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Volumn 8, Issue 7, 2013, Pages

Refolding of a Thermostable Glyceraldehyde Dehydrogenase for Application in Synthetic Cascade Biomanufacturing

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DEHYDROGENASE; GLYCERALDEHYDE DEHYDROGENASE; ORGANIC SOLVENT; UNCLASSIFIED DRUG;

EID: 84880837893     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0070592     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 78650647970 scopus 로고    scopus 로고
    • Evolution, genomic analysis, and reconstruction of isobutanol tolerance in Escherichia coli
    • Atsumi S, Wu TY, Machado IMP, Huang WC, Chen PY, et al. (2010) Evolution, genomic analysis, and reconstruction of isobutanol tolerance in Escherichia coli. Molecular Systems Biology 6: 11.
    • (2010) Molecular Systems Biology , vol.6 , pp. 11
    • Atsumi, S.1    Wu, T.Y.2    Machado, I.M.P.3    Huang, W.C.4    Chen, P.Y.5
  • 2
    • 67650685558 scopus 로고    scopus 로고
    • An integrated network approach identifies the isobutanol response network of Escherichia coli
    • Brynildsen MP, Liao JC, (2009) An integrated network approach identifies the isobutanol response network of Escherichia coli. Molecular Systems Biology 5: 13.
    • (2009) Molecular Systems Biology , vol.5 , pp. 13
    • Brynildsen, M.P.1    Liao, J.C.2
  • 3
    • 84872404856 scopus 로고    scopus 로고
    • Biosynthesis "debugged": Novel bioproduction strategies
    • Guterl J-K, Sieber V, (2013) Biosynthesis "debugged": Novel bioproduction strategies. Engineering in Life Sciences 13: 4-18.
    • (2013) Engineering in Life Sciences , vol.13 , pp. 4-18
    • Guterl, J.-K.1    Sieber, V.2
  • 4
    • 0021792109 scopus 로고
    • Studies on cell-free metabolism - Ethanol-production by extracts of Zymomonas mobilis
    • Algar EM, Scopes RK, (1985) Studies on cell-free metabolism- Ethanol-production by extracts of Zymomonas mobilis. Journal of Biotechnology 2: 275-287.
    • (1985) Journal of Biotechnology , vol.2 , pp. 275-287
    • Algar, E.M.1    Scopes, R.K.2
  • 5
    • 55849139751 scopus 로고    scopus 로고
    • High-Yield Hydrogen Production from Starch and Water by a Synthetic Enzymatic Pathway
    • Zhang YHP, Evans BR, Mielenz JR, Hopkins RC, Adams MWW, (2007) High-Yield Hydrogen Production from Starch and Water by a Synthetic Enzymatic Pathway. Plos One 2: 6.
    • (2007) Plos One , vol.2 , pp. 6
    • Zhang, Y.H.P.1    Evans, B.R.2    Mielenz, J.R.3    Hopkins, R.C.4    Adams, M.W.W.5
  • 6
    • 61349097193 scopus 로고    scopus 로고
    • Spontaneous High-Yield Production of Hydrogen from Cellulosic Materials and Water Catalyzed by Enzyme Cocktails
    • Ye XH, Wang YR, Hopkins RC, Adams MWW, Evans BR, et al. (2009) Spontaneous High-Yield Production of Hydrogen from Cellulosic Materials and Water Catalyzed by Enzyme Cocktails. ChemSusChem 2: 149-152.
    • (2009) ChemSusChem , vol.2 , pp. 149-152
    • Ye, X.H.1    Wang, Y.R.2    Hopkins, R.C.3    Adams, M.W.W.4    Evans, B.R.5
  • 7
    • 81855185462 scopus 로고    scopus 로고
    • Toward low-cost biomanufacturing through in vitro synthetic biology: bottom-up design
    • Zhang YHP, Myung S, You C, Zhu Z, Rollin JA, (2011) Toward low-cost biomanufacturing through in vitro synthetic biology: bottom-up design. Journal of Materials Chemistry 21: 18877-18886.
