indexed keywords

ALCOHOLS; AMINATION; AMINES; AMINO ACIDS; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; BIOSYNTHESIS; ESCHERICHIA COLI; GLUCOSE; ORGANIC ACIDS; TERNARY SYSTEMS;

EID: 54349114978     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2008.08.001     Document Type: Article
Times cited : (341)

References (31)
  • 1
    • 33845442201 scopus 로고    scopus 로고
    • Engineering yeast transcription machinery for improved ethanol tolerance and production
    • Alper H., Moxley J., Nevoigt E., Fink G.R., and Stephanopoulos G. Engineering yeast transcription machinery for improved ethanol tolerance and production. Science 314 (2006) 1565-1568
    • (2006) Science , vol.314 , pp. 1565-1568
    • Alper, H.1    Moxley, J.2    Nevoigt, E.3    Fink, G.R.4    Stephanopoulos, G.5
  • 3
    • 38049001166 scopus 로고    scopus 로고
    • Engineering synthetic non-fermentative pathways for production of branched-chain higher alcohols as biofuels
    • Atsumi S., Hanai T., and Liao J.C. Engineering synthetic non-fermentative pathways for production of branched-chain higher alcohols as biofuels. Nature 451 (2008) 86-89
    • (2008) Nature , vol.451 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3
  • 6
    • 34248196414 scopus 로고    scopus 로고
    • Dynamics of genomic-library enrichment and identification of solvent tolerance genes for Clostridium acetobutylicum
    • Borden J.R., and Papoutsakis E.T. Dynamics of genomic-library enrichment and identification of solvent tolerance genes for Clostridium acetobutylicum. Appl. Environ. Microbiol. 73 (2007) 3061-3068
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3061-3068
    • Borden, J.R.1    Papoutsakis, E.T.2
  • 7
    • 0028208541 scopus 로고
    • Overview of coenzyme A metabolism and its role in cellular toxicity
    • Brass E.P. Overview of coenzyme A metabolism and its role in cellular toxicity. Chem. Biol. Interact. 90 (1994) 203-214
    • (1994) Chem. Biol. Interact. , vol.90 , pp. 203-214
    • Brass, E.P.1
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in E. coli K-12 using PCR products
    • Datsenko K.A., and Wanner B.L. One-step inactivation of chromosomal genes in E. coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97 (2000) 6640-6645
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 10
    • 0035071031 scopus 로고    scopus 로고
    • Involvement of branched-chain amino acid aminotransferases in the production of fusel alcohols during fermentation in yeast
    • Eden A., Van Nedervelde L., Drukker M., Benvenisty N., and Debourg A. Involvement of branched-chain amino acid aminotransferases in the production of fusel alcohols during fermentation in yeast. Appl. Microbiol. Biotechnol. 55 (2001) 296-300
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 296-300
    • Eden, A.1    Van Nedervelde, L.2    Drukker, M.3    Benvenisty, N.4    Debourg, A.5
  • 11
    • 0026095288 scopus 로고
    • Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli
    • Eisenstein E. Cloning, expression, purification, and characterization of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 266 (1991) 5801-5807
    • (1991) J. Biol. Chem. , vol.266 , pp. 5801-5807
    • Eisenstein, E.1
  • 12
    • 0016813478 scopus 로고
    • Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli
    • Feldman D.A., and Datta P. Catabolite inactivation of biodegradative threonine dehydratase of Escherichia coli. J. Biochem. 14 (1975) 1760-1767
    • (1975) J. Biochem. , vol.14 , pp. 1760-1767
    • Feldman, D.A.1    Datta, P.2
  • 13
    • 0030908712 scopus 로고    scopus 로고
    • Enhanced butanol production by Clostridium beijerinckii BA101 grown in semidefined P2 medium containing 6 percent maltodextrin or glucose
    • Formanek J., Mackie R., and Blaschek H.P. Enhanced butanol production by Clostridium beijerinckii BA101 grown in semidefined P2 medium containing 6 percent maltodextrin or glucose. Appl. Environ. Microbiol. 63 (1997) 2306-2310
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2306-2310
    • Formanek, J.1    Mackie, R.2    Blaschek, H.P.3
  • 14
    • 0033014686 scopus 로고    scopus 로고
    • Expression of the Escherichia coli catabolic threonine dehydratase in Corynebacterium glutamicum and its effect on isoleucine production
    • Guillouet S., Rodal A.A., An G., Lessard P.A., and Sinskey A.J. Expression of the Escherichia coli catabolic threonine dehydratase in Corynebacterium glutamicum and its effect on isoleucine production. Appl. Environ. Microbiol. 65 (1999) 3100-3107
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3100-3107
    • Guillouet, S.1    Rodal, A.A.2    An, G.3    Lessard, P.A.4    Sinskey, A.J.5
  • 15
    • 57049088787 scopus 로고    scopus 로고
    • Gusyatiner, M.M., Lunts, M.G., Kozlov, Y.I., Ivanovskaya, L.V., Voroshilova, E.B., 2002. DNA coding for mutant isopropylmalate synthase l-leucine producing microorganism and method for producing l-leucine. US Patent 6403342.
