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Volumn 11, Issue , 2012, Pages

Synthetic metabolic engineering-a novel, simple technology for designing a chimeric metabolic pathway

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE;

EID: 84865800305     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-11-120     Document Type: Article
Times cited : (71)

References (42)
  • 1
    • 0034986950 scopus 로고    scopus 로고
    • Microbial pathway engineering for industrial processes: evolution, combinatorial biosynthesis and rational design
    • 10.1016/S1369-5274(00)00213-7, 11378488
    • Rohlin L, Oh MK, Liao JC. Microbial pathway engineering for industrial processes: evolution, combinatorial biosynthesis and rational design. Curr Opin Microbiol 2001, 4:330-335. 10.1016/S1369-5274(00)00213-7, 11378488.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 330-335
    • Rohlin, L.1    Oh, M.K.2    Liao, J.C.3
  • 2
    • 33846950348 scopus 로고    scopus 로고
    • Challenges in engineering microbes for biofuels production
    • 10.1126/science.1139612, 17289987
    • Stephanopoulos G. Challenges in engineering microbes for biofuels production. Science 2007, 315:801-804. 10.1126/science.1139612, 17289987.
    • (2007) Science , vol.315 , pp. 801-804
    • Stephanopoulos, G.1
  • 3
    • 0027657693 scopus 로고
    • Metabolic engineering-methodologies and future prospects
    • 10.1016/0167-7799(93)90099-U, 7764086
    • Stephanopoulos G, Sinskey AJ. Metabolic engineering-methodologies and future prospects. Trends Biotechnol 1993, 11:392-396. 10.1016/0167-7799(93)90099-U, 7764086.
    • (1993) Trends Biotechnol , vol.11 , pp. 392-396
    • Stephanopoulos, G.1    Sinskey, A.J.2
  • 4
    • 75149167486 scopus 로고    scopus 로고
    • Five hard truths for synthetic biology
    • 10.1038/463288a, 20090726
    • Kwok R. Five hard truths for synthetic biology. Nature 2010, 463:288-290. 10.1038/463288a, 20090726.
    • (2010) Nature , vol.463 , pp. 288-290
    • Kwok, R.1
  • 5
    • 77449142867 scopus 로고    scopus 로고
    • Production of biocommodities and bioelectricity by cell-free synthetic enzymatic pathway biotransformations: challenges and opportunities
    • Zhang YHP. Production of biocommodities and bioelectricity by cell-free synthetic enzymatic pathway biotransformations: challenges and opportunities. Biotechnol Bioeng 2010, 105:663-677.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 663-677
    • Zhang, Y.H.P.1
  • 6
    • 83255164998 scopus 로고    scopus 로고
    • Cell-free synthetic biology: thinking outside the cell
    • 10.1016/j.ymben.2011.09.002, 21946161
    • Hodgman CE, Jewett MC. Cell-free synthetic biology: thinking outside the cell. Metab Eng 2012, 14:261-269. 10.1016/j.ymben.2011.09.002, 21946161.
    • (2012) Metab Eng , vol.14 , pp. 261-269
    • Hodgman, C.E.1    Jewett, M.C.2
  • 7
    • 0021856395 scopus 로고
    • Studies on cell-free metabolism: Ethanol production by a yeast glycolytic system reconstituted from purified enzymes
    • Welch P, Scopes RK. Studies on cell-free metabolism: Ethanol production by a yeast glycolytic system reconstituted from purified enzymes. J Biotechnol 1985, 2:257-273.
    • (1985) J Biotechnol , vol.2 , pp. 257-273
    • Welch, P.1    Scopes, R.K.2
  • 8
    • 0021792109 scopus 로고
    • Studies on cell-free metabolism: Ethanol production by extracts of Zymomonas mobilis
    • Algar EM, Scopes RK. Studies on cell-free metabolism: Ethanol production by extracts of Zymomonas mobilis. J Biotechnol 1985, 2:275-287.
