메뉴 건너뛰기




Volumn 171, Issue 1, 2014, Pages 45-55

The bacterial Entner-Doudoroff pathway does not replace glycolysis in Saccharomyces cerevisiae due to the lack of activity of iron-sulfur cluster enzyme 6-phosphogluconate dehydratase

Author keywords

Entner Doudoroff pathway; Iron sulfur cluster; KDPG aldolase; Metabolic engineering; Product yield; Saccharomyces cerevisiae

Indexed keywords

ALDOLASES; BIOCHEMICAL PATHWAY; ENTNER-DOUDOROFF PATHWAYS; FUNCTIONAL EXPRESSION; GLYCOLYTIC PATHWAYS; IRON-SULFUR CLUSTERS; PENTOSE PHOSPHATE PATHWAY; PRODUCT YIELDS;

EID: 84890895919     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2013.11.025     Document Type: Article
Times cited : (36)

References (64)
  • 1
    • 0022763351 scopus 로고
    • Deletion of the phosphoglucose isomerase structural gene makes growth and sporulation glucose dependent in Saccharomyces cerevisiae
    • Aguilera A. Deletion of the phosphoglucose isomerase structural gene makes growth and sporulation glucose dependent in Saccharomyces cerevisiae. Mol. Gen. Genet. 1986, 204:310-316.
    • (1986) Mol. Gen. Genet. , vol.204 , pp. 310-316
    • Aguilera, A.1
  • 3
    • 0037962155 scopus 로고    scopus 로고
    • A modified Saccharomyces cerevisiae strain that consumes l-arabinose and produces ethanol
    • Becker J., Boles E. A modified Saccharomyces cerevisiae strain that consumes l-arabinose and produces ethanol. Appl. Environ. Microbiol. 2003, 69:4144-4150.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4144-4150
    • Becker, J.1    Boles, E.2
  • 4
    • 25444467580 scopus 로고    scopus 로고
    • 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast
    • 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast. Genome Biol. 2005, 6:R49.
    • (2005) Genome Biol. , vol.6
    • Blank, L.M.1    Kuepfer, L.2    Sauer, U.3
  • 5
    • 0032455440 scopus 로고    scopus 로고
    • Identification and characterization of MAE1, the Saccharomyces cerevisiae structural gene encoding mitochondrial malic enzyme
    • Boles E., de Jong-Gubbels P., Pronk J.T. Identification and characterization of MAE1, the Saccharomyces cerevisiae structural gene encoding mitochondrial malic enzyme. J. Bacteriol. 1998, 180:2875-2882.
    • (1998) J. Bacteriol. , vol.180 , pp. 2875-2882
    • Boles, E.1    de Jong-Gubbels, P.2    Pronk, J.T.3
  • 6
    • 0027524880 scopus 로고
    • The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant
    • Boles E., Lehnert W., Zimmermann F.K. The role of the NAD-dependent glutamate dehydrogenase in restoring growth on glucose of a Saccharomyces cerevisiae phosphoglucose isomerase mutant. Eur. J. Biochem. 1993, 217:469-477.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 469-477
    • Boles, E.1    Lehnert, W.2    Zimmermann, F.K.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation 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
  • 8
    • 64749094343 scopus 로고    scopus 로고
    • Functional expression of a bacterial xylose isomerase in Saccharomyces cerevisiae
    • Brat D., Boles E., Wiedemann B. Functional expression of a bacterial xylose isomerase in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 2009, 75:2304-2311.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2304-2311
    • Brat, D.1    Boles, E.2    Wiedemann, B.3
  • 9
    • 84865777627 scopus 로고    scopus 로고
    • Cytosolic re-localization and optimization of valine synthesis and catabolism enables increased isobutanol production with the yeast Saccharomyces cerevisiae
    • Brat D., Weber C., Lorenzen W., Bode H.B., Boles E. Cytosolic re-localization and optimization of valine synthesis and catabolism enables increased isobutanol production with the yeast Saccharomyces cerevisiae. Biotechnol. Biofuels 2012, 5:65.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 65
    • Brat, D.1    Weber, C.2    Lorenzen, W.3    Bode, H.B.4    Boles, E.5
  • 11
    • 35648977174 scopus 로고    scopus 로고
    • Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates
    • Cheriyan M., Toone E.J., Fierke C.A. Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates. Protein Sci. 2007, 16:2368-2377.
