메뉴 건너뛰기




Volumn 9, Issue 7, 2014, Pages

2-Butanol and butanone production in Saccharomyces cerevisiae through combination of a B12 dependent dehydratase and a secondary alcohol dehydrogenase using a TEV-based expression system

Author keywords

[No Author keywords available]

Indexed keywords

2 BUTANOL; 2 BUTANONE; 2,3 BUTANEDIOL; ALCOHOL DEHYDROGENASE; DIOL DEHYDRATASE; HYDROLYASE; SECONDARY ALCOHOL DEHYDROGENASE; UNCLASSIFIED DRUG; 2-BUTANOL; ALCOHOL DEHYDROGENASE (NAD(P)+); ALKANONE; BACTERIAL PROTEIN; BUTANOL; CYANOCOBALAMIN; PROPANEDIOL DEHYDRATASE; PROTEINASE; TEV PROTEASE;

EID: 84904639399     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0102774     Document Type: Article
Times cited : (37)

References (36)
  • 1
    • 38149030843 scopus 로고    scopus 로고
    • Biobutanol: An attractive biofuel
    • Dürre P (2007) Biobutanol: An attractive biofuel. Biotechnology Journal 2: 1525-1534.
    • (2007) Biotechnology Journal , vol.2 , pp. 1525-1534
    • Dürre, P.1
  • 2
    • 38049001166 scopus 로고    scopus 로고
    • Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
    • Atsumi S, Hanai T, Liao JC (2008) Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 451: 86-89.
    • (2008) Nature , vol.451 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3
  • 3
    • 54349114978 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for 1-butanol and 1-propanol production via the keto-acid pathways
    • Shen CR, Liao JC (2008) Metabolic engineering of Escherichia coli for 1-butanol and 1-propanol production via the keto-acid pathways. Metab Eng 10: 312-320.
    • (2008) Metab Eng , vol.10 , pp. 312-320
    • Shen, C.R.1    Liao, J.C.2
  • 4
    • 84870384496 scopus 로고    scopus 로고
    • Isobutanol production in engineered Saccharomyces cerevisiae by overexpression of 2-ketoisovalerate decarboxylase and valine biosynthetic enzymes
    • Lee WH, Seo SO, Bae YH, Nan H, Jin YS, et al. (2012) Isobutanol production in engineered Saccharomyces cerevisiae by overexpression of 2-ketoisovalerate decarboxylase and valine biosynthetic enzymes. Bioprocess Biosyst Eng 35: 1467-1475.
    • (2012) Bioprocess Biosyst Eng , vol.35 , pp. 1467-1475
    • Lee, W.H.1    Seo, S.O.2    Bae, Y.H.3    Nan, H.4    Jin, Y.S.5
  • 5
    • 84884351687 scopus 로고    scopus 로고
    • Improving biobutanol production in engineered Saccharomyces cerevisiae by manipulation of acetyl-CoA metabolism
    • Krivoruchko A, Serrano-Amatriain C, Chen Y, Siewers V, Nielsen J (2013) Improving biobutanol production in engineered Saccharomyces cerevisiae by manipulation of acetyl-CoA metabolism. J Ind Microbiol Biotechnol 40: 1051-1056.
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 1051-1056
    • Krivoruchko, A.1    Serrano-Amatriain, C.2    Chen, Y.3    Siewers, V.4    Nielsen, J.5
  • 6
    • 38049162218 scopus 로고    scopus 로고
    • Expression of Clostridium acetobutylicum butanol synthetic genes in Escherichia coli
    • Inui M, Suda M, Kimura S, Yasuda K, Suzuki H, et al. (2008) Expression of Clostridium acetobutylicum butanol synthetic genes in Escherichia coli. Appl Microbiol Biotechnol 77: 1305-1316.
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1305-1316
    • Inui, M.1    Suda, M.2    Kimura, S.3    Yasuda, K.4    Suzuki, H.5
  • 7
    • 58249098522 scopus 로고    scopus 로고
    • Metabolic engineering of Saccharomyces cerevisiae for the production of n-butanol
    • Steen EJ, Chan R, Prasad N, Myers S, Petzold CJ, et al. (2008) Metabolic engineering of Saccharomyces cerevisiae for the production of n-butanol. Microb Cell Fact 7: 36.
    • (2008) Microb Cell Fact , vol.7 , pp. 36
    • Steen, E.J.1    Chan, R.2    Prasad, N.3    Myers, S.4    Petzold, C.J.5
