메뉴 건너뛰기




Volumn 31, Issue 2, 1999, Pages 473-487

The sodium ion translocating glutaconyl-CoA decarboxylase from Acidaminococcus fermentans: Cloning and function of the genes forming a second operon

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; BIOTIN; CARBOXYLYASE; GENE PRODUCT; LYSINE; PROLINE; PROTON; SODIUM ION; VALINE;

EID: 0032956982     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01189.x     Document Type: Article
Times cited : (30)

References (69)
  • 2
    • 0025063535 scopus 로고    scopus 로고
    • The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum)
    • Beatrix, B., Bendrat, K., Rospert, S., and Buckel, W. (1990) The biotin-dependent sodium ion pump glutaconyl-CoA decarboxylase from Fusobacterium nucleatum (subsp. nucleatum). Arch Microbiol 154: 362-369.
    • Arch Microbiol , vol.154 , pp. 362-369
    • Beatrix, B.1    Bendrat, K.2    Rospert, S.3    Buckel, W.4
  • 3
    • 0025667281 scopus 로고
    • Carbon-13 labelled biotin - A new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions
    • Bendrat, K., Berger, S., Buckel, W., Etzel, W.A., and Röhm, K.-H. (1990) Carbon-13 labelled biotin - a new probe for the study of enzyme catalyzed carboxylation and decarboxylation reactions. FEBS Lett 277: 156-158.
    • (1990) FEBS Lett , vol.277 , pp. 156-158
    • Bendrat, K.1    Berger, S.2    Buckel, W.3    Etzel, W.A.4    Röhm, K.-H.5
  • 4
    • 0027413302 scopus 로고
    • + pump glutaconyl-CoA decarboxylase from Acidaminococcus fermentans in Escherichia coli
    • + pump glutaconyl-CoA decarboxylase from Acidaminococcus fermentans in Escherichia coli. Eur J Biochem 211: 697-702.
    • (1993) Eur J Biochem , vol.211 , pp. 697-702
    • Bendrat, K.1    Buckel, W.2
  • 5
    • 0027258114 scopus 로고
    • Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • Bendrat, K., Müller, U., Klees, A.-G., and Buckel, W. (1993) Identification of the gene encoding the activator of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. FEBS Lett 329: 329-331.
    • (1993) FEBS Lett , vol.329 , pp. 329-331
    • Bendrat, K.1    Müller, U.2    Klees, A.-G.3    Buckel, W.4
  • 8
    • 0013515167 scopus 로고    scopus 로고
    • 13C-spin-spin coupling. Angew Chem 108: 2259-2261; Angew Chem Int Ed Engl 35: 2132-2133.
    • Angew Chem Int Ed Engl , vol.35 , pp. 2132-2133
  • 9
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H.C., and Doly, J. (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7: 1513-1523.
    • (1979) Nucleic Acids Res , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 10
    • 0026941152 scopus 로고
    • Phylogenetic and chemotaxonomic characterization of Acidaminococcus fermentans
    • Both, B., Buckel, W., Kroppenstedt, R., and Stackebrandt, E. (1992) Phylogenetic and chemotaxonomic characterization of Acidaminococcus fermentans. FEMS Microbiol Lett 97: 7-12.
    • (1992) FEMS Microbiol Lett , vol.97 , pp. 7-12
    • Both, B.1    Buckel, W.2    Kroppenstedt, R.3    Stackebrandt, E.4
  • 11
    • 0031465120 scopus 로고    scopus 로고
    • Methylmalonyl-CoA decarboxylase from Propionigenium modestum. Cloning and sequencing of the structural genes and purification of the enzyme complex
    • Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woelke, G., and Dimroth, P. (1997) Methylmalonyl-CoA decarboxylase from Propionigenium modestum. Cloning and sequencing of the structural genes and purification of the enzyme complex. Eur J Biochem 250: 590-599.
    • (1997) Eur J Biochem , vol.250 , pp. 590-599
    • Bott, M.1    Pfister, K.2    Burda, P.3    Kalbermatter, O.4    Woelke, G.5    Dimroth, P.6
  • 12
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P.D. (1997) The ATP synthase - a splendid molecular machine. Annu Rev Biochem 66: 717-749.