    • (1985) J Biotechnol , vol.2 , pp. 275-287
    • Algar, E.M.1    Scopes, R.K.2
  • 9
    • 0035313249 scopus 로고    scopus 로고
    • Enzymes from extremophiles
    • 10.1016/S1367-5931(00)00183-6, 11282340
    • Demirjian DC, Morís-Varas F, Cassidy CS. Enzymes from extremophiles. Curr Opin Chem Biol 2001, 5:144-151. 10.1016/S1367-5931(00)00183-6, 11282340.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 144-151
    • Demirjian, D.C.1    Morís-Varas, F.2    Cassidy, C.S.3
  • 10
    • 0033050423 scopus 로고    scopus 로고
    • Extremophiles as a source of novel enzymes for industrial application
    • 10.1007/s002530051456, 10422220
    • Niehaus F, Bertoldo C, Kähler M, Antranikian G. Extremophiles as a source of novel enzymes for industrial application. Appl Microbiol Biotechnol 1999, 51:711-729. 10.1007/s002530051456, 10422220.
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 711-729
    • Niehaus, F.1    Bertoldo, C.2    Kähler, M.3    Antranikian, G.4
  • 11
    • 77955055053 scopus 로고    scopus 로고
    • Production of 2-deoxyribose 5-phosphate from fructose to demonstrate a potential of artificial bio-synthetic pathway using thermophilic enzymes
    • 10.1016/j.jbiotec.2010.06.008, 20547190
    • Honda K, Maya S, Omasa T, Hirota R, Kuroda A, Ohtake H. Production of 2-deoxyribose 5-phosphate from fructose to demonstrate a potential of artificial bio-synthetic pathway using thermophilic enzymes. J Biotechnol 2010, 148:204-207. 10.1016/j.jbiotec.2010.06.008, 20547190.
    • (2010) J Biotechnol , vol.148 , pp. 204-207
    • Honda, K.1    Maya, S.2    Omasa, T.3    Hirota, R.4    Kuroda, A.5    Ohtake, H.6
  • 12
    • 33947166251 scopus 로고    scopus 로고
    • Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for D-amino acid dipeptide synthesis
    • 10.1263/jbb.103.179, 17368402
    • Sato M, Masuda Y, Kirimura K, Kino K. Thermostable ATP regeneration system using polyphosphate kinase from Thermosynechococcus elongatus BP-1 for D-amino acid dipeptide synthesis. J Biosci Bioeng 2007, 103:179-184. 10.1263/jbb.103.179, 17368402.
    • (2007) J Biosci Bioeng , vol.103 , pp. 179-184
    • Sato, M.1    Masuda, Y.2    Kirimura, K.3    Kino, K.4
  • 13
    • 34548514448 scopus 로고    scopus 로고
    • Use of an Escherichia coli recombinant producing thermostable polyphosphate kinase as an ATP regenerator to produce fructose 1,6-diphosphate
    • 10.1128/AEM.00278-07, 2042086, 17616610
    • Iwamoto S, Motomura K, Shinoda Y, Urata M, Kato J, Takiguchi N, Ohtake H, Hirota R, Kuroda A. Use of an Escherichia coli recombinant producing thermostable polyphosphate kinase as an ATP regenerator to produce fructose 1,6-diphosphate. Appl Environ Microbiol 2007, 73:5676-5678. 10.1128/AEM.00278-07, 2042086, 17616610.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5676-5678
    • Iwamoto, S.1    Motomura, K.2    Shinoda, Y.3    Urata, M.4    Kato, J.5    Takiguchi, N.6    Ohtake, H.7    Hirota, R.8    Kuroda, A.9
  • 14
    • 67649876342 scopus 로고    scopus 로고
    • Overexpression and simple purification of the Thermotoga maritima 6-phosphogluconate dehydrogenase in Escherichia coli and its application for NADPH regeneration
    • 10.1186/1475-2859-8-30, 2701922, 19497097
    • Wang Y, Zhang YHP. Overexpression and simple purification of the Thermotoga maritima 6-phosphogluconate dehydrogenase in Escherichia coli and its application for NADPH regeneration. Microb Cell Fact 2009, 8:30. 10.1186/1475-2859-8-30, 2701922, 19497097.
