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Volumn 182, Issue 10, 2000, Pages 2823-2830

In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; GLYCEROPHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0034057725     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.10.2823-2830.2000     Document Type: Article
Times cited : (120)

References (39)
  • 1
    • 0029786406 scopus 로고    scopus 로고
    • Influence of the nitrogen source on Saccharomyces cerevisiae anaerobic growth and product formation
    • Albers, E., C. Larsson, G. Lidén, C. Niklasson, and L. Gustafsson. 1996. Influence of the nitrogen source on Saccharomyces cerevisiae anaerobic growth and product formation. Appl. Environ. Microhiol. 62:3187-3195.
    • (1996) Appl. Environ. Microhiol. , vol.62 , pp. 3187-3195
    • Albers, E.1    Larsson, C.2    Lidén, G.3    Niklasson, C.4    Gustafsson, L.5
  • 3
    • 0001144466 scopus 로고
    • Hydrogen transport and transport metabolites
    • P. Karson (ed.), Springer-Verlag KG, Heidelberg, Germany
    • Borst, P. 1963. Hydrogen transport and transport metabolites, p. 137-162. In P. Karson (ed.), Funktionelle und morphologischen Organisation der Zelle. Springer-Verlag KG, Heidelberg, Germany.
    • (1963) Funktionelle und Morphologischen Organisation der Zelle , pp. 137-162
    • Borst, P.1
  • 4
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • Chance, B., and G. R. Williams. 1956. The respiratory chain and oxidative phosphorylation. Adv. Enzymol. 17:65-134.
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.R.2
  • 5
    • 0018399737 scopus 로고
    • Oxidation of cytosolic NADH formed during aerobic metabolism in mammalian cells
    • Dawson, A. G. 1979. Oxidation of cytosolic NADH formed during aerobic metabolism in mammalian cells. Trends Biochem. Sci. 4:171-176.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 171-176
    • Dawson, A.G.1
  • 7
    • 0023561970 scopus 로고
    • The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism
    • de Vries, S., and C. A. Marres. 1987. The mitochondrial respiratory chain of yeast. Structure and biosynthesis and the role in cellular metabolism. Biochim. Biophys. Acta 895:205-239.
    • (1987) Biochim. Biophys. Acta , vol.895 , pp. 205-239
    • De Vries, S.1    Marres, C.A.2
  • 8
    • 0026504047 scopus 로고
    • Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
    • de Vries, S., R. van Witzenburg, L. A. Grivell, and C. A. Marres. 1992. Primary structure and import pathway of the rotenone-insensitive NADH-ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur. J. Biochem. 203:587-592.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 587-592
    • De Vries, S.1    Van Witzenburg, R.2    Grivell, L.A.3    Marres, C.A.4
  • 10
    • 84965086439 scopus 로고
    • Fermentation processes leading to glycerol. I. The influence of certain variables on glycerol formation in the presence of sulfites
    • Freeman, G. G., and G. M. S. Donald. 1957. Fermentation processes leading to glycerol. I. The influence of certain variables on glycerol formation in the presence of sulfites. Appl. Microbiol. 5:197-210.
    • (1957) Appl. Microbiol. , vol.5 , pp. 197-210
    • Freeman, G.G.1    Donald, G.M.S.2
  • 11
    • 0031810672 scopus 로고    scopus 로고
    • Yeast carbon cataholite repression
    • Gancedo, J. M. 1998. Yeast carbon cataholite repression. Microbiol. Mol. Biol. Rev. 62:334-361.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 334-361
    • Gancedo, J.M.1
  • 12
  • 13
    • 0014964294 scopus 로고
    • The glutamate dehydrogenases of yeast: Extra-mitochondrial enzymes
    • Hollenberg, C. P., W. F. Riks, and P. Borst. 1970. The glutamate dehydrogenases of yeast: extra-mitochondrial enzymes. Biochim. Biophys. Acta 201: 13-19.
    • (1970) Biochim. Biophys. Acta , vol.201 , pp. 13-19
    • Hollenberg, C.P.1    Riks, W.F.2    Borst, P.3
  • 14
    • 0025964378 scopus 로고
    • Respiration of pea leaf mitochondria and redox transfer between the mitochondrial and extramitochondrial compartment
    • Krömer, S., and H. W. Heldt. 1991. Respiration of pea leaf mitochondria and redox transfer between the mitochondrial and extramitochondrial compartment. Biochim. Biophys. Acta 1057:42-50.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 42-50
    • Krömer, S.1    Heldt, H.W.2
  • 15
    • 0022946405 scopus 로고
    • Misconceptions about the energy metabolism of Saccharomyces cerevisiae
    • Lagunas, R. 1986. Misconceptions about the energy metabolism of Saccharomyces cerevisiae. Yeast 2:221-228.
