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Volumn 178, Issue 3, 1996, Pages 871-880

Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; COENZYME A; COENZYME A TRANSFERASE; DNA; GENE PRODUCT; HYDROXYBUTYRATE DEHYDROGENASE; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RNA; SIGMA FACTOR; SUCCINATE DEHYDROGENASE; SUCCINIC ACID;

EID: 0030047157     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.3.871-880.1996     Document Type: Article
Times cited : (87)

References (61)
  • 1
    • 0018936601 scopus 로고
    • Utilization of (E)-2-butenoate (crotonate) by Clostridium kluyveri and some other Clostridium species
    • Bader, J., H. Günther, H. Simon, S. Pohl, and W. Mannheim. 1980. Utilization of (E)-2-butenoate (crotonate) by Clostridium kluyveri and some other Clostridium species. Arch. Microbiol 125:159-165.
    • (1980) Arch. Microbiol , vol.125 , pp. 159-165
    • Bader, J.1    Günther, H.2    Simon, H.3    Pohl, S.4    Mannheim, W.5
  • 2
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. 1991. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 19(Suppl.):2241-2245.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.SUPPL. , pp. 2241-2245
    • Bairoch, A.1
  • 3
    • 0011916014 scopus 로고
    • Clostridium kluyveri, an organism concerned in the formation of caproic acid from ethyl alcohol
    • Barker, H. A. 1942. Clostridium kluyveri, an organism concerned in the formation of caproic acid from ethyl alcohol J Biol Chem. 43:347-363.
    • (1942) J Biol Chem. , vol.43 , pp. 347-363
    • Barker, H.A.1
  • 4
    • 0003144833 scopus 로고
    • A vinylacetyl isomerase from Clostridium kluyveri
    • Bartsch, R. G., and H. A. Barker. 1961. A vinylacetyl isomerase from Clostridium kluyveri Arch Biochem. Biophys. 92:122-132.
    • (1961) Arch Biochem. Biophys. , vol.92 , pp. 122-132
    • Bartsch, R.G.1    Barker, H.A.2
  • 5
    • 0345176212 scopus 로고
    • Phosphotrans-acetylase aus Clostridium khyveri. Zuchtung des Bakteriums, Isolierung, Kristallisation und Eigenschaften des Enzyms
    • Bergmeyer, H. U., G. Holz, H. Klotzsch, and G. Lang. 1963. Phosphotrans-acetylase aus Clostridium khyveri. Zuchtung des Bakteriums, Isolierung, Kristallisation und Eigenschaften des Enzyms. Biochem. Z. 338:114-121.
    • (1963) Biochem. Z. , vol.338 , pp. 114-121
    • Bergmeyer, H.U.1    Holz, G.2    Klotzsch, H.3    Lang, G.4
  • 6
    • 0017687507 scopus 로고
    • Generalized indicator plate for genetic, metabolic, and taxonomic studies with microorganisms
    • Bochner, B. R., and M. A. Savageau. 1977 Generalized indicator plate for genetic, metabolic, and taxonomic studies with microorganisms. Appl. Environ Microbiol. 33:434-444.
    • (1977) Appl. Environ Microbiol. , vol.33 , pp. 434-444
    • Bochner, B.R.1    Savageau, M.A.2
  • 7
    • 0001433764 scopus 로고
    • The energy metabolism of Clostridium kluyveri and the synthesis of fatty acids
    • Bornstein, B. T., and H. A. Barker. 1948. The energy metabolism of Clostridium kluyveri and the synthesis of fatty acids. J. Biol. Chem. 172:659-669.
    • (1948) J. Biol. Chem. , vol.172 , pp. 659-669
    • Bornstein, B.T.1    Barker, H.A.2
  • 8
    • 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
  • 9
    • 0024723183 scopus 로고
    • The fermentation pathways of Escherichia coli
    • Clark, D. P. 1989. The fermentation pathways of Escherichia coli. FEMS Microbiol Rev. 63:223-234.
    • (1989) FEMS Microbiol Rev. , vol.63 , pp. 223-234
    • Clark, D.P.1
  • 10
    • 0024342310 scopus 로고
    • Similarity of Escherithia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae
    • Conway, T., and L. O. Ingram. 1989. Similarity of Escherithia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J Bacteriol 171:3754-3759.
    • (1989) J Bacteriol , vol.171 , pp. 3754-3759
    • Conway, T.1    Ingram, L.O.2
  • 11
    • 0023267608 scopus 로고
    • Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis
    • Conway, T., G. W. Sewell, Y. A. Osman, and L. O. Ingram. 1987. Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis J Bacteriol. 169:2591-2597.