    • (2011) Journal of Materials Chemistry , vol.21 , pp. 18877-18886
    • Zhang, Y.H.P.1    Myung, S.2    You, C.3    Zhu, Z.4    Rollin, J.A.5
  • 9
    • 84869409254 scopus 로고    scopus 로고
    • Cell-Free Metabolic Engineering: Production of Chemicals by Minimized Reaction Cascades
    • Guterl J-K, Garbe D, Carsten J, Steffler F, Sommer B, et al. (2012) Cell-Free Metabolic Engineering: Production of Chemicals by Minimized Reaction Cascades. ChemSusChem 5: 2165-2172.
    • (2012) ChemSusChem , vol.5 , pp. 2165-2172
    • Guterl, J.-K.1    Garbe, D.2    Carsten, J.3    Steffler, F.4    Sommer, B.5
  • 10
    • 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
  • 12
    • 84858251973 scopus 로고    scopus 로고
    • Solubilization of hemicellulose and lignin from wheat straw through microwave-assisted alkali treatment
    • Janker-Obermeier I, Sieber V, Faulstich M, Schieder D, (2012) Solubilization of hemicellulose and lignin from wheat straw through microwave-assisted alkali treatment. Industrial Crops and Products 39: 198-203.
    • (2012) Industrial Crops and Products , vol.39 , pp. 198-203
    • Janker-Obermeier, I.1    Sieber, V.2    Faulstich, M.3    Schieder, D.4
  • 13
    • 84655161967 scopus 로고    scopus 로고
    • Removal of monomer delignification products by laccase from Trametes versicolor
    • Kolb M, Sieber V, Amann M, Faulstich M, Schieder D, (2012) Removal of monomer delignification products by laccase from Trametes versicolor. Bioresource Technology 104: 298-304.
    • (2012) Bioresource Technology , vol.104 , pp. 298-304
    • Kolb, M.1    Sieber, V.2    Amann, M.3    Faulstich, M.4    Schieder, D.5
  • 14
    • 85057715328 scopus 로고    scopus 로고
    • Feasibility of simultaneous saccharification and juice co-fermentation on hydrothermal pretreated sweet sorghum bagasse for ethanol production
    • Rohowsky B, Häßler T, Gladis A, Remmele E, Schieder D,et al. (2012) Feasibility of simultaneous saccharification and juice co-fermentation on hydrothermal pretreated sweet sorghum bagasse for ethanol production. Applied Energy.
    • (2012) Applied Energy
    • Rohowsky, B.1    Häßler, T.2    Gladis, A.3    Remmele, E.4    Schieder, D.5
  • 17
  • 18
    • 33744459223 scopus 로고    scopus 로고
    • Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases
    • Rodriguez-Zavala JS, Allali-Hassani A, Weiner H, (2006) Characterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases. Protein Science 15: 1387-1396.
    • (2006) Protein Science , vol.15 , pp. 1387-1396
    • Rodriguez-Zavala, J.S.1    Allali-Hassani, A.2    Weiner, H.3
  • 20
    • 0024462630 scopus 로고
    • Kinetic evidence for human liver and stomach aldehyde dehydrogenase-3 representing an unique class of isozymes
    • Yin SJ, Liao CS, Wang SL, Chen YJ, Wu CW, (1989) Kinetic evidence for human liver and stomach aldehyde dehydrogenase-3 representing an unique class of isozymes. Biochemical Genetics 27: 321-331.
    • (1989) Biochemical Genetics , vol.27 , pp. 321-331
    • Yin, S.J.1    Liao, C.S.2    Wang, S.L.3    Chen, Y.J.4    Wu, C.W.5
  • 21
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier FW, (2005) Protein production by auto-induction in high-density shaking cultures. Protein Expression and Purification 41: 207-234.