    • (1997) Annu Rev Biochem , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 13
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0019017657 scopus 로고
    • The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate
    • Buckel, W. (1980) The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate. Eur J Biochem 106: 439-447.
    • (1980) Eur J Biochem , vol.106 , pp. 439-447
    • Buckel, W.1
  • 15
    • 0022485604 scopus 로고
    • Biotin-dependent decarboxylases as bacterial sodium pumps: Purification and reconstitution of glutaconyl-CoA decarboxylase from Acidaminococcus fermentans
    • Buckel, W. (1986) Biotin-dependent decarboxylases as bacterial sodium pumps: purification and reconstitution of glutaconyl-CoA decarboxylase from Acidaminococcus fermentans. Methods Enzymol 125: 547-558.
    • (1986) Methods Enzymol , vol.125 , pp. 547-558
    • Buckel, W.1
  • 16
    • 0019401061 scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans
    • Buckel, W., Dorn, U., and Semmler, R. (1981) Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur J Biochem 118: 315-321.
    • (1981) Eur J Biochem , vol.118 , pp. 315-321
    • Buckel, W.1    Dorn, U.2    Semmler, R.3
  • 17
    • 0023049495 scopus 로고
    • The sodium pump glutaconyl-CoA decarboxylase from A. fermentans. Specific cleavage by n-alkanols
    • Buckel, W., and Liedtke, H. (1986) The sodium pump glutaconyl-CoA decarboxylase from A. fermentans. Specific cleavage by n-alkanols. Eur J Biochem 156: 251-257.
    • (1986) Eur J Biochem , vol.156 , pp. 251-257
    • Buckel, W.1    Liedtke, H.2
  • 18
    • 0020214108 scopus 로고
    • A biotin-dependent sodium pump: Glutaconyl-CoA decarboxylase from Acidaminococcus fermentans
    • Buckel, W., and Semmler, R. (1982) A biotin-dependent sodium pump: glutaconyl-CoA decarboxylase from Acidaminococcus fermentans. FEBS Lett 148: 35-38.
    • (1982) FEBS Lett , vol.148 , pp. 35-38
    • Buckel, W.1    Semmler, R.2
  • 19
    • 0021093632 scopus 로고
    • Purification, characterization and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria
    • Buckel, W., and Semmler, R. (1983) Purification, characterization and reconstitution of glutaconyl-CoA decarboxylase, a biotin-dependent sodium pump from anaerobic bacteria. Eur J Biochem 136: 427-434.
    • (1983) Eur J Biochem , vol.136 , pp. 427-434
    • Buckel, W.1    Semmler, R.2
  • 20
    • 0028126829 scopus 로고
    • The phylogeny of the genus Clostridium: Proposal of five new genera and eleven new species combinations
    • Collins, M.D., Lawson, P.A., Willems, A., Cordoba, J.J., Fernandez-Garayzabal, J., Garcia, P., et al. (1994) The phylogeny of the genus Clostridium: proposal of five new genera and eleven new species combinations. Int J Bacteriol 44: 812-826.
    • (1994) Int J Bacteriol , vol.44 , pp. 812-826
    • Collins, M.D.1    Lawson, P.A.2    Willems, A.3    Cordoba, J.J.4    Fernandez-Garayzabal, J.5    Garcia, P.6
  • 21
    • 0028239570 scopus 로고
    • Emendation of the description of Acidaminococcus fermentans, a trans-aconitate and citrate-oxidizing bacterium
    • Cook, G.M., Rainey, F.A., Chen, G., Stackebrandt, E., and Russell, J.B. (1994) Emendation of the description of Acidaminococcus fermentans, a trans-aconitate and citrate-oxidizing bacterium. Int J Sys Bact 44: 576-578.
    • (1994) Int J Sys Bact , vol.44 , pp. 576-578
    • Cook, G.M.1    Rainey, F.A.2    Chen, G.3    Stackebrandt, E.4    Russell, J.B.5
  • 22
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo
    • Cronan, J.E. Jr (1990) Biotination of proteins in vivo. J Biol Chem 265: 10327-10333.