    • (1986) Yeast , vol.2 , pp. 221-228
    • Lagunas, R.1
  • 16
    • 2642671097 scopus 로고    scopus 로고
    • The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae
    • Larsson, C., I. L. Påhlman, R. Ansell, M. Rigoulet, L. Adler, and L. Gustafsson. 1998. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 14:347-357.
    • (1998) Yeast , vol.14 , pp. 347-357
    • Larsson, C.1    Påhlman, I.L.2    Ansell, R.3    Rigoulet, M.4    Adler, L.5    Gustafsson, L.6
  • 17
    • 15644371838 scopus 로고    scopus 로고
    • The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane
    • Lee, A. C., X. Xu, E. Blachly-Dyson, M. Forte, and M. Colombini. 1998. The role of yeast VDAC genes on the permeability of the mitochondrial outer membrane. J. Membr. Biol. 161:173-181.
    • (1998) J. Membr. Biol. , vol.161 , pp. 173-181
    • Lee, A.C.1    Xu, X.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 19
    • 0032544505 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH
    • Luttik, M. A. H., K. M. Overkamp, P. Kötter, S. de Vries, J. P. van Dijken, and J. T. Pronk. 1998. The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J. Biol. Chem. 273:24529-24534.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24529-24534
    • Luttik, M.A.H.1    Overkamp, K.M.2    Kötter, P.3    De Vries, S.4    Van Dijken, J.P.5    Pronk, J.T.6
  • 20
    • 0026089901 scopus 로고
    • Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: Ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
    • Marres, C. A., S. de Vries, and L. A. Grivell. 1991. Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur. J. Biochem. 195:857-862.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 857-862
    • Marres, C.A.1    De Vries, S.2    Grivell, L.A.3
  • 21
    • 0027079917 scopus 로고
    • AATI, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae
    • Morin, P. J., G. S. Subramanian, and T. D. Gilmore. 1992. AATI, a gene encoding a mitochondrial aspartate aminotransferase in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1171:211-214.
    • (1992) Biochim. Biophys. Acta , vol.1171 , pp. 211-214
    • Morin, P.J.1    Subramanian, G.S.2    Gilmore, T.D.3
  • 22
    • 0015866720 scopus 로고
    • Mechanism of electron transport and energy conservation in the site I region of the respiratory chain
    • Ohnishi, T. 1973. Mechanism of electron transport and energy conservation in the site I region of the respiratory chain. Biochim. Biophys. Acta 301:105-128.
    • (1973) Biochim. Biophys. Acta , vol.301 , pp. 105-128
    • Ohnishi, T.1
  • 24
    • 0023004947 scopus 로고
    • The apparent oxidation of NADH by whole cells of the methylotrophic bacterium Methylophilus methylothropus: A cautionary tale
    • Patchett, R. A., and C. W. Jones. 1986. The apparent oxidation of NADH by whole cells of the methylotrophic bacterium Methylophilus methylothropus: a cautionary tale. Antonie Leeuwenhoek 52:387-392.
    • (1986) Antonie Leeuwenhoek , vol.52 , pp. 387-392
    • Patchett, R.A.1    Jones, C.W.2
  • 25
    • 0020694191 scopus 로고
    • An expanded concept for the glucose effect in the yeast Saccharomyces cerevisiae: Involvement of short-and long-term regulation
    • Petrik, M., O. Käppeli, and A. Fiechter. 1983. An expanded concept for the glucose effect in the yeast Saccharomyces cerevisiae: involvement of short-and long-term regulation. J. Gen. Microbiol. 129:43-49.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 43-49
    • Petrik, M.1    Käppeli, O.2    Fiechter, A.3
  • 26
    • 0024615221 scopus 로고
    • Enzymic analysis of the Crabtree effect in glucose-limited chemostat cultures of Saccharomyces cerevisiae
    • Postma, E., C. Verduyn, W. A. Scheffers, and J. P. van Dijken. 1989. Enzymic analysis of the Crabtree effect in glucose-limited chemostat cultures of Saccharomyces cerevisiae. Appl. Environ. Microbiol. 55:468-477.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 468-477
    • Postma, E.1    Verduyn, C.2    Scheffers, W.A.3    Van Dijken, J.P.4
  • 28
    • 0027501168 scopus 로고
    • Yeast sequencing reports. IX. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae
    • Rønnow, B., and M. C. Kielland-Brandt. 1993. Yeast sequencing reports. IX. GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Yeast 9:1121-1130.
