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Volumn 1709, Issue 2, 2005, Pages 181-190

The bacterial-like lactate shuttle components from heterotrophic Euglena gracilis

Author keywords

Energy metabolism; Membrane bound lactate dehydrogenase; Mitochondrion; NAD+ dependent lactate dehydrogenase

Indexed keywords

AMMONIA; DIPHENYLIODONIUM SALT; FLAVOPROTEIN; FRUCTOSE BISPHOSPHATASE; LACTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; POTASSIUM; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

EID: 24044453432     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2005.07.007     Document Type: Article
Times cited : (18)

References (47)
  • 1
    • 0018818947 scopus 로고
    • Bacterial lactate dehydrogenases
    • E.I. Garvie Bacterial lactate dehydrogenases Microbiol. Rev. 44 1980 106 139
    • (1980) Microbiol. Rev. , vol.44 , pp. 106-139
    • Garvie, E.I.1
  • 3
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • W.J. Ingledew, and R.K. Poole The respiratory chains of Escherichia coli Microbiol. Rev. 48 1984 222 271
    • (1984) Microbiol. Rev. , vol.48 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 4
    • 0020479807 scopus 로고
    • 2 and cytochrome c peroxidase are located in the intermembrane space of mitochondria
    • 2 and cytochrome c peroxidase are located in the intermembrane space of mitochondria J. Biol. Chem. 257 1982 13028 13033
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Ovni, P.C.2    Schatz, G.3
  • 5
    • 0015854555 scopus 로고
    • Membrane d-lactate dehydrogenase from Escherichia coli. Purification and properties
    • M. Futai Membrane d-lactate dehydrogenase from Escherichia coli. Purification and properties Biochemistry 12 1973 2468 2474
    • (1973) Biochemistry , vol.12 , pp. 2468-2474
    • Futai, M.1
  • 6
    • 0027210771 scopus 로고
    • Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme d-lactate ferricytochrome c oxidoreductase
    • T. Lodi, and Y. Ferrero Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme d-lactate ferricytochrome c oxidoreductase Mol. Gen. Genet. 238 1993 315 324
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 315-324
    • Lodi, T.1    Ferrero, Y.2
  • 7
    • 0003312430 scopus 로고
    • D- and l-lactic acid oxidase of E. coli
    • N. Haugaard d- and l-lactic acid oxidase of E. coli Biochim. Biophys. Acta 31 1968 66 72
    • (1968) Biochim. Biophys. Acta , vol.31 , pp. 66-72
    • Haugaard, N.1
  • 8
    • 0024121496 scopus 로고
    • Arc a (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways
    • S. Iuchi, and E.C.C. Lin arc A (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways Proc. Natl. Acad. Sci. U. S. A. 85 1988 1888 1892
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 1888-1892
    • Iuchi, S.1    Lin, E.C.C.2
  • 9
    • 0001648802 scopus 로고
    • Induction des lactico-cytochrome c reductase (d- et l-) de la leuvre aerobie par les (d- et l-)
    • M. Somlo Induction des lactico-cytochrome c reductase (d- et l-) de la leuvre aerobie par les (d- et l-) Biochim. Biophys. Acta 97 1965 183 201
    • (1965) Biochim. Biophys. Acta , vol.97 , pp. 183-201
    • Somlo, M.1
  • 10
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing enzymes
    • O. Dym, and D. Eisenberg Sequence-structure analysis of FAD-containing enzymes Protein Sci. 10 2001 1712 1728
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 12
    • 0035876053 scopus 로고    scopus 로고
    • The membrane-bound l- and d-lactate dehydrogenase activities in mitochondria from Euglena gracilis
    • R. Jasso-Chávez, M.E. Torres-Márquez, and R. Moreno-Sánchez The membrane-bound l- and d-lactate dehydrogenase activities in mitochondria from Euglena gracilis Arch. Biochem. Biophys. 390 2001 295 303
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 295-303
    • Jasso-Chávez, R.1    Torres-Márquez, M.E.2    Moreno-Sánchez, R.3
  • 13
    • 18244426772 scopus 로고    scopus 로고
    • Cytosol-mitochondria transfer of reducing equivalents by a lactate shuttle in heterotrophic Euglena