    • (1990) J Biol Chem , vol.265 , pp. 10327-10333
    • Cronan J.E., Jr.1
  • 23
    • 0029804064 scopus 로고    scopus 로고
    • Butyrate, aspirin and colorectal cancer
    • Csordas, A. (1996) Butyrate, aspirin and colorectal cancer. Eur J Cancer Prevent 5: 221-231.
    • (1996) Eur J Cancer Prevent , vol.5 , pp. 221-231
    • Csordas, A.1
  • 24
    • 0029092741 scopus 로고
    • + pump and its individual subunits in Escherichia coli and analysis of their function
    • + pump and its individual subunits in Escherichia coli and analysis of their function. Eur J Biochem 231: 790-801.
    • (1995) Eur J Biochem , vol.231 , pp. 790-801
    • Di Berardino, M.1    Dimroth, P.2
  • 26
    • 0019335466 scopus 로고
    • A new sodium-transport system energized by the decarboxylation of oxaloacetate
    • Dimroth, P. (1980) A new sodium-transport system energized by the decarboxylation of oxaloacetate. FEBS Lett 122: 234-236.
    • (1980) FEBS Lett , vol.122 , pp. 234-236
    • Dimroth, P.1
  • 27
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • Dimroth, P. (1997) Primary sodium ion translocating enzymes. Biochim Biophys Acta 1318: 11-51.
    • (1997) Biochim Biophys Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 28
    • 0027474059 scopus 로고
    • On the mechanism of sodium ion translocation by oxaloacetate decarboxylase from Klebsiella pneumoniae
    • Dimroth, P., and Thomer, A. (1993) On the mechanism of sodium ion translocation by oxaloacetate decarboxylase from Klebsiella pneumoniae. Biochemistry 32: 1734-1739.
    • (1993) Biochemistry , vol.32 , pp. 1734-1739
    • Dimroth, P.1    Thomer, A.2
  • 29
    • 0024363274 scopus 로고
    • Cloning and sequencing of the genes of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • Dutscho, R., Wohlfarth, G., Buckel, P., and Buckel, W. (1989) Cloning and sequencing of the genes of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Eur J Biochem 181: 741-746.
    • (1989) Eur J Biochem , vol.181 , pp. 741-746
    • Dutscho, R.1    Wohlfarth, G.2    Buckel, P.3    Buckel, W.4
  • 30
    • 0015524195 scopus 로고
    • Acetyl coenzyme A carboxylase. Molecular forms and subunit composition of biotin carboxyl carrier protein
    • Fall, R.R., and Vagelos, P.R. (1972) Acetyl coenzyme A carboxylase. Molecular forms and subunit composition of biotin carboxyl carrier protein. J Biol Chem 247: 8005-8015.
    • (1972) J Biol Chem , vol.247 , pp. 8005-8015
    • Fall, R.R.1    Vagelos, P.R.2
  • 31
    • 0013935204 scopus 로고
    • Some morphological and physiological characteristics of Gram-negative anaerobic bacteria isolated from the alimentary tract of the pig
    • Fuller, R. (1966) Some morphological and physiological characteristics of Gram-negative anaerobic bacteria isolated from the alimentary tract of the pig. J Appl Bacteriol 29: 375-379.
    • (1966) J Appl Bacteriol , vol.29 , pp. 375-379
    • Fuller, R.1
  • 32
    • 0019258624 scopus 로고
    • Elution of proteins from sodium dodecylsulfate polyacrylamide gels, removal of SDS and renaturation of enzymatic activity: Results with sigma subunit of E. coli RNA polymerase, wheat germ DNA topoisomerase and other enzymes
    • Hager, D.A., and Burgess, R.R. (1980) Elution of proteins from sodium dodecylsulfate polyacrylamide gels, removal of SDS and renaturation of enzymatic activity: results with sigma subunit of E. coli RNA polymerase, wheat germ DNA topoisomerase and other enzymes. Anal Biochem 109: 76-86.