    • (2009) Microb Cell Fact , vol.8 , pp. 30
    • Wang, Y.1    Zhang, Y.H.P.2
  • 15
    • 77955853857 scopus 로고    scopus 로고
    • Metabolic engineering to improve ethanol production in Thermoanaerobacter mathranii
    • 10.1007/s00253-010-2703-3, 20552355
    • Yao S, Mikkelsen MJ. Metabolic engineering to improve ethanol production in Thermoanaerobacter mathranii. Appl Microbiol Biotechnol 2010, 88:199-208. 10.1007/s00253-010-2703-3, 20552355.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 199-208
    • Yao, S.1    Mikkelsen, M.J.2
  • 18
    • 0033215210 scopus 로고    scopus 로고
    • Pathway alignment: application to the comparative analysis of glycolytic enzymes
    • 10.1042/0264-6021:3430115, 1220531, 10493919
    • Dandekar T, Schuster S, Snel B, Huynen M, Bork P. Pathway alignment: application to the comparative analysis of glycolytic enzymes. Biochem J 1999, 343:115-124. 10.1042/0264-6021:3430115, 1220531, 10493919.
    • (1999) Biochem J , vol.343 , pp. 115-124
    • Dandekar, T.1    Schuster, S.2    Snel, B.3    Huynen, M.4    Bork, P.5
  • 19
    • 0029417337 scopus 로고
    • Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus
    • 10.1074/jbc.270.51.30453, 8530474
    • Kengen SWM, Tuininga JE, de Bok FAM, Stams AJM, de Vos WM. Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 1995, 270:30453-30457. 10.1074/jbc.270.51.30453, 8530474.
    • (1995) J Biol Chem , vol.270 , pp. 30453-30457
    • Kengen, S.W.M.1    Tuininga, J.E.2    de Bok, F.A.M.3    Stams, A.J.M.4    de Vos, W.M.5
  • 20
    • 0033597824 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus
    • 10.1074/jbc.274.30.21023, 10409652
    • Tuininga JE, Verhees CH, van der Oost J, Kengen SW, Stams AJ, de Vos WM. Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 1999, 274:21023-21028. 10.1074/jbc.274.30.21023, 10409652.
    • (1999) J Biol Chem , vol.274 , pp. 21023-21028
    • Tuininga, J.E.1    Verhees, C.H.2    van der Oost, J.3    Kengen, S.W.4    Stams, A.J.5    de Vos, W.M.6
  • 21
    • 0028927080 scopus 로고
    • Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
    • 10.1074/jbc.270.15.8389, 7721730
    • Mukund S, Adams MW. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 1995, 270:8389-8392. 10.1074/jbc.270.15.8389, 7721730.
    • (1995) J Biol Chem , vol.270 , pp. 8389-8392
    • Mukund, S.1    Adams, M.W.2
  • 22
    • 0032513241 scopus 로고    scopus 로고
    • NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties
    • 10.1074/jbc.273.11.6149, 9497334
    • Brunner NA, Brinkmann H, Siebers B, Hensel R. NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J Biol Chem 1998, 273:6149-6156. 10.1074/jbc.273.11.6149, 9497334.
    • (1998) J Biol Chem , vol.273 , pp. 6149-6156
    • Brunner, N.A.1    Brinkmann, H.2    Siebers, B.3    Hensel, R.4
  • 23
    • 38049000397 scopus 로고    scopus 로고
    • The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of Sulfolobus solfataricus: a key-enzyme of the semi-phosphorylative branch of the Entner-Doudoroff pathway
    • Ettema TJ, Ahmed H, Geerling AC, van der Oost J, Siebers B. The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) of Sulfolobus solfataricus: a key-enzyme of the semi-phosphorylative branch of the Entner-Doudoroff pathway. Extremophiles 2007, 12:75-88.