    • (2007) Protein Sci. , vol.16 , pp. 2368-2377
    • Cheriyan, M.1    Toone, E.J.2    Fierke, C.A.3
  • 13
    • 0026913168 scopus 로고
    • The Entner-Doudoroff pathway: history, physiology and molecular biology
    • Conway T. The Entner-Doudoroff pathway: history, physiology and molecular biology. FEMS Microbiol. Rev. 1992, 9:1-27.
    • (1992) FEMS Microbiol. Rev. , vol.9 , pp. 1-27
    • Conway, T.1
  • 14
    • 84860258944 scopus 로고    scopus 로고
    • Energy coupling in Saccharomyces cerevisiae: selected opportunities for metabolic engineering
    • de Kok S., Kozak B.U., Pronk J.T., van Maris A.J.A. Energy coupling in Saccharomyces cerevisiae: selected opportunities for metabolic engineering. FEMS Yeast Res. 2012, 12:387-397.
    • (2012) FEMS Yeast Res. , vol.12 , pp. 387-397
    • de Kok, S.1    Kozak, B.U.2    Pronk, J.T.3    van Maris, A.J.A.4
  • 15
    • 0015609412 scopus 로고
    • New pathway for nonphosphorylated degradation of gluconate by Aspergillus niger
    • Elzainy T.A., Hassan M.M., Allam A.M. New pathway for nonphosphorylated degradation of gluconate by Aspergillus niger. J. Bacteriol. 1973, 114:457-459.
    • (1973) J. Bacteriol. , vol.114 , pp. 457-459
    • Elzainy, T.A.1    Hassan, M.M.2    Allam, A.M.3
  • 16
    • 0015905047 scopus 로고
    • Occurrence of the non-phosphorylative pathway for gluconate degradation in different fungi
    • Elzainy T.A., Hassan M.M., Allam A.M. Occurrence of the non-phosphorylative pathway for gluconate degradation in different fungi. Biochem. Syst. Ecol. 1973, 1:127-128.
    • (1973) Biochem. Syst. Ecol. , vol.1 , pp. 127-128
    • Elzainy, T.A.1    Hassan, M.M.2    Allam, A.M.3
  • 17
    • 76949122636 scopus 로고
    • Glucose and gluconic acid oxidation of Pseudomonas saccharophila
    • Entner N., Doudoroff M. Glucose and gluconic acid oxidation of Pseudomonas saccharophila. J. Biol. Chem. 1952, 196:853-862.
    • (1952) J. Biol. Chem. , vol.196 , pp. 853-862
    • Entner, N.1    Doudoroff, M.2
  • 18
    • 84862171231 scopus 로고    scopus 로고
    • The metabolic blueprint of Phaeodactylum tricornutum reveals a eukaryotic Entner-Doudoroff glycolytic pathway
    • Fabris M., Matthijs M., Rombauts S., Vyverman W., Goossens A., Baart G.J.E. The metabolic blueprint of Phaeodactylum tricornutum reveals a eukaryotic Entner-Doudoroff glycolytic pathway. Plant J. 2012, 70:1004-1014.
    • (2012) Plant J. , vol.70 , pp. 1004-1014
    • Fabris, M.1    Matthijs, M.2    Rombauts, S.3    Vyverman, W.4    Goossens, A.5    Baart, G.J.E.6
  • 21
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • Flint D.H., Allen R.M. Iron-sulfur proteins with nonredox functions. Chem. Rev. 1996, 96:2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 23
    • 14244256095 scopus 로고    scopus 로고
    • Experimental identification and quantification of glucose metabolism in seven bacterial species
    • Fuhrer T., Fischer E., Sauer U. Experimental identification and quantification of glucose metabolism in seven bacterial species. J. Bacteriol. 2005, 187:1581-1590.