    • Gusyatiner, M.M., Lunts, M.G., Kozlov, Y.I., Ivanovskaya, L.V., Voroshilova, E.B., 2002. DNA coding for mutant isopropylmalate synthase l-leucine producing microorganism and method for producing l-leucine. US Patent 6403342.
  • 16
    • 0007438459 scopus 로고
    • Nucleotide activation of threonine deaminase from Escherichia coli
    • Hirata M., Tokushige M., Inagaki A., and Hayaishi O. Nucleotide activation of threonine deaminase from Escherichia coli. J. Biol. Chem. 240 (1965) 1711-1717
    • (1965) J. Biol. Chem. , vol.240 , pp. 1711-1717
    • Hirata, M.1    Tokushige, M.2    Inagaki, A.3    Hayaishi, O.4
  • 17
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., and Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77 (1989) 61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 11944269758 scopus 로고    scopus 로고
    • Propanol as an end product of threonine fermentation
    • Janssen P.H. Propanol as an end product of threonine fermentation. Arch. Microbiol. 182 (2004) 482-486
    • (2004) Arch. Microbiol. , vol.182 , pp. 482-486
    • Janssen, P.H.1
  • 19
    • 0017073795 scopus 로고
    • l-Norvaline and l-homoisoleucine formation by Serratia marcescens
    • Kisumi M., Sugiura M., Kato J., and Chibata I. l-Norvaline and l-homoisoleucine formation by Serratia marcescens. J. Biochem. 79 (1976) 1021-1028
    • (1976) J. Biochem. , vol.79 , pp. 1021-1028
    • Kisumi, M.1    Sugiura, M.2    Kato, J.3    Chibata, I.4
  • 20
    • 0021909278 scopus 로고
    • Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence
    • Kuramitsu S., Ogawa T., Ogawa H., and Kagamiyama H. Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence. J. Biochem. 97 (1985) 993-999
    • (1985) J. Biochem. , vol.97 , pp. 993-999
    • Kuramitsu, S.1    Ogawa, T.2    Ogawa, H.3    Kagamiyama, H.4
  • 21
    • 0020678924 scopus 로고
    • Butanol production by a butanol-tolerant strain of Clostridium acetobutylicum in extruded corn broth
    • Lin Y., and Blaschek H.P. Butanol production by a butanol-tolerant strain of Clostridium acetobutylicum in extruded corn broth. Appl. Environ. Microbiol. 45 (1983) 966-973
    • (1983) Appl. Environ. Microbiol. , vol.45 , pp. 966-973
    • Lin, Y.1    Blaschek, H.P.2
  • 22
    • 0030861452 scopus 로고    scopus 로고
    • Independent and tight of transcriptional units in E. coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements
    • Lutz R., and Bujard H. Independent and tight of transcriptional units in E. coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements. Nucleic Acids Res. 25 (1997) 1203-1210
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1203-1210
    • Lutz, R.1    Bujard, H.2
  • 23
    • 33747135959 scopus 로고    scopus 로고
    • Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids
    • McCourt J.A., and Duggleby R.G. Acetohydroxyacid synthase and its role in the biosynthetic pathway for branched-chain amino acids. Amino Acids 31 (2006) 173-210
    • (2006) Amino Acids , vol.31 , pp. 173-210
    • McCourt, J.A.1    Duggleby, R.G.2
  • 24
    • 0028029330 scopus 로고
    • Expression of plasmid-encoded aad in Clostridium acetobutylicum M5 restores vigorous butanol production
    • Nair R.V., and Papoutsakis E.T. Expression of plasmid-encoded aad in Clostridium acetobutylicum M5 restores vigorous butanol production. J. Bacteriol. 176 (1994) 5843-5846
    • (1994) J. Bacteriol. , vol.176 , pp. 5843-5846
    • Nair, R.V.1    Papoutsakis, E.T.2
  • 26
    • 57049108411 scopus 로고    scopus 로고
    • Shiio, I., Nakamori, S., Sano, K., 1971. Fermentation production of l-threonine. US Patent 3580810.