    • (1987) J Bacteriol. , vol.169 , pp. 2591-2597
    • Conway, T.1    Sewell, G.W.2    Osman, Y.A.3    Ingram, L.O.4
  • 12
    • 0028962143 scopus 로고    scopus 로고
    • Purification of 1,3-propanediol dehydrogenase from Citrobacter freundu: Sequencing and overexpression of the corresponding gene in Escherichia coli
    • Daniel, R., and G. Gottschalk. Purification of 1,3-propanediol dehydrogenase from Citrobacter freundu: sequencing and overexpression of the corresponding gene in Escherichia coli. J. Bacteriol 177:2151-2156.
    • J. Bacteriol , vol.177 , pp. 2151-2156
    • Daniel, R.1    Gottschalk, G.2
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devreux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX Nucleic Acids Res. 12:387-395
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devreux, J.1    Haeberli, P.2    Smithies, O.3
  • 14
    • 0026730941 scopus 로고
    • Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene
    • De Vries, G. E., N. Arfman, P. Terpstra, and L. Dijkhuizen. 1992 Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene. J. Bactenol. 174:5346-5353.
    • (1992) J. Bactenol. , vol.174 , pp. 5346-5353
    • De Vries, G.E.1    Arfman, N.2    Terpstra, P.3    Dijkhuizen, L.4
  • 15
    • 0019459218 scopus 로고
    • Two sucemic semialdehyde dehydrogenases are induced when Escherichia coli K-12 is grown on γ-aminobutyrate
    • Donnelly, M. I., and R. A. Cooper. 1981. Two sucemic semialdehyde dehydrogenases are induced when Escherichia coli K-12 is grown on γ-aminobutyrate. J Bacteriol 145:1425-1427
    • (1981) J Bacteriol , vol.145 , pp. 1425-1427
    • Donnelly, M.I.1    Cooper, R.A.2
  • 16
    • 0027383357 scopus 로고
    • Cloning, sequencing and molecular analysis of the sol operon of Clostridium acetobutylicum, a chromosomal locus involved m solventogenesis
    • Fischer, R. J., J. Helms, and P, Dürre. 1993 Cloning, sequencing and molecular analysis of the sol operon of Clostridium acetobutylicum, a chromosomal locus involved m solventogenesis. J. Bacteriol. 175:6959-6969.
    • (1993) J. Bacteriol. , vol.175 , pp. 6959-6969
    • Fischer, R.J.1    Helms, J.2    Dürre, P.3
  • 18
    • 0025694980 scopus 로고
    • Cloning, sequencing, and molecular analysis of the acetoacctate decarboxylase gene region from Clostridium acetobutylicum
    • Gerischer, U., and P. Dürre. 1990. Cloning, sequencing, and molecular analysis of the acetoacctate decarboxylase gene region from Clostridium acetobutylicum J. Bacteriol. 172:6907-6918
    • (1990) J. Bacteriol. , vol.172 , pp. 6907-6918
    • Gerischer, U.1    Dürre, P.2
  • 19
    • 0026531061 scopus 로고
    • mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis
    • Gerischer, U., and P. Dürre. 1992. mRNA analysis of the adc gene region of Clostridium acetobutylicum during the shift to solventogenesis. J. Bacteriol. 174:426-433.
    • (1992) J. Bacteriol. , vol.174 , pp. 426-433
    • Gerischer, U.1    Dürre, P.2
  • 20
    • 0024849185 scopus 로고
    • Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli
    • Goodlove, P. E., P. R. Cunningham, J. Parker, and D. P. Clark. 1989. Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene 85:209-214
    • (1989) Gene , vol.85 , pp. 209-214
    • Goodlove, P.E.1    Cunningham, P.R.2    Parker, J.3    Clark, D.P.4
  • 22
    • 0008287085 scopus 로고
    • γ-Hydroxybutyrate dehydrogenase from Clostridium aminobutyricum
    • Hardman, J. K. 1962. γ-Hydroxybutyrate dehydrogenase from Clostridium aminobutyricum Methods Enzymol. 5:778-783.
    • (1962) Methods Enzymol. , vol.5 , pp. 778-783
    • Hardman, J.K.1
  • 23
    • 0024549056 scopus 로고
    • Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinome and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treatedl liver, distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria
    • Hempel, J., K. Harper, and R. Lindahl. 1989. Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinome and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treatedl liver, distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria. Biochemistry 28:1160-1167.
    • (1989) Biochemistry , vol.28 , pp. 1160-1167
    • Hempel, J.1    Harper, K.2    Lindahl, R.3
  • 24
    • 0026052705 scopus 로고
    • Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase
    • Hidalgo, E., Y.-M. Chen, E. C. C. Lin, and J. Aguilar. 1991. Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase. J. Bacteriol. 173:6118-6123.
