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Volumn 178, Issue 20, 1996, Pages 5960-5970

Pyruvate carboxylase from Rhizobium etli: Mutant characterization, nucleotide sequence, and physiological role

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; PYRUVATE CARBOXYLASE; SUCCINIC ACID;

EID: 0029795574     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.20.5960-5970.1996     Document Type: Article
Times cited : (47)

References (68)
  • 1
    • 0017381779 scopus 로고
    • Activities of anaplerotic enzymes and acetyl coenzyme A carboxylase in biotin-deficient Bacillus megaterium
    • Al-ssum, R. M., and P. J. White. 1977. Activities of anaplerotic enzymes and acetyl coenzyme A carboxylase in biotin-deficient Bacillus megaterium. J. Gen. Microbiol. 100:203-206.
    • (1977) J. Gen. Microbiol. , vol.100 , pp. 203-206
    • Al-ssum, R.M.1    White, P.J.2
  • 3
    • 0022513892 scopus 로고
    • Properties of double mutants of Rhizobium leguminosarum which are defective in the utilization of dicarboxylic acids and sugars
    • Arwas, R., A. R. Glenn, I. A. McKay, and M. J. Dilworth. 1986. Properties of double mutants of Rhizobium leguminosarum which are defective in the utilization of dicarboxylic acids and sugars. J. Gen. Microbiol. 132:2743-2747.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2743-2747
    • Arwas, R.1    Glenn, A.R.2    McKay, I.A.3    Dilworth, M.J.4
  • 4
    • 0029035048 scopus 로고
    • The structure and the mechanism of action of pyruvate carboxylase
    • Attwood, P. V. 1995. The structure and the mechanism of action of pyruvate carboxylase. Int. J. Biochem. Cell Biol. 27:231-249.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 231-249
    • Attwood, P.V.1
  • 5
    • 0016231913 scopus 로고
    • R factor transfer in Rhizobium leguminosarum
    • Beringer, J. E. 1974. R factor transfer in Rhizobium leguminosarum. J. Gen. Microbiol. 84:188-198.
    • (1974) J. Gen. Microbiol. , vol.84 , pp. 188-198
    • Beringer, J.E.1
  • 6
    • 0029047343 scopus 로고
    • Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro
    • Birch, O. M., M. Fuhrmann, and N. M. Shaw. 1995. Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro. J. Biol. Chem. 270:19158-19165.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19158-19165
    • Birch, O.M.1    Fuhrmann, M.2    Shaw, N.M.3
  • 7
    • 0023958508 scopus 로고
    • Introduction of the Escherichia coli gdhA gene into Rhizobium phaseoli: Effect on nitrogen fixation
    • Bravo, A., B. Becerril, and J. Mora. 1988. Introduction of the Escherichia coli gdhA gene into Rhizobium phaseoli: effect on nitrogen fixation. J. Bacteriol. 170:985-988.
    • (1988) J. Bacteriol. , vol.170 , pp. 985-988
    • Bravo, A.1    Becerril, B.2    Mora, J.3
  • 8
    • 0023957787 scopus 로고
    • Ammonium assimilation in Rhizobium phaseoli by the glutamine synthetase-glutamate synthase pathway
    • Bravo, A., and J. Mora. 1988. Ammonium assimilation in Rhizobium phaseoli by the glutamine synthetase-glutamate synthase pathway. J. Bacteriol. 170:980-984.
    • (1988) J. Bacteriol. , vol.170 , pp. 980-984
    • Bravo, A.1    Mora, J.2
  • 9
    • 0001655919 scopus 로고
    • A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter
    • Bray, G. A. 1960. A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Anal. Biochem. 1:279-285.