    • (2007) Extremophiles , vol.12 , pp. 75-88
    • Ettema, T.J.1    Ahmed, H.2    Geerling, A.C.3    van der Oost, J.4    Siebers, B.5
  • 24
    • 80051931950 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of the three metabolic routes in Thermococcus kodakarensis linking glyceraldehyde 3-phosphate and 3-phosphoglycerate
    • 10.1111/j.1365-2958.2011.07762.x, 21736643
    • Matsubara K, Yokooji Y, Atomi H, Imanaka T. Biochemical and genetic characterization of the three metabolic routes in Thermococcus kodakarensis linking glyceraldehyde 3-phosphate and 3-phosphoglycerate. Mol Microbiol 2011, 81:1300-1312. 10.1111/j.1365-2958.2011.07762.x, 21736643.
    • (2011) Mol Microbiol , vol.81 , pp. 1300-1312
    • Matsubara, K.1    Yokooji, Y.2    Atomi, H.3    Imanaka, T.4
  • 25
    • 37849041676 scopus 로고    scopus 로고
    • Utilization of molasses sugar for lactic acid production by Lactobacillus delbrueckii subsp. delbrueckiimutant Uc-3 in batch fermentation
    • Dumbrepatil A, Adsul M, Chaudhari S, Khire J, Gokhale D. Utilization of molasses sugar for lactic acid production by Lactobacillus delbrueckii subsp. delbrueckiimutant Uc-3 in batch fermentation. Appl Environ Microbial 2008, 74:333-335.
    • (2008) Appl Environ Microbial , vol.74 , pp. 333-335
    • Dumbrepatil, A.1    Adsul, M.2    Chaudhari, S.3    Khire, J.4    Gokhale, D.5
  • 27
    • 0035145302 scopus 로고    scopus 로고
    • Lactic acid recovery from fermentation broth using one-stage electrodialysis
    • Kim YH, Moon SH. Lactic acid recovery from fermentation broth using one-stage electrodialysis. J Chem Technol 2001, 76:169-178.
    • (2001) J Chem Technol , vol.76 , pp. 169-178
    • Kim, Y.H.1    Moon, S.H.2
  • 28
    • 0022893844 scopus 로고
    • Stability of NADPH: effect of various factors on the kinetics of degradation
    • Wu JT, Wu LH, Knight JA. Stability of NADPH: effect of various factors on the kinetics of degradation. Clin Chem 1986, 32:314-319.
    • (1986) Clin Chem , vol.32 , pp. 314-319
    • Wu, J.T.1    Wu, L.H.2    Knight, J.A.3
  • 29
    • 2642641281 scopus 로고    scopus 로고
    • Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough
    • 10.1007/s007920050051, 9672687
    • González JM, Masuchi Y, Robb FT, Ammerman JW, Maeder DL, Yanagibayashi M, Tamaoka J, Kato C. Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough. Extremophiles 1998, 2:123-130. 10.1007/s007920050051, 9672687.
    • (1998) Extremophiles , vol.2 , pp. 123-130
    • González, J.M.1    Masuchi, Y.2    Robb, F.T.3    Ammerman, J.W.4    Maeder, D.L.5    Yanagibayashi, M.6    Tamaoka, J.7    Kato, C.8
  • 30
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese Thermal Spa
    • Oshima T, Imahori K. Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese Thermal Spa. Int J Syst Bacteriol 1974, 24:102-112.
    • (1974) Int J Syst Bacteriol , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2
  • 31
    • 34447538639 scopus 로고    scopus 로고
    • Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea
    • 10.1007/s00792-007-0094-x, 17576516
    • Johnsen U, Schönheit P. Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea. Extremophiles 2007, 11:647-657. 10.1007/s00792-007-0094-x, 17576516.
    • (2007) Extremophiles , vol.11 , pp. 647-657
    • Johnsen, U.1    Schönheit, P.2
  • 32
    • 0018818947 scopus 로고
    • Bacterial lactate dehydrogenases
    • 373236, 6997721
    • Garvie EI. Bacterial lactate dehydrogenases. Microbiol Rev 1980, 44:106-139. 373236, 6997721.
    • (1980) Microbiol Rev , vol.44 , pp. 106-139
    • Garvie, E.I.1
  • 34
    • 4344705563 scopus 로고    scopus 로고
    • Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies
    • 10.1002/elps.200305905, 15237399
    • Itoh A, Ohashi Y, Soga T, Mori H, Nishioka T, Tomita M. Application of capillary electrophoresis-mass spectrometry to synthetic in vitro glycolysis studies. Electrophoresis 2004, 25:1996-2002. 10.1002/elps.200305905, 15237399.
