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Volumn 87, Issue 1, 1999, Pages 28-36

Effect of gene disruptions of the TCA cycle on production of succinic acid in Saccharomyces cerevisiae

Author keywords

Aconitase; Fumarase; Fumarate reductase; Gene disruption; Isocitrate lyase; Organic acid; Saccharomyces cerevisiae; Sake; Succinate dehydrogenase; ketoglutarate dehydrogenase

Indexed keywords

BIOSYNTHESIS; ENZYMES; FERMENTATION; GLUCOSE; ORGANIC ACIDS; PLANT CELL CULTURE; WINE; YEAST;

EID: 0032952709     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(99)80004-8     Document Type: Article
Times cited : (92)

References (30)
  • 1
    • 0001375189 scopus 로고
    • Studies on utilization rate of raw materials on sake-making industry (part 9)
    • 1. Tomizawa, M., Yonezaki, H., Ueda, R., and Hayashida, M.: Studies on utilization rate of raw materials on sake-making industry (part 9). Hakkokogaku, 38, 342-350 (1960).
    • (1960) Hakkokogaku , vol.38 , pp. 342-350
    • Tomizawa, M.1    Yonezaki, H.2    Ueda, R.3    Hayashida, M.4
  • 2
    • 0000024938 scopus 로고
    • Formation of succinate during fermentation of sake mash and grape must
    • 2. Wakai, Y., Shimazaki, T., and Hara, S.: Formation of succinate during fermentation of sake mash and grape must. Hakkokogaku, 58, 363-368 (1980).
    • (1980) Hakkokogaku , vol.58 , pp. 363-368
    • Wakai, Y.1    Shimazaki, T.2    Hara, S.3
  • 3
    • 0028827364 scopus 로고
    • Effect of yeast fumarase gene (FUM1) disruption on production of malic, fumaric and succinic acids in sake mash
    • 3. Magarifuchi, T., Goto, K., Iimura, Y., Tadenuma, M., and Tamura, G.: Effect of yeast fumarase gene (FUM1) disruption on production of malic, fumaric and succinic acids in sake mash. J. Ferment. Bioeng., 80, 355-361 (1995).
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 355-361
    • Magarifuchi, T.1    Goto, K.2    Iimura, Y.3    Tadenuma, M.4    Tamura, G.5
  • 4
    • 0023645433 scopus 로고
    • Mitochondrial and cytoplasmic fumarase in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1
    • 4. Wu, M. and Tzagoloff, A.: Mitochondrial and cytoplasmic fumarase in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1. J. Biol. Chem., 262, 12275-12282 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 12275-12282
    • Wu, M.1    Tzagoloff, A.2
  • 5
    • 0001383845 scopus 로고
    • Mitochondrial and cytoplasmic enzymes for the reduction of fumarate to succinate in yeast
    • 5. Rossi, C., Hauber, J., and Singer, T. P.: Mitochondrial and cytoplasmic enzymes for the reduction of fumarate to succinate in yeast. Nature, 204, 167-170 (1964) .
    • (1964) Nature , vol.204 , pp. 167-170
    • Rossi, C.1    Hauber, J.2    Singer, T.P.3
  • 6
    • 0000092520 scopus 로고
    • Purification and properties of fumarate reductase from baker's yeast
    • 6. Muratsubaki, H. and Katsume, T.: Purification and properties of fumarate reductase from baker's yeast. Agric. Biol. Chem., 46, 2909-2917 (1982).
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2909-2917
    • Muratsubaki, H.1    Katsume, T.2
  • 7
    • 0030608184 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae
    • 7. Enomoto, K., Ohki, R., and Muratsubaki, H.: Cloning and sequencing of the gene encoding the soluble fumarate reductase from Saccharomyces cerevisiae. DNA Res., 3, 263-267 (1996) .
    • (1996) DNA Res. , vol.3 , pp. 263-267
    • Enomoto, K.1    Ohki, R.2    Muratsubaki, H.3
  • 8
    • 0014441132 scopus 로고