    • (1960) Anal. Biochem. , vol.1 , pp. 279-285
    • Bray, G.A.1
  • 10
    • 0017105264 scopus 로고
    • Occurrence of phosphoenolpyruvate carboxylase in the extremely thermophilic bacterium Thermus aquaticus
    • Bridger, G. P., and T. K. Sundaram. 1976. Occurrence of phosphoenolpyruvate carboxylase in the extremely thermophilic bacterium Thermus aquaticus. J. Bacteriol. 125:1211-1213.
    • (1976) J. Bacteriol. , vol.125 , pp. 1211-1213
    • Bridger, G.P.1    Sundaram, T.K.2
  • 11
    • 0029883692 scopus 로고    scopus 로고
    • Genetic and physiological characterization of a Rhizobium etli mutant strain unable to synthesize poly-β-hydroxybutyrate
    • Cevallos, M. A., S. Encarnación, A. Leija, Y. Mora, and J. Mora. 1996. Genetic and physiological characterization of a Rhizobium etli mutant strain unable to synthesize poly-β-hydroxybutyrate. J. Bacteriol. 178:1646-1654.
    • (1996) J. Bacteriol. , vol.178 , pp. 1646-1654
    • Cevallos, M.A.1    Encarnación, S.2    Leija, A.3    Mora, Y.4    Mora, J.5
  • 12
    • 0018666573 scopus 로고
    • Quaternary structure of pyruvate carboxylase from Pseudomonas citronellolis
    • Cohen, N. D., J. A. Duc, H. Beegan, and M. F. Utter. 1979. Quaternary structure of pyruvate carboxylase from Pseudomonas citronellolis. J. Biol. Chem. 254:9262-9269.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9262-9269
    • Cohen, N.D.1    Duc, J.A.2    Beegan, H.3    Utter, M.F.4
  • 13
    • 0015886456 scopus 로고
    • Role of pyruvate carboxylase, phosphenolpyruvate carboxykinase and malic enzyme during growth and sporulation of Bacillus subtilis
    • Diesterhaft, M. D., and E. Freese. 1973. Role of pyruvate carboxylase, phosphenolpyruvate carboxykinase and malic enzyme during growth and sporulation of Bacillus subtilis. J. Biol. Chem. 248:6062-6070.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6062-6070
    • Diesterhaft, M.D.1    Freese, E.2
  • 15
    • 10144246029 scopus 로고
    • Biochemical and genetic characterization of pyruvate carboxylase in Rhizobium etli and R. tropici
    • I. A. Tikhonovich, N. A. Provorov, V. I. Romanov, and W. E. Newton (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Dunn, M. F., and J. Mora. 1995. Biochemical and genetic characterization of pyruvate carboxylase in Rhizobium etli and R. tropici, p. 576. In I. A. Tikhonovich, N. A. Provorov, V. I. Romanov, and W. E. Newton (ed.), Nitrogen fixation: fundamentals and applications. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 576
    • Dunn, M.F.1    Mora, J.2
  • 16
    • 0018162579 scopus 로고
    • A rapid method for the identification of plasmid deoxyribonucleic acid in bacteria
    • Eckhardt, T. 1978. A rapid method for the identification of plasmid deoxyribonucleic acid in bacteria. Plasmid 1:584-588.
    • (1978) Plasmid , vol.1 , pp. 584-588
    • Eckhardt, T.1
  • 17
    • 84889540514 scopus 로고
    • Alternative metabolic programs in Rhizobium
    • I. A. Tikhonovich, N. A. Provorov, V. I. Romanov, and W. E. Newton (ed.), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Encarnación, S., M. Dunn, A. Leija, M. C. Vargas, H. Peralta, and J. Mora. 1995. Alternative metabolic programs in Rhizobium, p. 577. In I. A. Tikhonovich, N. A. Provorov, V. I. Romanov, and W. E. Newton (ed.), Nitrogen fixation: fundamentals and applications. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 577
    • Encarnación, S.1    Dunn, M.2    Leija, A.3    Vargas, M.C.4    Peralta, H.5    Mora, J.6
  • 18
    • 0029051430 scopus 로고
    • Fermentative and aerobic metabolism in Rhizobium etli
    • Encarnación, S., M. Dunn, K. Willms, and J. Mora. 1995. Fermentative and aerobic metabolism in Rhizobium etli. J. Bacteriol. 177:3058-3066.