    • (1993) Yeast , vol.9 , pp. 1121-1130
    • Rønnow, B.1    Kielland-Brandt, M.C.2
  • 29
    • 0031878085 scopus 로고    scopus 로고
    • Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae
    • Small, W. C., and L. McAlister-Henn. 1998. Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J. Bacteriol. 180:4051-4055.
    • (1998) J. Bacteriol. , vol.180 , pp. 4051-4055
    • Small, W.C.1    McAlister-Henn, L.2
  • 30
    • 0022507007 scopus 로고
    • Redox balances in the metabolism of sugars by yeast
    • van Dijken, J. P., and W. A. Scheffers. 1986. Redox balances in the metabolism of sugars by yeast. FEMS Microbiol. Rev. 32:199-224.
    • (1986) FEMS Microbiol. Rev. , vol.32 , pp. 199-224
    • Van Dijken, J.P.1    Scheffers, W.A.2
  • 31
    • 0031746509 scopus 로고    scopus 로고
    • Effects of pyruvate decarboxylase over-production on flux distribution at the pyruvate branch point in Saccharomyces cerevisiae
    • van Hoek, P., M. T. Flikweert, Q. J. M. van der Aart, H. Y. Steensma, J. P. van Dijken, and J. T. Pronk. 1998. Effects of pyruvate decarboxylase over-production on flux distribution at the pyruvate branch point in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 64:2133-2140.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2133-2140
    • Van Hoek, P.1    Flikweert, M.T.2    Van Der Aart, Q.J.M.3    Steensma, H.Y.4    Van Dijken, J.P.5    Pronk, J.T.6
  • 32
    • 0025318231 scopus 로고
    • Physiology of Saccharomyces cerivisiae in anaerobic glucose-limited chemostat cultures
    • Verduyn, C., E. Postma, W. A. Scheffers, and J. P. van Dijken. 1990. Physiology of Saccharomyces cerivisiae in anaerobic glucose-limited chemostat cultures. J. Gen. Microbiol. 136:395-403.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 395-403
    • Verduyn, C.1    Postma, E.2    Scheffers, W.A.3    Van Dijken, J.P.4
  • 33
    • 0026710123 scopus 로고
    • Effect of benzoic acid on metabolic fluxes in yeasts: A continuous culture study on the regulation of respiration and alcoholic fermentation
    • Verduyn, C., E. Postma, W. A. Scheffers, and J. P. van Dijken. 1992. Effect of benzoic acid on metabolic fluxes in yeasts: a continuous culture study on the regulation of respiration and alcoholic fermentation. Yeast 8:501-517.
    • (1992) Yeast , vol.8 , pp. 501-517
    • Verduyn, C.1    Postma, E.2    Scheffers, W.A.3    Van Dijken, J.P.4
  • 34
    • 0021220715 scopus 로고
    • Continuous measurement of ethanol production by aerobic yeast suspensions with an enzyme electrode
    • Verduyn, C., T. P. L. Zomerdijk, J. P. van Dijken, and W. A. Scheffers. 1984. Continuous measurement of ethanol production by aerobic yeast suspensions with an enzyme electrode. Appl. Microbiol. Biotechnol. 19:181-185.
    • (1984) Appl. Microbiol. Biotechnol. , vol.19 , pp. 181-185
    • Verduyn, C.1    Zomerdijk, T.P.L.2    Van Dijken, J.P.3    Scheffers, W.A.4
  • 35
    • 0014734642 scopus 로고
    • Pathways of hydrogen in mitochondria of Saccharomyces carlsbergensis
    • von Jagow, G., and M. Klingenberg. 1970. Pathways of hydrogen in mitochondria of Saccharomyces carlsbergensis. Eur. J. Biochem. 12:583-592.
    • (1970) Eur. J. Biochem. , vol.12 , pp. 583-592
    • Von Jagow, G.1    Klingenberg, M.2
  • 36
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Poehlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Poehlmann, R.3    Philippsen, P.4
  • 37
    • 0027227437 scopus 로고
    • Energetics and kinetics of maltose transport in Saccharomyces cerevisiae - A continuous-culture study
    • Weusthuis, R. A., H. Adams, W. A. Scheffers, and J. P. van Dijken. 1993. Energetics and kinetics of maltose transport in Saccharomyces cerevisiae - a continuous-culture study. Appl. Environ. Microbiol. 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
  • 39
    • 0021747597 scopus 로고
    • Effect of mutants and inhibitors on mitochondrial transport systems in vivo in yeast
    • Wills, C., P. Benhaim, and T. Martin. 1984. Effect of mutants and inhibitors on mitochondrial transport systems in vivo in yeast. Biochim. Biophys. Acta 778:57-66.
    • (1984) Biochim. Biophys. Acta , vol.778 , pp. 57-66
    • Wills, C.1    Benhaim, P.2    Martin, T.3


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