    • (2005) Protein Expression and Purification , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 22
    • 0029329082 scopus 로고
    • Influence of substrate oscillations on acetate formation and growth-yield in Escherichia coli glucose-limited fed-batch cultivations
    • Neubauer P, Haggstrom L, Enfors SO, (1995) Influence of substrate oscillations on acetate formation and growth-yield in Escherichia coli glucose-limited fed-batch cultivations. Biotechnology and Bioengineering 47: 139-146.
    • (1995) Biotechnology and Bioengineering , vol.47 , pp. 139-146
    • Neubauer, P.1    Haggstrom, L.2    Enfors, S.O.3
  • 23
    • 0000448017 scopus 로고    scopus 로고
    • Single-step purification solubilization of recombinant proteins: Application to surfactant protein B
    • Holzinger A, Phillips KS, Weaver TE (1996) Single-step purification solubilization of recombinant proteins: Application to surfactant protein B. Biotechniques 20: 804-806, 808.
    • (1996) Biotechniques , vol.20
    • Holzinger, A.1    Phillips, K.S.2    Weaver, T.E.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
    • Laemmli UK, (1970) Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0017184389 scopus 로고
    • Rapid and Sensitive Method for Quantification of Microgram Quantities of Protein Utilizing Principle of Protein-Dye Binding
    • Bradford MM, (1976) Rapid and Sensitive Method for Quantification of Microgram Quantities of Protein Utilizing Principle of Protein-Dye Binding. Analytical Biochemistry 72: 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • In: Creighton TE, editor, Oxford: IRL Press
    • Schmid FX (1989) Spectral methods of characterizing protein conformation and conformational changes. In: Creighton TE, editor. Protein Structure: a Practical Approach. Oxford: IRL Press. 251-285 p.
    • (1989) Protein Structure: A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 29
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA, (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers 89: 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 30
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW, (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 31
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJE, (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nature Protocols 4: 363-371.
    • (2009) Nature Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 32
    • 0037465682 scopus 로고    scopus 로고
    • Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck
    • Sørensen HP, Sperling-Petersen HU, Mortensen KK, (2003) Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck. Journal of Chromatography B 786: 207-214.
    • (2003) Journal of Chromatography B , vol.786 , pp. 207-214
    • Sørensen, H.P.1    Sperling-Petersen, H.U.2    Mortensen, K.K.3
  • 33
    • 79551646745 scopus 로고    scopus 로고
    • Engineering of Therapeutic Proteins Production in Escherichia coli
    • Kamionka M, (2011) Engineering of Therapeutic Proteins Production in Escherichia coli. Current Pharmaceutical Biotechnology 12: 268-274.
    • (2011) Current Pharmaceutical Biotechnology , vol.12 , pp. 268-274
    • Kamionka, M.1
  • 34
    • 33750006508 scopus 로고    scopus 로고
    • Directed evolution: An approach to engineer enzymes
    • Kaur J, Sharma R, (2006) Directed evolution: An approach to engineer enzymes. Critical Reviews in Biotechnology 26: 165-199.
    • (2006) Critical Reviews in Biotechnology , vol.26 , pp. 165-199
    • Kaur, J.1    Sharma, R.2
  • 35
    • 32444448426 scopus 로고    scopus 로고
    • Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily
    • Reher M, Schönheit P, (2006) Glyceraldehyde dehydrogenases from the thermoacidophilic euryarchaeota Picrophilus torridus and Thermoplasma acidophilum, key enzymes of the non-phosphorylative Entner-Doudoroff pathway, constitute a novel enzyme family within the aldehyde dehydrogenase superfamily. Febs Letters 580: 1198-1204.
    • (2006) Febs Letters , vol.580 , pp. 1198-1204
    • Reher, M.1    Schönheit, P.2
  • 36
    • 33745574021 scopus 로고    scopus 로고
    • Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase
    • Jung JH, Lee SB, (2006) Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase. Biochemical Journal 397: 131-138.