    • (1995) J. Bacteriol. , vol.177 , pp. 3058-3066
    • Encarnación, S.1    Dunn, M.2    Willms, K.3    Mora, J.4
  • 20
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 21
    • 0020429966 scopus 로고
    • Construction of a broad host range cosmid cloning vector and its use in the genetic analysis of Rhizobium mutants
    • Friedman, A. M., S. R. Long, S. E. Brown, W. J. Buikema, and F. M. Ausubel. 1982. Construction of a broad host range cosmid cloning vector and its use in the genetic analysis of Rhizobium mutants. Gene 18:289-296.
    • (1982) Gene , vol.18 , pp. 289-296
    • Friedman, A.M.1    Long, S.R.2    Brown, S.E.3    Buikema, W.J.4    Ausubel, F.M.5
  • 22
    • 0346497938 scopus 로고
    • ATP-binding site of adenylate kinase: Mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins
    • Fry, D. C., S. A. Kuby, and A. S. Mildvan. 1986. ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. Proc. Natl. Acad. Sci. USA 83:907-911.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 907-911
    • Fry, D.C.1    Kuby, S.A.2    Mildvan, A.S.3
  • 23
    • 0025255109 scopus 로고
    • One-dimensional gel electrophoresis
    • M. P. Deutcher (ed.), Academic Press Inc., New York
    • Garfin, D. E. 1990. One-dimensional gel electrophoresis, p. 425-441. In M. P. Deutcher (ed.), Guide to protein purification. Academic Press Inc., New York.
    • (1990) Guide to Protein Purification , pp. 425-441
    • Garfin, D.E.1
  • 25
    • 0023886015 scopus 로고
    • Posttranscriptional regulatory mechanisms in Escherichia coli
    • Gold, L. 1988. Posttranscriptional regulatory mechanisms in Escherichia coli. Annu. Rev. Biochem. 57:199-233.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 199-233
    • Gold, L.1
  • 26
    • 0019888654 scopus 로고
    • Characterization of the subunit structure of pyruvate carboxylase from Pseudomonas citronellolis
    • Goss, J. A., N. D. Cohen, and M. F. Utter. 1981. Characterization of the subunit structure of pyruvate carboxylase from Pseudomonas citronellolis. J. Biol. Chem. 256:11819-11825.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11819-11825
    • Goss, J.A.1    Cohen, N.D.2    Utter, M.F.3
  • 29
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • Knowles, J. R. 1989. The mechanism of biotin-dependent enzymes. Annu. Rev. Biochem. 58:195-221.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 30
    • 0023777889 scopus 로고
    • Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase
    • Kumer, G. K., F. C. Haase, N. F. B. Phillips, and H. G. Wood. 1988. Involvement and identification of a tryptophanyl residue at the pyruvate binding site of transcarboxylase. Biochemistry 27:5978-5983.
    • (1988) Biochemistry , vol.27 , pp. 5978-5983
    • Kumer, G.K.1    Haase, F.C.2    Phillips, N.F.B.3    Wood, H.G.4
  • 31
    • 0023241711 scopus 로고
    • Sequence homology around the biotin-binding site of human propionyl-CoA and pyruvate carboxylase
    • Lamhonwah, A., F. Quan, and R. A. Gravel. 1987. Sequence homology around the biotin-binding site of human propionyl-CoA and pyruvate carboxylase. Arch. Biochem. Biophys. 254:631-636.
    • (1987) Arch. Biochem. Biophys. , vol.254 , pp. 631-636
    • Lamhonwah, A.1    Quan, F.2    Gravel, R.A.3
  • 32
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
    • Li, S., and J. E. Cronan. 1992. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267:855-863.