    • R. Jasso-Chávez, and R. Moreno-Sánchez Cytosol-mitochondria transfer of reducing equivalents by a lactate shuttle in heterotrophic Euglena Eur. J. Biochem. 270 2003 4942 4951
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4942-4951
    • Jasso-Chávez, R.1    Moreno-Sánchez, R.2
  • 14
    • 0001527861 scopus 로고
    • Preparation of coupled mitochondria from Euglena by sonication
    • R. Moreno-Sánchez, and J.C. Raya Preparation of coupled mitochondria from Euglena by sonication Plant Sci. 48 1987 151 157
    • (1987) Plant Sci. , vol.48 , pp. 151-157
    • Moreno-Sánchez, R.1    Raya, J.C.2
  • 15
  • 16
    • 0000853187 scopus 로고
    • The molar extinction coefficient of 2, 6-dichlorophenol indophenol
    • J.M. Armstrong The molar extinction coefficient of 2, 6-dichlorophenol indophenol Biochim. Biophys. Acta 86 1964 194 197
    • (1964) Biochim. Biophys. Acta , vol.86 , pp. 194-197
    • Armstrong, J.M.1
  • 17
    • 0036829501 scopus 로고    scopus 로고
    • Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride
    • S. Chakraborty, and V. Massey Reaction of reduced flavins and flavoproteins with diphenyliodonium chloride J. Biol. Chem. 277 2002 41507 41516
    • (2002) J. Biol. Chem. , vol.277 , pp. 41507-41516
    • Chakraborty, S.1    Massey, V.2
  • 18
    • 0017898228 scopus 로고
    • Affinity chromatography of bacterial lactate dehydrogenases
    • N. Kelly, M. Delaney, and P. ÓCarra Affinity chromatography of bacterial lactate dehydrogenases Biochem. J. 171 1978 543 547
    • (1978) Biochem. J. , vol.171 , pp. 543-547
    • Kelly, N.1    Delaney, M.2    Ócarra, P.3
  • 19
    • 0032945180 scopus 로고    scopus 로고
    • Purification and properties of NADH-dependent 5,10- Methylenetetrahydrofolate reductase (MetF) from Escherichia coli
    • C.A. Sheppard, E.E. Trimmer, and R.G. Matthews Purification and properties of NADH-dependent 5,10-Methylenetetrahydrofolate reductase (MetF) from Escherichia coli J. Bacteriol. 181 1999 718 725
    • (1999) J. Bacteriol. , vol.181 , pp. 718-725
    • Sheppard, C.A.1    Trimmer, E.E.2    Matthews, R.G.3
  • 20
    • 0022004306 scopus 로고
    • Membrane-bound lactate dehydrogenase and mandelate dehydrogenase of Acinetobacter calcoaceticus
    • N. Allison, M.J. ÓDonell, M.E. Hoey, and C.A. Fewson Membrane-bound lactate dehydrogenase and mandelate dehydrogenase of Acinetobacter calcoaceticus Biochem. J. 231 1985 407 416
    • (1985) Biochem. J. , vol.231 , pp. 407-416
    • Allison, N.1    Ódonell, M.J.2    Hoey, M.E.3    Fewson, C.A.4
  • 21
    • 0018798889 scopus 로고
    • Membrane-bound d-lactate dehydrogenase from Escherichia coli: Purification and properties
    • E.A. Pratt, L.W.-M. Fung, J.A. Flowers, and C. Ho Membrane-bound d-lactate dehydrogenase from Escherichia coli: purification and properties Biochemistry 18 1979 312 316
    • (1979) Biochemistry , vol.18 , pp. 312-316
    • Pratt, E.A.1    Fung, L.W.-M.2    Flowers, J.A.3    Ho, C.4
  • 22
    • 0033929687 scopus 로고    scopus 로고
    • Reduction of Cob (III)alamin to Cob (II)alamin in Salmonella enterica Serovar Typhimurium LT2
    • M.V. Fonseca, and J.C. Escalante-Semerena Reduction of Cob (III)alamin to Cob (II)alamin in Salmonella enterica Serovar Typhimurium LT2 J. Bacteriol. 182 2000 4304 4309
    • (2000) J. Bacteriol. , vol.182 , pp. 4304-4309
    • Fonseca, M.V.1    Escalante-Semerena, J.C.2
  • 23
    • 0027367411 scopus 로고
    • Oxidation of d-lactate and l-lactate by Neisseria meningitidis: Purification and cloning of meningococcal d-lactate dehydrogenase
    • A.L. Erwin, and E.C. Gotschlich Oxidation of d-lactate and l-lactate by Neisseria meningitidis: purification and cloning of meningococcal d-lactate dehydrogenase J. Bacteriol. 175 1993 6382 6391
    • (1993) J. Bacteriol. , vol.175 , pp. 6382-6391
    • Erwin, A.L.1    Gotschlich, E.C.2
  • 24
    • 0035936673 scopus 로고    scopus 로고
    • Determination of biologically active acid based on the electrochemical reduction of quinone in acetonitrile + water mixed solvent
    • J. Kim, T.D. Chung, and H. Kim Determination of biologically active acid based on the electrochemical reduction of quinone in acetonitrile + water mixed solvent J. Electroanal. Chem. 499 2001 78 84