    • (2005) J. Bacteriol. , vol.187 , pp. 1581-1590
    • Fuhrer, T.1    Fischer, E.2    Sauer, U.3
  • 24
    • 0032519423 scopus 로고    scopus 로고
    • Rapid accumulation of intracellular 2-keto-3-deoxy-6-phosphogluconate in an Entner-Doudoroff aldolase mutant results in bacteriostasis
    • Fuhrman L.K., Wanken A., Nickerson K.W., Conway T. Rapid accumulation of intracellular 2-keto-3-deoxy-6-phosphogluconate in an Entner-Doudoroff aldolase mutant results in bacteriostasis. FEMS Microbiol. Lett. 1998, 159:261-266.
    • (1998) FEMS Microbiol. Lett. , vol.159 , pp. 261-266
    • Fuhrman, L.K.1    Wanken, A.2    Nickerson, K.W.3    Conway, T.4
  • 25
    • 0026011632 scopus 로고
    • Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
    • Gardner P.R., Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. J. Biol. Chem. 1991, 266:1478-1483.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1478-1483
    • Gardner, P.R.1    Fridovich, I.2
  • 26
    • 34347260322 scopus 로고    scopus 로고
    • Frozen competent yeast cells that can be transformed with high efficiency using the LiAc/SS carrier DNA/PEG method
    • Gietz R.D., Schiestl R.H. Frozen competent yeast cells that can be transformed with high efficiency using the LiAc/SS carrier DNA/PEG method. Nat. Protoc. 2007, 2:1-4.
    • (2007) Nat. Protoc. , vol.2 , pp. 1-4
    • Gietz, R.D.1    Schiestl, R.H.2
  • 27
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz R.D., Woods R.A. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 2002, 350:87-96.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 30
    • 0036738179 scopus 로고    scopus 로고
    • Characterization of the xylose-transporting properties of yeast hexose transporters and their influence on xylose utilization
    • Hamacher T., Becker J., Gárdonyi M., Hahn-Hägerdal B., Boles E. Characterization of the xylose-transporting properties of yeast hexose transporters and their influence on xylose utilization. Microbiology 2002, 148:2783-2788.
    • (2002) Microbiology , vol.148 , pp. 2783-2788
    • Hamacher, T.1    Becker, J.2    Gárdonyi, M.3    Hahn-Hägerdal, B.4    Boles, E.5
  • 31
    • 38849180187 scopus 로고    scopus 로고
    • Glucose utilization of strains lacking PGI1 and expressing a transhydrogenase suggests differences in the pentose phosphate capacity among Saccharomyces cerevisiae strains
    • Heux S., Cadiere A., Dequin S. Glucose utilization of strains lacking PGI1 and expressing a transhydrogenase suggests differences in the pentose phosphate capacity among Saccharomyces cerevisiae strains. FEMS Yeast Res. 2008, 8:217-224.
    • (2008) FEMS Yeast Res. , vol.8 , pp. 217-224
    • Heux, S.1    Cadiere, A.2    Dequin, S.3
  • 33
    • 84858983547 scopus 로고    scopus 로고
    • KEGG for integration and interpretation of large-scale molecular data sets
    • Kanehisa M., Goto S., Sato Y., Furumichi M., Tanabe M. KEGG for integration and interpretation of large-scale molecular data sets. Nucleic Acids Res. 2012, 40:D109-D114.
    • (2012) Nucleic Acids Res. , vol.40
    • Kanehisa, M.1    Goto, S.2    Sato, Y.3    Furumichi, M.4    Tanabe, M.5
  • 34
    • 33646356744 scopus 로고    scopus 로고
    • Catalytic promiscuity in dihydroxy-acid dehydratase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Kim S., Lee S.B. Catalytic promiscuity in dihydroxy-acid dehydratase from the thermoacidophilic archaeon Sulfolobus solfataricus. J. Biochem. 2006, 139:591-596.