    • (1992) J. Biol. Chem. , vol.267 , pp. 855-863
    • Li, S.1    Cronan, J.E.2
  • 33
    • 0018321181 scopus 로고
    • Pyruvate carboxylase from a thermophilic Bacillus: Some molecular characteristics
    • Libor, S., T. K. Sundaram, R. Warwick, J. A. Chapman, and S. M. W. Grundy. 1979. Pyruvate carboxylase from a thermophilic Bacillus: some molecular characteristics. Biochemistry 18:3647-3653.
    • (1979) Biochemistry , vol.18 , pp. 3647-3653
    • Libor, S.1    Sundaram, T.K.2    Warwick, R.3    Chapman, J.A.4    Grundy, S.M.W.5
  • 34
    • 0023758327 scopus 로고
    • Sequence and domain structure of yeast pyruvate carboxylase
    • Lim, F., C. P. Morris, F. Occhiodoro, and J. C. Wallace. 1988. Sequence and domain structure of yeast pyruvate carboxylase. J. Biol. Chem. 263:11493-11497.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11493-11497
    • Lim, F.1    Morris, C.P.2    Occhiodoro, F.3    Wallace, J.C.4
  • 36
    • 0023202768 scopus 로고
    • Nitrogen-fixing nodules induced by Agrobacterium tumefaciens harboring Rhizobium phaseoli plasmids
    • Martínez, E., R. Palacios, and F. Sánchez. 1987. Nitrogen-fixing nodules induced by Agrobacterium tumefaciens harboring Rhizobium phaseoli plasmids. J. Bacteriol. 169:2828-2834.
    • (1987) J. Bacteriol. , vol.169 , pp. 2828-2834
    • Martínez, E.1    Palacios, R.2    Sánchez, F.3
  • 37
    • 0019491697 scopus 로고
    • Properties of a mutant Escherichia coli phosphoenolpyruvate carboxylase deficient in coregulation by intermediary metabolites
    • McAlister, L. E., E. L. Evans and T. E. Smith. 1981. Properties of a mutant Escherichia coli phosphoenolpyruvate carboxylase deficient in coregulation by intermediary metabolites. J. Bacteriol. 146:200-208.
    • (1981) J. Bacteriol. , vol.146 , pp. 200-208
    • McAlister, L.E.1    Evans, E.L.2    Smith, T.E.3
  • 38
    • 0017253676 scopus 로고
    • Some properties of the pyruvate carboxylase from Pseudomonas fluorescens
    • Milrad de Forchetti, S. R., and J. J. Cazzulo. 1976. Some properties of the pyruvate carboxylase from Pseudomonas fluorescens. J. Gen. Microbiol. 93:75-81.
    • (1976) J. Gen. Microbiol. , vol.93 , pp. 75-81
    • Milrad de Forchetti, S.R.1    Cazzulo, J.J.2
  • 39
    • 0028786959 scopus 로고
    • Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: Rapid and efficient purification using dye-ligand affinity Chromatography
    • Modak, H. V., and D. J. Kelly. 1995. Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: rapid and efficient purification using dye-ligand affinity Chromatography. Microbiology 141:2619-2628.
    • (1995) Microbiology , vol.141 , pp. 2619-2628
    • Modak, H.V.1    Kelly, D.J.2
  • 41
    • 0024386754 scopus 로고
    • Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli
    • Muramatsu, S., and T. Mizuno. 1989. Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 17:3982.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3982
    • Muramatsu, S.1    Mizuno, T.2
  • 42
    • 0021112620 scopus 로고
    • Activation of yeast pyruvate carboxylase: Interactions between acyl coenzyme A compounds, aspartate, and substrates of the reaction
    • Myers, D. E., B. Tolbert, and M. F. Utter. 1983. Activation of yeast pyruvate carboxylase: interactions between acyl coenzyme A compounds, aspartate, and substrates of the reaction. Biochemistry 22:5090-5096.