    • (2001) J. Electroanal. Chem. , vol.499 , pp. 78-84
    • Kim, J.1    Chung, T.D.2    Kim, H.3
  • 25
    • 0001420328 scopus 로고
    • The mitochondrion
    • D.E. Buetow Academic Press New York
    • D.E. Buetow The mitochondrion D.E. Buetow The Biology of Euglena vol. IV 1989 Academic Press New York 247 314
    • (1989) The Biology of Euglena , vol.4 , pp. 247-314
    • Buetow, D.E.1
  • 27
    • 84897095977 scopus 로고
    • Enzymology of Euglena
    • D.E. Buetow Academic Press New York
    • R.M. Smillie Enzymology of Euglena D.E. Buetow The Biology of Euglena Vol. II 1968 Academic Press New York 2 54
    • (1968) The Biology of Euglena , vol.2 , pp. 2-54
    • Smillie, R.M.1
  • 28
    • 0017577897 scopus 로고
    • Comparative studies of lactate dehydrogenases in lactic acid bacteria: Amino-acid composition of an active-site region and chemical properties of the l-lactate dehydrogenase of Lactobacillus casei, Lactobacillus curvatus, Lactobacillus plantarum, and Lactobacillus acidophilus
    • R. Hensel, U. Mayr, K.O. Stetter, and O. Kandler Comparative studies of lactate dehydrogenases in lactic acid bacteria: amino-acid composition of an active-site region and chemical properties of the l-lactate dehydrogenase of Lactobacillus casei, Lactobacillus curvatus, Lactobacillus plantarum, and Lactobacillus acidophilus Arch. Microbiol. 112 1977 81 93
    • (1977) Arch. Microbiol. , vol.112 , pp. 81-93
    • Hensel, R.1    Mayr, U.2    Stetter, K.O.3    Kandler, O.4
  • 29
    • 0023145318 scopus 로고
    • Kinetics of activation of l-lactate dehydrogenase from Streptococcus faecalis by fructose 1, 6-bisphosphate and by metal ions
    • M.J. Hardman, and G.G. Pritchard Kinetics of activation of l-lactate dehydrogenase from Streptococcus faecalis by fructose 1, 6-bisphosphate and by metal ions Biochim. Biophys. Acta 912 1987 185 190
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 185-190
    • Hardman, M.J.1    Pritchard, G.G.2
  • 30
    • 0027402941 scopus 로고
    • Molecular basis of allosteric activation of bacterial l-lactate dehydrogenase
    • S. Iwata, and T. Ohta Molecular basis of allosteric activation of bacterial l-lactate dehydrogenase J. Mol. Biol. 230 1993 21 27
    • (1993) J. Mol. Biol. , vol.230 , pp. 21-27
    • Iwata, S.1    Ohta, T.2
  • 31
    • 0032579247 scopus 로고    scopus 로고
    • Homotropic activation via the subunit interaction and allosteric symmetry revealed on analysis of hybrid enzymes of l-lactate dehydrogenase
    • S. Fushinobu, K. Kamata, S. Iwata, H. Sakai, T. Ohta, and H. Matsuzawa Homotropic activation via the subunit interaction and allosteric symmetry revealed on analysis of hybrid enzymes of l-lactate dehydrogenase J. Biol. Chem. 273 1996 2971 2976
    • (1996) J. Biol. Chem. , vol.273 , pp. 2971-2976
    • Fushinobu, S.1    Kamata, K.2    Iwata, S.3    Sakai, H.4    Ohta, T.5    Matsuzawa, H.6
  • 32
    • 0030910904 scopus 로고    scopus 로고
    • Cloning, sequence, and expression of l-(+) lactate dehydrogenase of Streptococcus bovis
    • H.A. Wyckoff, J. Chow, T.R. Whitehead, and M.A. Cotta Cloning, sequence, and expression of l-(+) lactate dehydrogenase of Streptococcus bovis Curr. Microbiol. 34 1997 367 373
    • (1997) Curr. Microbiol. , vol.34 , pp. 367-373
    • Wyckoff, H.A.1    Chow, J.2    Whitehead, T.R.3    Cotta, M.A.4
  • 33
    • 0015175101 scopus 로고
    • Nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lactate dehydrogenases in homofermentative and heterofermentative lactic acid bacteria
    • H.W. Doelle Nicotinamide adenine dinucleotide-dependent and nicotinamide adenine dinucleotide-independent lactate dehydrogenases in homofermentative and heterofermentative lactic acid bacteria J. Bacteriol. 108 1971 1284 1289
    • (1971) J. Bacteriol. , vol.108 , pp. 1284-1289
    • Doelle, H.W.1
  • 34
    • 0019444405 scopus 로고
    • D-lactate dehydrogenase of Desulfovibrio vulgaris
    • M. Ogata, K. Arihata, and T. Yagi d-lactate dehydrogenase of Desulfovibrio vulgaris J. Biochem. 89 1981 1423 1431