    • (2006) Biochemical Journal , vol.397 , pp. 131-138
    • Jung, J.H.1    Lee, S.B.2
  • 37
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability
    • Vieille C, Zeikus GJ, (2001) Hyperthermophilic Enzymes: Sources, Uses, and Molecular Mechanisms for Thermostability. Microbiology and Molecular Biology Reviews 65: 1-43.
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 38
    • 84875486460 scopus 로고    scopus 로고
    • Thermostable alcohol dehydrogenase from Thermococcus kodakarensis KOD1 for enantioselective bioconversion of aromatic secondary alcohols
    • Wu X, Zhang C, Orita I, Imanaka T, Fukui T,et al. (2013) Thermostable alcohol dehydrogenase from Thermococcus kodakarensis KOD1 for enantioselective bioconversion of aromatic secondary alcohols. Applied and Environmental Microbiology.
    • (2013) Applied and Environmental Microbiology
    • Wu, X.1    Zhang, C.2    Orita, I.3    Imanaka, T.4    Fukui, T.5
  • 39
    • 0033858185 scopus 로고    scopus 로고
    • Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima
    • Consalvi V, Chiaraluce R, Giangiacomo L, Scandurra R, Christova P, et al. (2000) Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima. Protein Engineering 13: 501-507.
    • (2000) Protein Engineering , vol.13 , pp. 501-507
    • Consalvi, V.1    Chiaraluce, R.2    Giangiacomo, L.3    Scandurra, R.4    Christova, P.5
  • 40
    • 0023996274 scopus 로고
    • Protein design for non-aqueous solvents
    • Arnold FH, (1988) Protein design for non-aqueous solvents. Protein Engineering 2: 21-25.
    • (1988) Protein Engineering , vol.2 , pp. 21-25
    • Arnold, F.H.1
  • 41
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber V, Pluckthun A, Schmid FX, (1998) Selecting proteins with improved stability by a phage-based method. Nature Biotechnology 16: 955-960.
    • (1998) Nature Biotechnology , vol.16 , pp. 955-960
    • Sieber, V.1    Pluckthun, A.2    Schmid, F.X.3
  • 42
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: stability and function in aqueous and organic solvents
    • Cowan DA, (1997) Thermophilic proteins: stability and function in aqueous and organic solvents. Comparative biochemistry and physiology Part A, Physiology 118: 429-438.
    • (1997) Comparative Biochemistry and Physiology Part A, Physiology , vol.118 , pp. 429-438
    • Cowan, D.A.1
  • 43
    • 52949100181 scopus 로고    scopus 로고
    • Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners
    • Kim S, Lee SB, (2008) Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners. Protein Expression and Purification 62: 116-119.
    • (2008) Protein Expression and Purification , vol.62 , pp. 116-119
    • Kim, S.1    Lee, S.B.2
  • 44
    • 33745711929 scopus 로고    scopus 로고
    • Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli
    • Kube J, Brokamp C, Machielsen R, Oost J, Maerkl H, (2006) Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli. Extremophiles 10: 221-227.
    • (2006) Extremophiles , vol.10 , pp. 221-227
    • Kube, J.1    Brokamp, C.2    Machielsen, R.3    Oost, J.4    Maerkl, H.5
  • 47
    • 79551708337 scopus 로고    scopus 로고
    • Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis
    • Liu Y, Koh CMJ, Sun L, Ji L, (2011) Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis. Plos One 6: e16438.
    • (2011) Plos One , vol.6
    • Liu, Y.1    Koh, C.M.J.2    Sun, L.3    Ji, L.4
  • 48
    • 0039536809 scopus 로고
    • The nonoxidative decarboxylation of hydroxypyruvate in mammalian systems
    • Hedrick JL, Sallach HJ, (1964) The nonoxidative decarboxylation of hydroxypyruvate in mammalian systems. Archives of Biochemistry and Biophysics 105: 261-269.