    • (1980) Anal Biochem , vol.109 , pp. 76-86
    • Hager, D.A.1    Burgess, R.R.2
  • 33
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557.
    • (1983) J Mol Biol , vol.166 , pp. 557
    • Hanahan, D.1
  • 34
    • 0029839587 scopus 로고    scopus 로고
    • Fermentation of trans-aconitate via citrate, oxaloacetate and pyruvate by Acidaminococcus fermentans
    • Härtel, U., and Buckel, W. (1996a) Fermentation of trans-aconitate via citrate, oxaloacetate and pyruvate by Acidaminococcus fermentans. Arch Microbiol 166: 342-349.
    • (1996) Arch Microbiol , vol.166 , pp. 342-349
    • Härtel, U.1    Buckel, W.2
  • 35
    • 0029803262 scopus 로고    scopus 로고
    • Sodium ion-dependent hydrogen production in Acidaminococcus fermentans
    • Härtel, U., and Buckel, W. (1996b) Sodium ion-dependent hydrogen production in Acidaminococcus fermentans. Arch Microbiol 166: 350-356.
    • (1996) Arch Microbiol , vol.166 , pp. 350-356
    • Härtel, U.1    Buckel, W.2
  • 36
    • 0021111879 scopus 로고
    • Compilation and analysis of Escherichia coli promoter DNA sequences
    • Hawley, D.K., and McClure, W.R. (1983) Compilation and analysis of Escherichia coli promoter DNA sequences. Nucleic Acids Res 11: 2237-2255.
    • (1983) Nucleic Acids Res , vol.11 , pp. 2237-2255
    • Hawley, D.K.1    McClure, W.R.2
  • 37
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne, G. (1986) The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J 5: 3021-3027.
    • (1986) EMBO J , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 38
    • 0022503287 scopus 로고
    • Sodium pump methylmalonyl-CoA decarboxylase from Veillonella parvula
    • Hilpert, W., and Dimroth, P. (1986) Sodium pump methylmalonyl-CoA decarboxylase from Veillonella parvula. Methods Enzymol 125: 540-546.
    • (1986) Methods Enzymol , vol.125 , pp. 540-546
    • Hilpert, W.1    Dimroth, P.2
  • 39
    • 0027367414 scopus 로고
    • Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula
    • Huder, J.B., and Dimroth, P. (1993) Sequence of the sodium ion pump methylmalonyl-CoA decarboxylase from Veillonella parvula. J Biol Chem 268: 24564-24571.
    • (1993) J Biol Chem , vol.268 , pp. 24564-24571
    • Huder, J.B.1    Dimroth, P.2
  • 40
    • 0031569327 scopus 로고    scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans: The crystal structure reveals homology with other CoA-transferases
    • Jacob, U., Mack, M., Clausen, T., Huber, R., Buckel, W., and Messerschmidt, A. (1997) Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal structure reveals homology with other CoA-transferases. Structure 5: 415-426.
    • (1997) Structure , vol.5 , pp. 415-426
    • Jacob, U.1    Mack, M.2    Clausen, T.3    Huber, R.4    Buckel, W.5    Messerschmidt, A.6
  • 41
    • 0031458333 scopus 로고    scopus 로고
    • The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
    • Klenk, H.P., Clayton, R.A., Tomb, J., White, O., Nelson, K.E., Ketchum, K.A., et al. (1997) The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390: 364-370.
    • (1997) Nature , vol.390 , pp. 364-370
    • Klenk, H.P.1    Clayton, R.A.2    Tomb, J.3    White, O.4    Nelson, K.E.5    Ketchum, K.A.6
  • 42
    • 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
  • 43
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0028075976 scopus 로고
    • Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
    • Mack, M., Bendrat, K., Zelder, O., Eckel, E., Linder, D., and Buckel, W. (1994) Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans. Eur J Biochem 226: 41-51.