    • (1983) Biochemistry , vol.22 , pp. 5090-5096
    • Myers, D.E.1    Tolbert, B.2    Utter, M.F.3
  • 43
    • 0001538565 scopus 로고
    • Two-carbon compounds and fatty acids as carbon sources
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Nunn, W. D. 1987. Two-carbon compounds and fatty acids as carbon sources, p. 285-301. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol. 2. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.2 , pp. 285-301
    • Nunn, W.D.1
  • 44
    • 0022388322 scopus 로고
    • Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat
    • Nyunoya, H., K. E. Broglie, E. E. Widgren, and C. J. Lusty. 1985. Characterization and derivation of the gene coding for mitochondrial carbamyl phosphate synthetase I of rat. J. Biol. Chem. 260:9346-9356.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9346-9356
    • Nyunoya, H.1    Broglie, K.E.2    Widgren, E.E.3    Lusty, C.J.4
  • 45
    • 0017581550 scopus 로고
    • Novel enzymic machinery for the metabolism of oxalacetate, phosphoenolpyruvate, and pyruvate in Pseudomonas citronellolis
    • O'Brien, R. W., D. T. Chuang, B. L. Taylor, and M. F. Utter. 1977. Novel enzymic machinery for the metabolism of oxalacetate, phosphoenolpyruvate, and pyruvate in Pseudomonas citronellolis. J. Biol. Chem. 252:1257-1263.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1257-1263
    • O'Brien, R.W.1    Chuang, D.T.2    Taylor, B.L.3    Utter, M.F.4
  • 46
    • 0014599987 scopus 로고
    • Pyruvate carboxylase in Rhodopseudomonas spheroides
    • Payne, J., and J. G. Morris. 1969. Pyruvate carboxylase in Rhodopseudomonas spheroides. J. Gen. Microbiol. 59:97-101.
    • (1969) J. Gen. Microbiol. , vol.59 , pp. 97-101
    • Payne, J.1    Morris, J.G.2
  • 47
  • 48
    • 0025349207 scopus 로고
    • Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthetase by site-directed mutagenesis
    • Post, L. E., D. J. Post, and F. M. Raushel. 1990. Dissection of the functional domains of Escherichia coli carbamoyl phosphate synthetase by site-directed mutagenesis. J. Biol. Chem. 265:7742-7747.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7742-7747
    • Post, L.E.1    Post, D.J.2    Raushel, F.M.3
  • 49
    • 0015295768 scopus 로고
    • Characterization and regulation of pyruvate carboxylase of Bacillus licheniformis
    • Renner, E. D., and R. W. Bernlohr. 1972. Characterization and regulation of pyruvate carboxylase of Bacillus licheniformis. J. Bacteriol. 109:764-772.
    • (1972) J. Bacteriol. , vol.109 , pp. 764-772
    • Renner, E.D.1    Bernlohr, R.W.2
  • 50
    • 0018358621 scopus 로고
    • Carbohydrate metabolism in Rhizobium trifolii: Identification and symbiotic properties of mutants
    • Ronson, C. W., and S. B. Primrose. 1979. Carbohydrate metabolism in Rhizobium trifolii: identification and symbiotic properties of mutants. J. Gen. Microbiol. 112:77-88.
    • (1979) J. Gen. Microbiol. , vol.112 , pp. 77-88
    • Ronson, C.W.1    Primrose, S.B.2
  • 54
    • 0017822194 scopus 로고
    • Fine control of the conversion of pyruvate (phosphoenolpyruvate) to oxaloacetate in various species
    • Scrutton, M. C. 1978. Fine control of the conversion of pyruvate (phosphoenolpyruvate) to oxaloacetate in various species. FEBS Lett. 89:1-9.