    • (1964) Archives of Biochemistry and Biophysics , vol.105 , pp. 261-269
    • Hedrick, J.L.1    Sallach, H.J.2
  • 49
    • 0347601883 scopus 로고    scopus 로고
    • Tartrate dehydrogenase reductive decarboxylation: stereochemical generation of diastereotopically deuterated hydroxymethylenes
    • Ruszczycky MW, Anderson VE, (2004) Tartrate dehydrogenase reductive decarboxylation: stereochemical generation of diastereotopically deuterated hydroxymethylenes. Bioorganic Chemistry 32: 51-61.
    • (2004) Bioorganic Chemistry , vol.32 , pp. 51-61
    • Ruszczycky, M.W.1    Anderson, V.E.2
  • 50
    • 0036669691 scopus 로고    scopus 로고
    • Industrial microbial enzymes: their discovery by screening and use in large-scale production of useful chemicals in Japan
    • Ogawa J, Shimizu S, (2002) Industrial microbial enzymes: their discovery by screening and use in large-scale production of useful chemicals in Japan. Current Opinion in Biotechnology 13: 367-375.
    • (2002) Current Opinion in Biotechnology , vol.13 , pp. 367-375
    • Ogawa, J.1    Shimizu, S.2
  • 51
    • 70349554299 scopus 로고    scopus 로고
    • Characterisation of a Recombinant NADP-Dependent Glycerol Dehydrogenase from Gluconobacter oxydans and its Application in the Production of L-Glyceraldehyde
    • Richter N, Neumann M, Liese A, Wohlgemuth R, Eggert T, et al. (2009) Characterisation of a Recombinant NADP-Dependent Glycerol Dehydrogenase from Gluconobacter oxydans and its Application in the Production of L-Glyceraldehyde. ChemBioChem 10: 1888-1896.
    • (2009) ChemBioChem , vol.10 , pp. 1888-1896
    • Richter, N.1    Neumann, M.2    Liese, A.3    Wohlgemuth, R.4    Eggert, T.5
  • 52
    • 0036432690 scopus 로고    scopus 로고
    • Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties
    • Yamanaka Y, Kazuoka T, Yoshida M, Yamanaka K, Oikawa T, et al. (2002) Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties. Biochemical and Biophysical Research Communications 298: 632-637.
    • (2002) Biochemical and Biophysical Research Communications , vol.298 , pp. 632-637
    • Yamanaka, Y.1    Kazuoka, T.2    Yoshida, M.3    Yamanaka, K.4    Oikawa, T.5
  • 53
    • 72449181283 scopus 로고    scopus 로고
    • Gene cloning and characterization of an aldehyde dehydrogenase from long-chain alkane-degrading Geobacillus thermoleovorans B23
    • Kato T, Miyanaga A, Kanaya S, Morikawa M, (2010) Gene cloning and characterization of an aldehyde dehydrogenase from long-chain alkane-degrading Geobacillus thermoleovorans B23. Extremophiles 14: 33-39.
    • (2010) Extremophiles , vol.14 , pp. 33-39
    • Kato, T.1    Miyanaga, A.2    Kanaya, S.3    Morikawa, M.4
  • 54
    • 0027453979 scopus 로고
    • Cloning, nucleotide sequence, and efficient expression of the gene coding for thermostable aldehyde dehydrogenase from Bacillus stearothermophilus, and characterization of the enzyme
    • Imanaka T, Ohta T, Sakoda H, Widhyastuti N, Matsuoka M, (1993) Cloning, nucleotide sequence, and efficient expression of the gene coding for thermostable aldehyde dehydrogenase from Bacillus stearothermophilus, and characterization of the enzyme. Journal of Fermentation and Bioengineering 76: 161-167.
    • (1993) Journal of Fermentation and Bioengineering , vol.76 , pp. 161-167
    • Imanaka, T.1    Ohta, T.2    Sakoda, H.3    Widhyastuti, N.4    Matsuoka, M.5


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