    • (1994) Eur J Biochem , vol.226 , pp. 41-51
    • Mack, M.1    Bendrat, K.2    Zelder, O.3    Eckel, E.4    Linder, D.5    Buckel, W.6
  • 47
    • 0023813683 scopus 로고
    • Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering
    • Miles, J.S., Guest, J.R., Radford, S.E., and Perham, R.H. (1988) Investigation of the mechanism of active site coupling in the pyruvate dehydrogenase multienzyme complex of Escherichia coli by protein engineering. J Mol Biol 202: 97-106.
    • (1988) J Mol Biol , vol.202 , pp. 97-106
    • Miles, J.S.1    Guest, J.R.2    Radford, S.E.3    Perham, R.H.4
  • 48
    • 0029040983 scopus 로고
    • Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • Müller, U., and Buckel, W. (1995) Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Eur J Biochem 230: 698-704.
    • (1995) Eur J Biochem , vol.230 , pp. 698-704
    • Müller, U.1    Buckel, W.2
  • 49
    • 0019296097 scopus 로고
    • Butyric acid: A small fatty acid with diverse biological functions
    • Prasad, K.N. (1980) Butyric acid: a small fatty acid with diverse biological functions. Life Sciences 27: 1351-1358.
    • (1980) Life Sciences , vol.27 , pp. 1351-1358
    • Prasad, K.N.1
  • 50
    • 0023440862 scopus 로고
    • Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Genetic reconstruction in vitro and 1H-n.m.r. spectroscopy
    • Radford, S.E., Laue, E.D., Perham, R.N., Miles, J.S., and Guest, J.R. (1987) Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Genetic reconstruction in vitro and 1H-n.m.r. spectroscopy. Biochem J 247: 641-649.
    • (1987) Biochem J , vol.247 , pp. 641-649
    • Radford, S.E.1    Laue, E.D.2    Perham, R.N.3    Miles, J.S.4    Guest, J.R.5
  • 51
    • 0014512027 scopus 로고
    • Acidaminococcus gen. n., Acidaminococcus fermentans sp. n. anaerobic Gram-negative diplococci using amino acids as the sole energy source for growth
    • Rogosa, M. (1969) Acidaminococcus gen. n., Acidaminococcus fermentans sp. n. anaerobic Gram-negative diplococci using amino acids as the sole energy source for growth. J Bacteriol 98: 756-766.
    • (1969) J Bacteriol , vol.98 , pp. 756-766
    • Rogosa, M.1
  • 55
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., Nicklen, S., and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74: 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 56
    • 0016714130 scopus 로고
    • Investigations of the structure of 3-methylcrotonyl-CoA carboxylase from Achromobacter
    • Schiele, U., Niedermeier, R., Stürzer, M., and Lynen, F. (1975) Investigations of the structure of 3-methylcrotonyl-CoA carboxylase from Achromobacter. Eur J Biochem 60: 256-266.
    • (1975) Eur J Biochem , vol.60 , pp. 256-266
    • Schiele, U.1    Niedermeier, R.2    Stürzer, M.3    Lynen, F.4
  • 57
    • 0023727091 scopus 로고
    • The sodium translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the biotin-containing α-subunit and relationship to other biotin-containing enzymes
    • Schwarz, E., Oesterhelt, D., Reinke, H., Beyreuther, K., and Dimroth, P. (1988) The sodium translocating oxaloacetate decarboxylase of Klebsiella pneumoniae. Sequence of the biotin-containing α-subunit and relationship to other biotin-containing enzymes. J Biol Chem 263: 9640-9645.
    • (1988) J Biol Chem , vol.263 , pp. 9640-9645
    • Schwarz, E.1    Oesterhelt, D.2    Reinke, H.3    Beyreuther, K.4    Dimroth, P.5
  • 58
    • 0016610995 scopus 로고
    • Determinant of cistron specificity in bacterial ribosomes
    • Shine, J., and Dalgarno, L. (1975) Determinant of cistron specificity in bacterial ribosomes. Nature 254: 34-38.
    • (1975) Nature , vol.254 , pp. 34-38
    • Shine, J.1    Dalgarno, L.2
  • 59
    • 0014010554 scopus 로고
    • Citrate-condensing enzyme-oxaloacetate binary complex
    • Srere, P.A. (1966) Citrate-condensing enzyme-oxaloacetate binary complex. J Biol Chem 241: 2157-2165.