    • Promitochondria of anaerobically grown yeast: I. Isolation and biochemical properties
    • 8. Criddle, R. S. and Schatz, G.: Promitochondria of anaerobically grown yeast: I. Isolation and biochemical properties. Biochemistry, 8, 322-334 (1969).
    • (1969) Biochemistry , vol.8 , pp. 322-334
    • Criddle, R.S.1    Schatz, G.2
  • 9
    • 0032522152 scopus 로고    scopus 로고
    • One of the fumarate reductase isoenzymes from Saccharomyces cerevisiae is encoded by the OSMI gene
    • 9. Muratsubaki, H. and Enomoto, K.: One of the fumarate reductase isoenzymes from Saccharomyces cerevisiae is encoded by the OSMI gene. Arch. Biochem. Biophys., 352, 175-181 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 175-181
    • Muratsubaki, H.1    Enomoto, K.2
  • 10
    • 0032145406 scopus 로고    scopus 로고
    • Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth
    • 10. Arikawa, Y., Enomoto, K., Muratubaki, H., and Okazaki, M.: Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth. FEMS Micobiol. Lett., 165, 111-116 (1998).
    • (1998) FEMS Micobiol. Lett. , vol.165 , pp. 111-116
    • Arikawa, Y.1    Enomoto, K.2    Muratubaki, H.3    Okazaki, M.4
  • 11
    • 0025336743 scopus 로고
    • Molecular cloning of the yeast mitochondrial aconitase gene (ACOI) and evidence of a synergistic regulation of expression by glucose plus glutamate
    • 11. Gangloff, S.P., Marguet, D., and Lauquin, G. J.-M.: Molecular cloning of the yeast mitochondrial aconitase gene (ACOI) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol., 10, 3551-3561 (1990).
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3551-3561
    • Gangloff, S.P.1    Marguet, D.2    Lauquin, G.J.-M.3
  • 12
    • 0024677063 scopus 로고
    • Structure and regulation of KGD1, the structural gene for yeast α-ketoglutarate dehydrogenase
    • 12. Repetto, B. and Tzagoloff, A.: Structure and regulation of KGD1, the structural gene for yeast α-ketoglutarate dehydrogenase. Mol. Cell. Biol., 9, 2695-2705 (1989).
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2695-2705
    • Repetto, B.1    Tzagoloff, A.2
  • 13
    • 0026714724 scopus 로고
    • SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunits from Saccharomyces cerevisiae
    • 13. Chapman, K. B., Solomon, S. D., and Boeke, J. D.: SDH1, the gene encoding the succinate dehydrogenase flavoprotein subunits from Saccharomyces cerevisiae. Gene, 118, 131-136 (1992).
    • (1992) Gene , vol.118 , pp. 131-136
    • Chapman, K.B.1    Solomon, S.D.2    Boeke, J.D.3
  • 14
    • 0026522337 scopus 로고
    • The ICL1 gene from Saccharomyces cerevisiae
    • 14. Fernandez, E., Moreno, F., and Rodicio, R.: The ICL1 gene from Saccharomyces cerevisiae. Eur. J. Biochem., 204, 983-990 (1992).
    • (1992) Eur. J. Biochem. , vol.204 , pp. 983-990
    • Fernandez, E.1    Moreno, F.2    Rodicio, R.3
  • 15
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • 15. Vieira, J. and Messing, J.: Production of single-stranded plasmid DNA. Methods Enzymol., 153, 3-11 (1987).
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 16
    • 0026663543 scopus 로고
    • DNA cassettes containing the origin of transfer (oriT) of two broad-host-range transfer systems
    • 16. Hengen, P. N. and Iyer, V. N.: DNA cassettes containing the origin of transfer (oriT) of two broad-host-range transfer systems. BioTechniques, 13, 60-62 (1992).
    • (1992) BioTechniques , vol.13 , pp. 60-62
    • Hengen, P.N.1    Iyer, V.N.2
  • 17
    • 0002595158 scopus 로고
    • Molecular breeding of yeast producing a large amount of β-phenetyl-alcohol