    • (2006) J. Biochem. , vol.139 , pp. 591-596
    • Kim, S.1    Lee, S.B.2
  • 35
    • 0024198152 scopus 로고
    • Isopropylmalate dehydratase from yeast
    • Kohlhaw G.B. Isopropylmalate dehydratase from yeast. Methods Enzymol. 1988, 166:423-429.
    • (1988) Methods Enzymol. , vol.166 , pp. 423-429
    • Kohlhaw, G.B.1
  • 36
    • 84890904525 scopus 로고    scopus 로고
    • DNA encoding enzymes of the glycolytic pathway for use in alcohol producing yeast. US Patent Number 5,786,186.
    • Lancashire, W., Dickinson, J., Malloch, R., 1998. DNA encoding enzymes of the glycolytic pathway for use in alcohol producing yeast. US Patent Number 5,786,186.
    • (1998)
    • Lancashire, W.1    Dickinson, J.2    Malloch, R.3
  • 37
    • 77952683487 scopus 로고    scopus 로고
    • Comparing the fermentation performance of Escherichia coli KO11, Saccharomyces cerevisiae 424A(LNH-ST) and Zymomonas mobilis AX101 for cellulosic ethanol production
    • Lau M.W., Gunawan C., Balan V., Dale B.E. Comparing the fermentation performance of Escherichia coli KO11, Saccharomyces cerevisiae 424A(LNH-ST) and Zymomonas mobilis AX101 for cellulosic ethanol production. Biotechnol. Biofuels 2010, 3:11.
    • (2010) Biotechnol. Biofuels , vol.3 , pp. 11
    • Lau, M.W.1    Gunawan, C.2    Balan, V.3    Dale, B.E.4
  • 38
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Mühlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 2008, 77:669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 39
    • 0020535447 scopus 로고
    • Phosphofructokinase mutants of yeast. Biochemistry and genetics
    • Lobo Z., Maitra P.K. Phosphofructokinase mutants of yeast. Biochemistry and genetics. J. Biol. Chem. 1983, 258:1444-1449.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1444-1449
    • Lobo, Z.1    Maitra, P.K.2
  • 40
    • 0015125608 scopus 로고
    • Glucose and fructose metabolism in a phosphoglucoisomeraseless mutant of Saccharomyces cerevisiae
    • Maitra P.K. Glucose and fructose metabolism in a phosphoglucoisomeraseless mutant of Saccharomyces cerevisiae. J. Bacteriol. 1971, 107:759-769.
    • (1971) J. Bacteriol. , vol.107 , pp. 759-769
    • Maitra, P.K.1
  • 41
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria
    • Mühlenhoff U., Lill R. Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim. Biophys. Acta 2000, 1459:370-382.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 370-382
    • Mühlenhoff, U.1    Lill, R.2
  • 42
    • 0345346377 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year 2000
    • Nakamura Y., Gojobori T., Ikemura T. Codon usage tabulated from international DNA sequence databases: status for the year 2000. Nucleic Acids Res. 2000, 28:292.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 43
    • 0027453012 scopus 로고
    • Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth on glucose
    • Navas M.A., Cerdán S., Gancedo J.M. Futile cycles in Saccharomyces cerevisiae strains expressing the gluconeogenic enzymes during growth on glucose. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:1290-1294.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1290-1294
    • Navas, M.A.1    Cerdán, S.2    Gancedo, J.M.3
  • 44
    • 84857465383 scopus 로고    scopus 로고
    • Induction of biogenic magnetization and redox control by a component of the target of rapamycin complex 1 signaling pathway
    • Nishida K., Silver P.A. Induction of biogenic magnetization and redox control by a component of the target of rapamycin complex 1 signaling pathway. PLoS Biol. 2012, 10:e1001269.