    • (1991) J. Bacteriol. , vol.173 , pp. 6118-6123
    • Hidalgo, E.1    Chen, Y.-M.2    Lin, E.C.C.3    Aguilar, J.4
  • 25
    • 0011425509 scopus 로고
    • Aldehyde dehydrogenases
    • P. D. Boyer (ed.). Academic Press, New York
    • Jakoby, W. B. 1963 Aldehyde dehydrogenases, p. 203-221 In P. D. Boyer (ed.). The enzymes, 2nd ed , vol. 7. Academic Press, New York.
    • (1963) The Enzymes, 2nd Ed , vol.7 , pp. 203-221
    • Jakoby, W.B.1
  • 26
    • 0023411028 scopus 로고
    • Characteristics of alcohol/ polyol dehydrogenases. The zinc-containing long-chain alcohol-dehydrogenases
    • Jornvall, H., B. Persson, and J. Jeffery. 1987. Characteristics of alcohol/ polyol dehydrogenases. The zinc-containing long-chain alcohol-dehydrogenases Eur. J. Biochem. 167:195-201
    • (1987) Eur. J. Biochem. , vol.167 , pp. 195-201
    • Jornvall, H.1    Persson, B.2    Jeffery, J.3
  • 27
    • 0021905346 scopus 로고
    • Studies on the substrate range of Clostridium kluyveri: The use of propanol and succinate
    • Kenealy, W. R., and D, M. Waselefsky. 1985. Studies on the substrate range of Clostridium kluyveri: the use of propanol and succinate. Arch. Microbiol. 141:187-194.
    • (1985) Arch. Microbiol. , vol.141 , pp. 187-194
    • Kenealy, W.R.1    Waselefsky, D.M.2
  • 28
    • 0025972739 scopus 로고
    • Pyruvate-formate-lyase-de-activase and acelyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE
    • Kessler, D., I. Leibrecht, and J. Knappe. 1991. Pyruvate-formate-lyase-de-activase and acelyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE. FEBS Lett. 281:59-63.
    • (1991) FEBS Lett. , vol.281 , pp. 59-63
    • Kessler, D.1    Leibrecht, I.2    Knappe, J.3
  • 29
    • 0026706351 scopus 로고
    • Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic archaeum Desulfurolobus ambivalens
    • Kletzin, A. 1992 Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic archaeum Desulfurolobus ambivalens. J. Bacteriol. 174:5854-5859
    • (1992) J. Bacteriol. , vol.174 , pp. 5854-5859
    • Kletzin, A.1
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. Mol Biol. 157:105-132.
    • (1982) Mol Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0025276123 scopus 로고
    • A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces cerevistae
    • Lee, F.-J. S., L.-W. Lin, and J. A. Smith. 1990. A glucose-repressible gene encodes acetyl-CoA hydrolase from Saccharomyces cerevistae. J. Biol. Chem. 265:7413-7418.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7413-7418
    • Lee, F.-J.S.1    Lin, L.-W.2    Smith, J.A.3
  • 32
    • 0026565685 scopus 로고
    • Sequence of a cDNA clone encoding pig heart mitochondrial CoA transferase
    • Lin, T., and W. A. Bridger. 1992 Sequence of a cDNA clone encoding pig heart mitochondrial CoA transferase. J. Biol. Chem. 267:975-978.
    • (1992) J. Biol. Chem. , vol.267 , pp. 975-978
    • Lin, T.1    Bridger, W.A.2
  • 33
    • 0018361778 scopus 로고
    • Electron microscopic study on the quarternary structure of the isolated particulate alcohol-acetaldehyde dehydrogenase complex and on its identity with the polygonal bodies of Clostridium kluyveri
    • Lurz, R., F. Mayer, and G. Gottschalk. 1979. Electron microscopic study on the quarternary structure of the isolated particulate alcohol-acetaldehyde dehydrogenase complex and on its identity with the polygonal bodies of Clostridium kluyveri. Arch. Microbiol. 120:255-262
    • (1979) Arch. Microbiol. , vol.120 , pp. 255-262
    • Lurz, R.1    Mayer, F.2    Gottschalk, G.3
  • 34
    • 0025352675 scopus 로고
    • Duplication-induced mutation of a new Neurospora gene required for acetate utilization: Properties of the mutant and predicted amino acid sequence of the protein product
    • Marathe, S., I. F. Connerton, and J. R. S. Fincham. 1990. Duplication-induced mutation of a new Neurospora gene required for acetate utilization: properties of the mutant and predicted amino acid sequence of the protein product. Mol. Cell. Biol. 10:2638-2644.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2638-2644
    • Marathe, S.1    Connerton, I.F.2    Fincham, J.R.S.3
  • 35
    • 0027957210 scopus 로고
    • Molecular characterization of an aldehyde/alcohol dehydrogenase gene from C. acetobutylicum ATCC 824
    • Nair, R. V., G. N. Bennett, and E. T. Papoutsakis. 1994. Molecular characterization of an aldehyde/alcohol dehydrogenase gene from C. acetobutylicum ATCC 824. J. Bacteriol. 176:871-885.