  • 10
    • 84861442550 scopus 로고    scopus 로고
    • Production of 2,3-butanediol in Saccharomyces cerevisiae by in silico aided metabolic engineering
    • Ng CY, Jung MY, Lee J, Oh MK (2012) Production of 2,3-butanediol in Saccharomyces cerevisiae by in silico aided metabolic engineering. Microb Cell Fact 11: 1475-2859.
    • (2012) Microb Cell Fact , vol.11 , pp. 1475-2859
    • Ng, C.Y.1    Jung, M.Y.2    Lee, J.3    Oh, M.K.4
  • 11
    • 84882274841 scopus 로고    scopus 로고
    • Production of 2,3-butanediol by engineered Saccharomyces cerevisiae
    • Kim S-J, Seo S-O, Jin Y-S, Seo J-H (2013) Production of 2,3-butanediol by engineered Saccharomyces cerevisiae. Bioresour Technol 146: 274-281.
    • (2013) Bioresour Technol , vol.146 , pp. 274-281
    • Kim, S.-J.1    Seo, S.-O.2    Jin, Y.-S.3    Seo, J.-H.4
  • 12
    • 69549103148 scopus 로고    scopus 로고
    • Yeast artificial chromosomes employed for random assembly of biosynthetic pathways and production of diverse compounds in Saccharomyces cerevisiae
    • Naesby M, Nielsen S, Nielsen C, Green T, Tange T, et al. (2009) Yeast artificial chromosomes employed for random assembly of biosynthetic pathways and production of diverse compounds in Saccharomyces cerevisiae. Microb Cell Fact 8: 45.
    • (2009) Microb Cell Fact , vol.8 , pp. 45
    • Naesby, M.1    Nielsen, S.2    Nielsen, C.3    Green, T.4    Tange, T.5
  • 13
    • 0023349389 scopus 로고
    • Cloning of large segments of exogenous DNA into yeast by means of artificial chromosome vectors
    • Burke D, Carle G, Olson M (1987) Cloning of large segments of exogenous DNA into yeast by means of artificial chromosome vectors. Science 236: 806-812. (Pubitemid 17071153)
    • (1987) Science , vol.236 , Issue.4803 , pp. 806-812
    • Burke, D.T.1    Carle, G.F.2    Olson, M.V.3
  • 14
    • 0024282985 scopus 로고
    • Development of large DNA methods for plants: Molecular cloning of large segments of Arabidopsis and carrot DNA into yeast
    • Guzán P, Ecker JR (1988) Development of large DNA methods for plants: molecular cloning of large segments of Arabidopsis and carrot DNA into yeast. Nucleic Acids Res 16: 11091-11105.
    • (1988) Nucleic Acids Res , vol.16 , pp. 11091-11105
    • Guzán, P.1    Ecker, J.R.2
  • 15
    • 0029687623 scopus 로고    scopus 로고
    • Amplification of the Copy Number of YACs
    • Markie D, editor. Humana Press
    • Ling L, Smith D, Moir D (1996) Amplification of the Copy Number of YACs. In: Markie D, editor. YAC Protocols: Humana Press. 231-237.
    • (1996) YAC Protocols , pp. 231-237
    • Ling, L.1    Smith, D.2    Moir, D.3
  • 16
    • 0345447491 scopus 로고    scopus 로고
    • Exploiting the yeast Saccharomyces cerevisiae for the study of the organization and evolution of complex genomes
    • DOI 10.1016/S0168-6445(03)00070-6
    • Kouprina N, Larionov V (2003) Exploiting the yeast Saccharomyces cerevisiae for the study of the organization and evolution of complex genomes. FEMS Microbiol Rev 27: 629-649. (Pubitemid 37456861)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.5 , pp. 629-649
    • Kouprina, N.1    Larionov, V.2
  • 18
    • 78649652504 scopus 로고    scopus 로고
    • TEV protease-facilitated stoichiometric delivery of multiple genes using a single expression vector
    • Chen X, Pham E, Truong K (2010) TEV protease-facilitated stoichiometric delivery of multiple genes using a single expression vector. Protein Sci 19: 2379-2388.
    • (2010) Protein Sci , vol.19 , pp. 2379-2388
    • Chen, X.1    Pham, E.2    Truong, K.3
  • 19
    • 15244363693 scopus 로고    scopus 로고
    • Self-cleavage of fusion protein in vivo using TEV protease to yield native protein