    • (2012) PLoS Biol. , vol.10
    • Nishida, K.1    Silver, P.A.2
  • 45
    • 0030873221 scopus 로고    scopus 로고
    • Recombination-mediated PCR-directed plasmid construction in vivo in yeast
    • Oldenburg K.R., Vo K.T., Michaelis S., Paddon C. Recombination-mediated PCR-directed plasmid construction in vivo in yeast. Nucleic Acids Res. 1997, 25:451-452.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 451-452
    • Oldenburg, K.R.1    Vo, K.T.2    Michaelis, S.3    Paddon, C.4
  • 46
    • 84888133282 scopus 로고    scopus 로고
    • Iron sensing and regulation in Saccharomyces cerevisiae: ironing out the mechanistic details
    • Outten C.E., Albetel A.-N. Iron sensing and regulation in Saccharomyces cerevisiae: ironing out the mechanistic details. Curr. Opin. Microbiol. 2013, 16:662-668.
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 662-668
    • Outten, C.E.1    Albetel, A.-N.2
  • 47
    • 84871676943 scopus 로고    scopus 로고
    • Reconstruction and evaluation of the synthetic bacterial MEP pathway in Saccharomyces cerevisiae
    • Partow S., Siewers V., Daviet L., Schalk M., Nielsen J. Reconstruction and evaluation of the synthetic bacterial MEP pathway in Saccharomyces cerevisiae. PLoS ONE 2012, 7:e52498.
    • (2012) PLoS ONE , vol.7
    • Partow, S.1    Siewers, V.2    Daviet, L.3    Schalk, M.4    Nielsen, J.5
  • 48
    • 77649235073 scopus 로고    scopus 로고
    • Bio-butanol vs. bio-ethanol: a technical and economic assessment for corn and switchgrass fermented by yeast or Clostridium acetobutylicum
    • Pfromm P.H., Amanor-Boadu V., Nelson R., Vadlani P., Madl R. Bio-butanol vs. bio-ethanol: a technical and economic assessment for corn and switchgrass fermented by yeast or Clostridium acetobutylicum. Biomass Bioenergy 2010, 34:515-524.
    • (2010) Biomass Bioenergy , vol.34 , pp. 515-524
    • Pfromm, P.H.1    Amanor-Boadu, V.2    Nelson, R.3    Vadlani, P.4    Madl, R.5
  • 49
    • 40649120516 scopus 로고    scopus 로고
    • Response to iron deprivation in Saccharomyces cerevisiae
    • Philpott C.C., Protchenko O. Response to iron deprivation in Saccharomyces cerevisiae. Eukaryot. Cell 2008, 7:20-27.
    • (2008) Eukaryot. Cell , vol.7 , pp. 20-27
    • Philpott, C.C.1    Protchenko, O.2
  • 50
    • 53149111160 scopus 로고    scopus 로고
    • CAIcal: a combined set of tools to assess codon usage adaptation
    • Puigbo P., Bravo I., Garcia-Vallve S. CAIcal: a combined set of tools to assess codon usage adaptation. Biol. Direct 2008, 3:38.
    • (2008) Biol. Direct , vol.3 , pp. 38
    • Puigbo, P.1    Bravo, I.2    Garcia-Vallve, S.3
  • 51
    • 0042847393 scopus 로고    scopus 로고
    • Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements
    • Rutherford J.C., Jaron S., Winge D.R. Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements. J. Biol. Chem. 2003, 278:27636-27643.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27636-27643
    • Rutherford, J.C.1    Jaron, S.2    Winge, D.R.3
  • 53
    • 33745654761 scopus 로고    scopus 로고
    • Microbial aldolases as CC bonding enzymes-unknown treasures and new developments
    • Samland A.K., Sprenger G.A. Microbial aldolases as CC bonding enzymes-unknown treasures and new developments. Appl. Microbiol. Biotechnol. 2006, 71:253-264.