    • (1981) J. Biochem. , vol.89 , pp. 1423-1431
    • Ogata, M.1    Arihata, K.2    Yagi, T.3
  • 36
  • 39
    • 0026613365 scopus 로고
    • The early evolution of eukaryotes: A geological perspective
    • A.H. Knoll The early evolution of eukaryotes: a geological perspective Science 256 1992 622 627
    • (1992) Science , vol.256 , pp. 622-627
    • Knoll, A.H.1
  • 40
    • 0026699609 scopus 로고
    • Aerobic fermentation of glucose by trypanosomatids
    • J.J. Cazzullo Aerobic fermentation of glucose by trypanosomatids FASEB J. 6 1992 3153 3161
    • (1992) FASEB J. , vol.6 , pp. 3153-3161
    • Cazzullo, J.J.1
  • 41
    • 0035184515 scopus 로고    scopus 로고
    • Some Lactobacillus l-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetate
    • K. Arai, T. Kamata, Y. Uchikoba, S. Fushinobu, H. Matsuzawa, and H. Taguchi Some Lactobacillus l-lactate dehydrogenases exhibit comparable catalytic activities for pyruvate and oxaloacetate J. Bacteriol. 183 2001 397 400
    • (2001) J. Bacteriol. , vol.183 , pp. 397-400
    • Arai, K.1    Kamata, T.2    Uchikoba, Y.3    Fushinobu, S.4    Matsuzawa, H.5    Taguchi, H.6
  • 42
    • 0036184069 scopus 로고    scopus 로고
    • An absolute requirement of fructose 1, 6-bisphosphate for the Lactobacillus casei l-lactate dehydrogenase activity induced by a single amino acid substitution
    • K. Arai, A. Hishida, M. Ishiyama, T. Kamata, H. Uchikoba, S. Fushinobu, H. Matsuzawa, and H. Taguchi An absolute requirement of fructose 1, 6-bisphosphate for the Lactobacillus casei l-lactate dehydrogenase activity induced by a single amino acid substitution Protein Eng. 15 2002 35 41
    • (2002) Protein Eng. , vol.15 , pp. 35-41
    • Arai, K.1    Hishida, A.2    Ishiyama, M.3    Kamata, T.4    Uchikoba, H.5    Fushinobu, S.6    Matsuzawa, H.7    Taguchi, H.8
  • 43
    • 0026437845 scopus 로고
    • Unusual amino acid substitution in the anion-binding site Lactobacillus plantarum non-allosteric l-lactate dehydrogenase
    • H. Taguchi, and T. Ohta Unusual amino acid substitution in the anion-binding site Lactobacillus plantarum non-allosteric l-lactate dehydrogenase Eur. J. Biochem. 209 1992 993 998
    • (1992) Eur. J. Biochem. , vol.209 , pp. 993-998
    • Taguchi, H.1    Ohta, T.2
  • 44
    • 0030598645 scopus 로고    scopus 로고
    • Second-hand chloroplasts and the case of the disappearing nucleus
    • J.D. Palmer, and C.F. Delwiche Second-hand chloroplasts and the case of the disappearing nucleus Proc. Natl. Acad. Sci. U. S. A. 93 1996 7432 7435
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7432-7435
    • Palmer, J.D.1    Delwiche, C.F.2
  • 45
    • 0032949947 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: Evidence for intra- and inter-kingdom gene transfer
    • R.M. Figge, M. Schubert, H. Brinkmann, and R. Cerff Glyceraldehyde-3- phosphate dehydrogenase gene diversity in eubacteria and eukaryotes: evidence for intra- and inter-kingdom gene transfer Mol. Biol. Evol. 16 1999 429 444
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 429-444
    • Figge, R.M.1    Schubert, M.2    Brinkmann, H.3    Cerff, R.4
  • 46
    • 0242416598 scopus 로고    scopus 로고
    • Release of extracellular transformable plasmid DNA from Escherichia coli co cultivated with algae
    • K. Matsui, N. Ishii, and Z. Kawabata Release of extracellular transformable plasmid DNA from Escherichia coli co cultivated with algae Appl. Environ. Microbiol. 69 2003 2399 2404
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2399-2404
    • Matsui, K.1    Ishii, N.2    Kawabata, Z.3
  • 47
    • 4444278762 scopus 로고    scopus 로고
    • A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major
    • T.J. Vickers, N. Greig, and A.H. Fairlamb A trypanothione-dependent glyoxalase I with a prokaryotic ancestry in Leishmania major Proc. Natl. Acad. Sci. U. S. A. 101 2004 13186 13191
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13186-13191
    • Vickers, T.J.1    Greig, N.2    Fairlamb, A.H.3


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