    • (1966) J Biol Chem , vol.241 , pp. 2157-2165
    • Srere, P.A.1
  • 60
    • 0020789034 scopus 로고
    • The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component
    • Stephens, P.E., Darlinson, M.G., Lewis, H.M., and Guest, J.R. (1983) The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur J Biochem 133: 481-489.
    • (1983) Eur J Biochem , vol.133 , pp. 481-489
    • Stephens, P.E.1    Darlinson, M.G.2    Lewis, H.M.3    Guest, J.R.4
  • 61
    • 0023042283 scopus 로고
    • Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F.W., and Moffatt, B.A. (1986) Use of the bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189: 113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 62
    • 0023571657 scopus 로고
    • High-copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- or kanamycin-resistance selection
    • Takeshita, S., Sato, M., Toba, M., Masahashi, W., and Hashimoto-Gotoh, T. (1987) High-copy-number and low-copy-number plasmid vectors for lacZ α-complementation and chloramphenicol- or kanamycin-resistance selection. Gene 61: 63-74.
    • (1987) Gene , vol.61 , pp. 63-74
    • Takeshita, S.1    Sato, M.2    Toba, M.3    Masahashi, W.4    Hashimoto-Gotoh, T.5
  • 63
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R.K., Jungermann, K., and Decker, K. (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41: 100-180.
    • (1977) Bacteriol Rev , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 65
    • 0028965949 scopus 로고
    • Phylogenetic placement of Dialister pneumosintes (formerly Bacteroides pneumosintes) within the Sporomusa subbranch of the Clostridium subphylum of the gram-positive bacteria
    • Willems, A., and Collins, M.D. (1995) Phylogenetic placement of Dialister pneumosintes (formerly Bacteroides pneumosintes) within the Sporomusa subbranch of the Clostridium subphylum of the gram-positive bacteria. Int J Syst Bacteriol 45: 403-405.
    • (1995) Int J Syst Bacteriol , vol.45 , pp. 403-405
    • Willems, A.1    Collins, M.D.2
  • 66
    • 0026495408 scopus 로고
    • Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium
    • Woehlke, G., Wifling, K., and Dimroth, P. (1992) Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium. J Biol Chem 267: 22798-22803. Appendix: Woehlke, G., Laussermair, E., Schwarz, E., Oesterhelt, D., Reinke, H., Beyreuther, K. and Dimroth, P. (1992) Sequence of the β-subunit of oxaloacetate decarboxylase from Salmonella typhimurium: a correction of the C-terminal part. J Biol Chem 267: 22804-22805.
    • (1992) J Biol Chem , vol.267 , pp. 22798-22803
    • Woehlke, G.1    Wifling, K.2    Dimroth, P.3
  • 67
    • 0026441329 scopus 로고
    • Sequence of the β-subunit of oxaloacetate decarboxylase from Salmonella typhimurium: A correction of the C-terminal part
    • Appendix
    • Woehlke, G., Wifling, K., and Dimroth, P. (1992) Sequence of the sodium ion pump oxaloacetate decarboxylase from Salmonella typhimurium. J Biol Chem 267: 22798-22803. Appendix: Woehlke, G., Laussermair, E., Schwarz, E., Oesterhelt, D., Reinke, H., Beyreuther, K. and Dimroth, P. (1992) Sequence of the β-subunit of oxaloacetate decarboxylase from Salmonella typhimurium: a correction of the C-terminal part. J Biol Chem 267: 22804-22805.
    • (1992) J Biol Chem , vol.267 , pp. 22804-22805
    • Woehlke, G.1    Laussermair, E.2    Schwarz, E.3    Oesterhelt, D.4    Reinke, H.5    Beyreuther, K.6    Dimroth, P.7
  • 68
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya
    • Woese, C.R., Kandler, O., and Wheelis, M.L. (1990) Towards a natural system of organisms: Proposal for the domains Archaea, Bacteria, and Eucarya. Proc Natl Acad Sci USA 87: 4576-4579.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 69
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors: Nucleotide sequences of M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors: nucleotide sequences of M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.