    • Shih YP, Wu HC, Hu SM, Wang TF, Wang AH (2005) Self-cleavage of fusion protein in vivo using TEV protease to yield native protein. Protein Sci 14: 936-941.
    • (2005) Protein Sci , vol.14 , pp. 936-941
    • Shih, Y.P.1    Wu, H.C.2    Hu, S.M.3    Wang, T.F.4    Wang, A.H.5
  • 20
    • 27644565866 scopus 로고    scopus 로고
    • Overview and analysis of the polyprotein cleavage sites in the family Potyviridae
    • DOI 10.1111/j.1364-3703.2005.00296.x
    • Adams MJ, Antoniw JF, Beaudoin F (2005) Overview and analysis of the polyprotein cleavage sites in the family Potyviridae. Mol Plant Pathol 6: 471-487. (Pubitemid 41577092)
    • (2005) Molecular Plant Pathology , vol.6 , Issue.4 , pp. 471-487
    • Adams, M.J.1    Antoniw, J.F.2    Beaudoin, F.3
  • 21
    • 0030878624 scopus 로고    scopus 로고
    • Transgenic accumulation of two plant virus coat proteins on a single self processing polypeptide
    • Marcos JF, Beachy RN (1997) Transgenic accumulation of two plant virus coat proteins on a single self-processing polypeptide. J Gen Virol 78: 1771-1778. (Pubitemid 27343117)
    • (1997) Journal of General Virology , vol.78 , Issue.7 , pp. 1771-1778
    • Marcos, J.F.1    Beachy, R.N.2
  • 22
    • 3242784644 scopus 로고    scopus 로고
    • A yeast-based growth assay for the analysis of site-specific proteases
    • Köhler F (2003) A yeast-based growth assay for the analysis of site-specific proteases. Nucleic Acids Res 31: e16.
    • (2003) Nucleic Acids Res , vol.31
    • Köhler, F.1
  • 23
    • 33750021276 scopus 로고    scopus 로고
    • Evidence that Loading of Cohesin Onto Chromosomes Involves Opening of Its SMC Hinge
    • DOI 10.1016/j.cell.2006.08.048, PII S0092867406012761
    • Gruber S, Arumugam P, Katou Y, Kuglitsch D, Helmhart W, et al. (2006) Evidence that loading of cohesin onto chromosomes involves opening of its SMC hinge. Cell 127: 523-537. (Pubitemid 44647422)
    • (2006) Cell , vol.127 , Issue.3 , pp. 523-537
    • Gruber, S.1    Arumugam, P.2    Katou, Y.3    Kuglitsch, D.4    Helmhart, W.5    Shirahige, K.6    Nasmyth, K.7
  • 25
    • 0345097578 scopus 로고    scopus 로고
    • +-Dependent Secondary Alcohol Dehydrogenase in Propane Metabolism by Gordonia sp. Strain TY-5
    • DOI 10.1128/JB.185.24.7120-7128.2003
    • Kotani T, Yamamoto T, Yurimoto H, Sakai Y, Kato N (2003) Propane Monooxygenase and NAD+ -Dependent Secondary Alcohol Dehydrogenase in Propane Metabolism by Gordonia sp. Strain. J Bacteriol 185: 7120-7128. (Pubitemid 37509827)
    • (2003) Journal of Bacteriology , vol.185 , Issue.24 , pp. 7120-7128
    • Kotani, T.1    Yamamoto, T.2    Yurimoto, H.3    Sakai, Y.4    Kato, N.5
  • 26
    • 0030908893 scopus 로고    scopus 로고
    • +-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
    • DOI 10.1093/emboj/16.9.2179
    • Ansell R, Granath K, Hohmann S, Thevelein JM, Adler L (1997) The two isoenzymes for yeast NAD+ -dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. Embo J 16: 2179-2187. (Pubitemid 27258621)
    • (1997) EMBO Journal , vol.16 , Issue.9 , pp. 2179-2187
    • Ansell, R.1    Granath, K.2    Hohmann, S.3    Thevelein, J.M.4    Adler, L.5
  • 27
    • 0027215424 scopus 로고
    • Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells
    • Beauvoit B, Rigoulet M, Bunoust O, Raffard G, Canioni P, et al. (1993) Interactions between glucose metabolism and oxidative phosphorylations on respiratory-competent Saccharomyces cerevisiae cells. Eur J Biochem 214: 163-172. (Pubitemid 23168531)
    • (1993) European Journal of Biochemistry , vol.214 , Issue.1 , pp. 163-172
    • Beauvoit, B.1    Rigoulet, M.2    Bunoust, O.3    Raffard, G.4    Canioni, P.5    Guerin, B.6
  • 28
    • 0022507007 scopus 로고