    • Shiio, I., Nakamori, S., Sano, K., 1971. Fermentation production of l-threonine. US Patent 3580810.
  • 27
    • 35348859006 scopus 로고    scopus 로고
    • Structure and function of enzymes involved in the anaerobic degradation of l-threonine to propionate
    • Simanshu D.K., Chittori S., Savithri H.S., and Murthy M.R.N. Structure and function of enzymes involved in the anaerobic degradation of l-threonine to propionate. J. Biosci. 32 (2007) 1195-1206
    • (2007) J. Biosci. , vol.32 , pp. 1195-1206
    • Simanshu, D.K.1    Chittori, S.2    Savithri, H.S.3    Murthy, M.R.N.4
  • 28
    • 12244283725 scopus 로고    scopus 로고
    • Identification, cloning, and characterization of a Lactococcus lactis branched-chain α-keto acid decarboxylase involved in flavor formation
    • Smit B.A., van Hylckama Vlieg J.E.T., Engels W.J.M., Meijer L., Wouters J.T.M., and Smit G. Identification, cloning, and characterization of a Lactococcus lactis branched-chain α-keto acid decarboxylase involved in flavor formation. Appl. Environ. Microbiol. 71 (2005) 303-311
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 303-311
    • Smit, B.A.1    van Hylckama Vlieg, J.E.T.2    Engels, W.J.M.3    Meijer, L.4    Wouters, J.T.M.5    Smit, G.6
  • 29
    • 0017148030 scopus 로고
    • Regulation of a metabolic system in vitro: synthesis of threonine from aspartic acid
    • Szczesiul M., and Wampler D.E. Regulation of a metabolic system in vitro: synthesis of threonine from aspartic acid. Biochemistry 15 (1976) 2236-2244
    • (1976) Biochemistry , vol.15 , pp. 2236-2244
    • Szczesiul, M.1    Wampler, D.E.2
  • 30
    • 0345273884 scopus 로고
    • Threonine deamination in Escherichiacoli. II. Evidence for the two l-threonine deaminases
    • Umbarger H.E., and Brown B. Threonine deamination in Escherichiacoli. II. Evidence for the two l-threonine deaminases. J. Bacteriol. 73 (1957) 105-112
    • (1957) J. Bacteriol. , vol.73 , pp. 105-112
    • Umbarger, H.E.1    Brown, B.2
  • 31
    • 0031923093 scopus 로고    scopus 로고
    • Isolation and characterization of ethanol-tolerant mutants of E. coli KO11 for fuel ethanol production
    • Yomano L.P., York S.W., and Ingram L.O. Isolation and characterization of ethanol-tolerant mutants of E. coli KO11 for fuel ethanol production. J. Ind. Microbiol. Biotechnol. 20 (1998) 132-138
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.20 , pp. 132-138
    • Yomano, L.P.1    York, S.W.2    Ingram, L.O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.