    • (1978) FEBS Lett. , vol.89 , pp. 1-9
    • Scrutton, M.C.1
  • 55
    • 0016303310 scopus 로고
    • Isolation and characterization of pyruvate carboxylase from Azotobacter vinelandii OP
    • Scrutton, M. C., and B. L. Taylor. 1974. Isolation and characterization of pyruvate carboxylase from Azotobacter vinelandii OP. Arch. Biochem. Biophys. 164:641-654.
    • (1974) Arch. Biochem. Biophys. , vol.164 , pp. 641-654
    • Scrutton, M.C.1    Taylor, B.L.2
  • 56
    • 0021205685 scopus 로고
    • High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-mob transposon
    • Simon, R. 1984. High frequency mobilization of gram-negative bacterial replicons by the in vitro constructed Tn5-mob transposon. Mol. Gen. Genet. 196:413-420.
    • (1984) Mol. Gen. Genet. , vol.196 , pp. 413-420
    • Simon, R.1
  • 57
    • 84889511410 scopus 로고
    • GenBank accession number U00024
    • Smith, D. R. 1994. GenBank accession number U00024.
    • (1994)
    • Smith, D.R.1
  • 58
    • 77956846102 scopus 로고
    • Transport and metabolism of carbon and nitrogen in legume nodules
    • Streeter, J. G. 1991. Transport and metabolism of carbon and nitrogen in legume nodules. Adv. Bot. Res. 18:129-187.
    • (1991) Adv. Bot. Res. , vol.18 , pp. 129-187
    • Streeter, J.G.1
  • 59
    • 0030199206 scopus 로고    scopus 로고
    • Biotin and other water-soluble vitamins are key growth factors for alfalfa root colonization by Rhizobium meliloti 1021
    • Streit, W. R., C. M. Joseph, and D. A. Phillips. 1996. Biotin and other water-soluble vitamins are key growth factors for alfalfa root colonization by Rhizobium meliloti 1021. Mol. Plant-Microbe Interact. 9:330-338.
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 330-338
    • Streit, W.R.1    Joseph, C.M.2    Phillips, D.A.3
  • 60
    • 0015579573 scopus 로고
    • Physiological role of pyruvate carboxylase in a thermophilic Bacillus
    • Sundaram, T. K. 1973. Physiological role of pyruvate carboxylase in a thermophilic Bacillus. J. Bacteriol. 113:307-315.
    • (1973) J. Bacteriol. , vol.113 , pp. 307-315
    • Sundaram, T.K.1
  • 61
    • 84889544265 scopus 로고    scopus 로고
    • Personal communication
    • Taboada, H. Personal communication.
    • Taboada, H.1
  • 62
    • 0016658309 scopus 로고
    • The control of the synthesis of pyruvate carboxylase in Pseudomonas citronellolis: Evidence from double labeling studies
    • Taylor, B. L., S. Routman, and M. F. Utter. 1975. The control of the synthesis of pyruvate carboxylase in Pseudomonas citronellolis: evidence from double labeling studies. J. Biol. Chem. 250:2376-2382.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2376-2382
    • Taylor, B.L.1    Routman, S.2    Utter, M.F.3
  • 63
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 65
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 66
    • 0042355955 scopus 로고
    • Biotin as a growth stimulant for the root nodule bacteria
    • West, P. M., and P. W. Wilson. 1940. Biotin as a growth stimulant for the root nodule bacteria. Enzymologia 8:152-162.
    • (1940) Enzymologia , vol.8 , pp. 152-162
    • West, P.M.1    Wilson, P.W.2
  • 68
    • 0001505524 scopus 로고
    • Pyruvate and acetate metabolism in the photosynthetic bacterium Rhodobacter capsulatus
    • Willison, J. C. 1988. Pyruvate and acetate metabolism in the photosynthetic bacterium Rhodobacter capsulatus. J. Gen. Microbiol. 134:2429-2439.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2429-2439
    • Willison, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.