    • Redox balances in the metabolism of sugars by yeasts
    • van Dijken JP, Scheffers WA (1986) Redox balances in the metabolism of sugars by yeasts. FEMS Microbiol Lett 32: 199-224.
    • (1986) FEMS Microbiol Lett , vol.32 , pp. 199-224
    • Van Dijken, J.P.1    Scheffers, W.A.2
  • 29
    • 0029891301 scopus 로고    scopus 로고
    • Evidence for enantiomorphic-enantiotopic group discrimination in diol dehydratase-catalyzed dehydration of meso-2,3-butanediol
    • DOI 10.1016/0040-4039(96)00808-8
    • Speranza G, Manitto P, Fontana G, Monti D, Galli A (1996) Evidence for enantiomorphic-enantiotopic group discrimination in diol dehydratase-catalyzed dehydration of meso-2,3-butanediol. Tetrahedron Lett 37: 4247-4250. (Pubitemid 26180343)
    • (1996) Tetrahedron Letters , vol.37 , Issue.24 , pp. 4247-4250
    • Speranza, G.1    Manitto, P.2    Fontana, G.3    Monti, D.4    Galli, A.5
  • 30
    • 0028970502 scopus 로고
    • The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli
    • Lawrence JG, Roth JR (1995) The cobalamin (coenzyme B12) biosynthetic genes of Escherichia coli. J Bacteriol 177: 6371-6380. (Pubitemid 3004526)
    • (1995) Journal of Bacteriology , vol.177 , Issue.22 , pp. 6371-6380
    • Lawrence, J.G.1    Roth, J.R.2
  • 31
    • 0029658689 scopus 로고    scopus 로고
    • 12): Synthesis and biological significance
    • DOI 10.1146/annurev.micro.50.1.137
    • Roth JR, Lawrence JG, Bobik TA (1996) Cobalamin (coenzyme B12): synthesis and biological significance. Annu Rev Microbiol 50: 137-181. (Pubitemid 26337461)
    • (1996) Annual Review of Microbiology , vol.50 , pp. 137-181
    • Roth, J.R.1    Lawrence, J.G.2    Bobik, T.A.3
  • 32
    • 1942502847 scopus 로고    scopus 로고
    • 12-Independent Glycerol Dehydratase from Clostridium butyricum: Preliminary Biochemical and Structural Characterization
    • DOI 10.1021/bi035930k
    • O'Brien JR, Raynaud C, Croux C, Girbal L, Soucaille P, et al. (2004) Insight into the Mechanism of the B12-Independent Glycerol Dehydratase from Clostridium butyricum: Preliminary Biochemical and Structural Characterization‡. Biochemistry 43: 4635-4645. (Pubitemid 38509083)
    • (2004) Biochemistry , vol.43 , Issue.16 , pp. 4635-4645
    • O'Brien, J.R.1    Raynaud, C.2    Croux, C.3    Girbal, L.4    Soucaille, P.5    Lanzilotta, W.N.6
  • 33
    • 78651261777 scopus 로고    scopus 로고
    • The diversity and molecular modelling analysis of B12-dependent and B12-independent glycerol dehydratases
    • Liu Y, Gallo AA, Bajpai RK, Chistoserdov A, Nelson A, et al. (2010) The diversity and molecular modelling analysis of B12-dependent and B12-independent glycerol dehydratases. Int J Bioinformat Res Appl 6: 484-507.
    • (2010) Int J Bioinformat Res Appl , vol.6 , pp. 484-507
    • Liu, Y.1    Gallo, A.A.2    Bajpai, R.K.3    Chistoserdov, A.4    Nelson, A.5
  • 34
    • 0032855711 scopus 로고    scopus 로고
    • Mechanism of Reactivation of Coenzyme B12-Dependent Diol Dehydratase by a Molecular Chaperone-like Reactivating Factor‡
    • Mori K, Toraya T (1999) Mechanism of Reactivation of Coenzyme B12-Dependent Diol Dehydratase by a Molecular Chaperone-like Reactivating Factor‡. Biochemistry 38: 13170-13178.
    • (1999) Biochemistry , vol.38 , pp. 13170-13178
    • Mori, K.1    Toraya, T.2
  • 35
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • DOI 10.1002/(SICI)1097-0061(19980130)14:2<115::AID
    • Brachmann CB, Davies A, Cost GJ, Caputo E, Li J, et al. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115-132. (Pubitemid 28062863)
    • (1998) Yeast , vol.14 , Issue.2 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 36
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.