    • 17. Arikawa, Y., Fujita, A., Baba, S., and Oguri, I.: Molecular breeding of yeast producing a large amount of β-phenetyl-alcohol. Seibutsu-kogaku, 72, 95-100 (1994).
    • (1994) Seibutsu-kogaku , vol.72 , pp. 95-100
    • Arikawa, Y.1    Fujita, A.2    Baba, S.3    Oguri, I.4
  • 18
    • 0023429343 scopus 로고
    • Regulation of reductive production of succinate under anaerobic conditions in baker's yeast
    • 18. Muratubakí, H.: Regulation of reductive production of succinate under anaerobic conditions in baker's yeast. J. Biochem., 102, 705-714 (1987).
    • (1987) J. Biochem. , vol.102 , pp. 705-714
    • Muratubakí, H.1
  • 20
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • 20. Hanahan, D.: Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol., 166, 557-580 (1983).
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 21
    • 0020529962 scopus 로고
    • Trasformation of intact yeast cells treated with alkali cations
    • 21. Ito, H., Fukuda, Y., Murata, K., and Kimura, A.: Trasformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168 (1983).
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 22
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • 22. Rothstein, R.J.: One-step gene disruption in yeast. Methods Enzymol., 101, 202-211 (1983).
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 24
    • 77956995420 scopus 로고
    • α-Ketoglutarate dehydrogenase complex from Escherichia coli
    • 24. Reed, L. J. and Mukherjee, B. B.: α-Ketoglutarate dehydrogenase complex from Escherichia coli. Methods Enzymol., 13, 55-61 (1969).
    • (1969) Methods Enzymol. , vol.13 , pp. 55-61
    • Reed, L.J.1    Mukherjee, B.B.2
  • 25
    • 0001904522 scopus 로고
    • Assay methods for key enzymes of the glyoxylate cycle
    • 25. Dixon, G. H. and Kornberg, H. L.: Assay methods for key enzymes of the glyoxylate cycle. Biochem. J., 72, 3 (1959).
    • (1959) Biochem. J. , vol.72 , pp. 3
    • Dixon, G.H.1    Kornberg, H.L.2
  • 26
    • 77956987911 scopus 로고
    • Preparation of succinate dehydrogenase and reconstitution of succinate oxidase
    • 26. King, T. E.: Preparation of succinate dehydrogenase and reconstitution of succinate oxidase. Methods Enzymol., 10, 322-331 (1967).
    • (1967) Methods Enzymol. , vol.10 , pp. 322-331
    • King, T.E.1
  • 27
    • 0000862805 scopus 로고
    • The preparation and characterization of fumarase from swin heart muscle
    • 27. Kanarek, L. and Hill, R. L.: The preparation and characterization of fumarase from swin heart muscle. J. Biol. Chem., 239, 4202-4206 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 4202-4206
    • Kanarek, L.1    Hill, R.L.2
  • 28
  • 29
    • 0013773214 scopus 로고
    • Glutamate auxotrophs in Saccharomyces, I. The biochemical lesion in the glt-1 mutants
    • 29. Ogur, M., Coker, L., and Ogur, S.: Glutamate auxotrophs in Saccharomyces, I. The biochemical lesion in the glt-1 mutants. Biochem. Biophys. Res. Commun., 14, 193-197 (1964).
    • (1964) Biochem. Biophys. Res. Commun. , vol.14 , pp. 193-197
    • Ogur, M.1    Coker, L.2    Ogur, S.3
  • 30
    • 0014267745 scopus 로고
    • The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria
    • 30. Chapman, C. and Bartley, W.: The kinetics of enzyme changes in yeast under conditions that cause the loss of mitochondria. Biochem. J., 107, 455-465 (1968).
    • (1968) Biochem. J. , vol.107 , pp. 455-465
    • Chapman, C.1    Bartley, W.2


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