    • (2006) Appl. Microbiol. Biotechnol. , vol.71 , pp. 253-264
    • Samland, A.K.1    Sprenger, G.A.2
  • 54
    • 0023352241 scopus 로고
    • Functional expression of the cre-lox site-specific recombination system in the yeast Saccharomyces cerevisiae
    • Sauer B. Functional expression of the cre-lox site-specific recombination system in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 1987, 7:2087-2096.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2087-2096
    • Sauer, B.1
  • 55
    • 0025349493 scopus 로고
    • Molecular analysis of the structural gene for yeast transaldolase
    • Schaaff I., Hohmann S., Zimmermann F.K. Molecular analysis of the structural gene for yeast transaldolase. Eur. J. Biochem. 1990, 188:597-603.
    • (1990) Eur. J. Biochem. , vol.188 , pp. 597-603
    • Schaaff, I.1    Hohmann, S.2    Zimmermann, F.K.3
  • 56
    • 0026782586 scopus 로고
    • Induction of specific enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone in Saccharomyces cerevisiae
    • Sinha A., Maitra P.K. Induction of specific enzymes of the oxidative pentose phosphate pathway by glucono-delta-lactone in Saccharomyces cerevisiae. J. Gen. Microbiol. 1992, 138:1865-1873.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1865-1873
    • Sinha, A.1    Maitra, P.K.2
  • 57
    • 0007522911 scopus 로고
    • Carbohydrate metabolism in Rhodopseudomonas sphreoides
    • Szymona M., Doudoroff M. Carbohydrate metabolism in Rhodopseudomonas sphreoides. J. Gen. Microbiol. 1960, 22:167-183.
    • (1960) J. Gen. Microbiol. , vol.22 , pp. 167-183
    • Szymona, M.1    Doudoroff, M.2
  • 58
    • 0022507007 scopus 로고
    • Redox balances in the metabolism of sugars by yeasts
    • van Dijken J.P., Scheffers W.A. Redox balances in the metabolism of sugars by yeasts. FEMS Microbiol. Lett. 1986, 32:199-224.
    • (1986) FEMS Microbiol. Lett. , vol.32 , pp. 199-224
    • van Dijken, J.P.1    Scheffers, W.A.2
  • 59
    • 0020338406 scopus 로고
    • The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA
    • Viebrock A., Perz A., Sebald W. The imported preprotein of the proteolipid subunit of the mitochondrial ATP synthase from Neurospora crassa. Molecular cloning and sequencing of the mRNA. EMBO J. 1982, 1:565-571.
    • (1982) EMBO J. , vol.1 , pp. 565-571
    • Viebrock, A.1    Perz, A.2    Sebald, W.3
  • 62
    • 0027227437 scopus 로고
    • Energetics and kinetics of maltose transport in Saccharomyces cerevisiae: a continuous culture study
    • Weusthuis R.A., Adams H., Scheffers W.A., van Dijken J.P. Energetics and kinetics of maltose transport in Saccharomyces cerevisiae: a continuous culture study. Appl. Environ. Microbiol. 1993, 59:3102-3109.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3102-3109
    • Weusthuis, R.A.1    Adams, H.2    Scheffers, W.A.3    van Dijken, J.P.4
  • 63
    • 0028961739 scopus 로고
    • AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae
    • Yamaguchi-Iwai Y., Dancis A., Klausner R.D. AFT1: a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae. EMBO J. 1995, 14:1231-1239.
    • (1995) EMBO J. , vol.14 , pp. 1231-1239
    • Yamaguchi-Iwai, Y.1    Dancis, A.2    Klausner, R.D.3
  • 64
    • 0016605653 scopus 로고
    • Procedures used in the induction of mitotic recombination and mutation in the yeast Saccharomyces cerevisiae
    • Zimmermann F.K. Procedures used in the induction of mitotic recombination and mutation in the yeast Saccharomyces cerevisiae. Mutat. Res. 1975, 31:71-86.
    • (1975) Mutat. Res. , vol.31 , pp. 71-86
    • Zimmermann, F.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.