    • (2004) Electrophoresis , vol.25 , pp. 1996-2002
    • Itoh, A.1    Ohashi, Y.2    Soga, T.3    Mori, H.4    Nishioka, T.5    Tomita, M.6
  • 35
    • 0025338715 scopus 로고
    • The bacterial phosphoenolpyruvate: glycose phosphotransferase system
    • 10.1146/annurev.bi.59.070190.002433, 2197982
    • Meadow ND, Fox DK, Roseman S. The bacterial phosphoenolpyruvate: glycose phosphotransferase system. Annu Rev Biochem 1990, 59:497-542. 10.1146/annurev.bi.59.070190.002433, 2197982.
    • (1990) Annu Rev Biochem , vol.59 , pp. 497-542
    • Meadow, N.D.1    Fox, D.K.2    Roseman, S.3
  • 36
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
    • 372926, 8246840
    • Postma PW, Lengeler JW, Jacobson GR. Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 1993, 57:543-594. 372926, 8246840.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 37
    • 79960414910 scopus 로고    scopus 로고
    • Systems metabolic engineering for chemicals and materials
    • 10.1016/j.tibtech.2011.04.001, 21561673
    • Lee JW, Kim TY, Jang YS, Choi S, Lee SY. Systems metabolic engineering for chemicals and materials. Trends Biotechnol 2011, 29:370-378. 10.1016/j.tibtech.2011.04.001, 21561673.
    • (2011) Trends Biotechnol , vol.29 , pp. 370-378
    • Lee, J.W.1    Kim, T.Y.2    Jang, Y.S.3    Choi, S.4    Lee, S.Y.5
  • 38
    • 0032959795 scopus 로고    scopus 로고
    • Engineering a central metabolic pathway: glycolysis with no net phosphorylation in an Escherichia coli gap mutant complemented with a plant GapN gene
    • 10.1016/S0014-5793(99)00430-5, 10338122
    • Valverde F, Losada M, Serrano A. Engineering a central metabolic pathway: glycolysis with no net phosphorylation in an Escherichia coli gap mutant complemented with a plant GapN gene. FEBS Lett 1999, 449:153-158. 10.1016/S0014-5793(99)00430-5, 10338122.
    • (1999) FEBS Lett , vol.449 , pp. 153-158
    • Valverde, F.1    Losada, M.2    Serrano, A.3
  • 39
    • 0033045731 scopus 로고    scopus 로고
    • Artificial redox coenzymes: Biomimetic analogues of NAD+
    • Ansell RJ, Lowe CR. Artificial redox coenzymes: Biomimetic analogues of NAD+. Appl Microbiol Biotechnol 1999, 51:703-710.
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 703-710
    • Ansell, R.J.1    Lowe, C.R.2
  • 40
    • 59449108061 scopus 로고    scopus 로고
    • Engineering cytochrome P450 enzymes for improved activity towards biomimetic 1,4-NADH cofactors
    • Ryan JD, Fish RH, Clark DS. Engineering cytochrome P450 enzymes for improved activity towards biomimetic 1,4-NADH cofactors. Chem Bio Chem 2008, 9:2579-2582.
    • (2008) Chem Bio Chem , vol.9 , pp. 2579-2582
    • Ryan, J.D.1    Fish, R.H.2    Clark, D.S.3
  • 42
    • 53049107187 scopus 로고    scopus 로고
    • Engineering the spatial organization of metabolic enzymes: mimicking nature's synergy
    • 10.1016/j.copbio.2008.07.006, 18725290
    • Conrado RJ, Varner JD, DeLisa MP. Engineering the spatial organization of metabolic enzymes: mimicking nature's synergy. Curr Opin Biotechnol 2008, 19:492-499. 10.1016/j.copbio.2008.07.006, 18725290.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 492-499
    • Conrado, R.J.1    Varner, J.D.2    DeLisa, M.P.3


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