    • (1994) J. Bacteriol. , vol.176 , pp. 871-885
    • Nair, R.V.1    Bennett, G.N.2    Papoutsakis, E.T.3
  • 36
    • 0023898663 scopus 로고
    • Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium ucetobutylicum
    • Palosaari, N. R., and P. Rogers. 1988. Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium ucetobutylicum. J. Bacteriol. 170:2971-2976.
    • (1988) J. Bacteriol. , vol.170 , pp. 2971-2976
    • Palosaari, N.R.1    Rogers, P.2
  • 37
    • 0026750750 scopus 로고
    • Characterization of the genes encoding β-ketoadipate:succinyl-coenzyme a transferase in Pseudomonas putida
    • Parales, R. E., and C. S. Harwood. 1992. Characterization of the genes encoding β-ketoadipate:succinyl-coenzyme A transferase in Pseudomonas putida J. Bacteriol. 174:4657-4666.
    • (1992) J. Bacteriol. , vol.174 , pp. 4657-4666
    • Parales, R.E.1    Harwood, C.S.2
  • 38
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 39
    • 0022555852 scopus 로고
    • Transcription termination and the regulation of gene expression
    • Platt, T. 1986. Transcription termination and the regulation of gene expression. Annu. Rev. Biochem. 55:339-372.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 339-372
    • Platt, T.1
  • 40
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • Reid, M. F., and C. A. Fewson. 1994 Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol. 20:13-35.
    • (1994) Crit. Rev. Microbiol. , vol.20 , pp. 13-35
    • Reid, M.F.1    Fewson, C.A.2
  • 41
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H., and K. I. Miura. 1963 Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim. Biophys. Acta 72:619-629.
    • (1963) Biochim. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.I.2
  • 44
    • 0025780688 scopus 로고
    • Purification and properties of 4-hydroxybutyrate coenzyme a transferase from Clustridium aminobutyricum
    • Scherf, U., and W. Buckel. 1991 Purification and properties of 4-hydroxybutyrate coenzyme A transferase from Clustridium aminobutyricum. Appl. Environ. Microbiol. 57:2699-2702.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2699-2702
    • Scherf, U.1    Buckel, W.2
  • 46
    • 0014657017 scopus 로고
    • Considerations on the energy metabolism of Clostridium kluyveri
    • Schoberth, S., and G. Gottschalk. 1969. Considerations on the energy metabolism of Clostridium kluyveri. Arch Microbiol 65:318-328.
    • (1969) Arch Microbiol , vol.65 , pp. 318-328
    • Schoberth, S.1    Gottschalk, G.2
  • 47
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J., and I., Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad Sci. USA 71:1342-1346.
    • (1974) Proc. Natl. Acad Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, I.2
  • 48
    • 0019125267 scopus 로고
    • Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri
    • Smith, L. T., and N. O. Kaplan. 1980. Purification, properties, and kinetic mechanism of coenzyme A-linked aldehyde dehydrogenase from Clostridium kluyveri. Arch. Biochem. Biophys. 203:663-675.
    • (1980) Arch. Biochem. Biophys. , vol.203 , pp. 663-675
    • Smith, L.T.1    Kaplan, N.O.2
  • 49
    • 0027400198 scopus 로고
    • Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri
    • Söhling, B., and G. Gottschalk. 1993. Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur J. Biochem 212:121-127.
    • (1993) Eur J. Biochem , vol.212 , pp. 121-127
    • Söhling, B.1    Gottschalk, G.2
  • 51
    • 0026563908 scopus 로고
    • Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes
    • Walter, K. A., G. N. Bennett, and E. T. Papoutsakis. 1992 Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes. J. Bacteriol. 174:7149-7158.
    • (1992) J. Bacteriol. , vol.174 , pp. 7149-7158
    • Walter, K.A.1    Bennett, G.N.2    Papoutsakis, E.T.3
  • 52
    • 0024465134 scopus 로고
    • The molecular mechanism of phase variation of H influenzae lipopolysaccharide
    • Weiser, J. N., J. M. Love, and E. R. Moxon. 1989. The molecular mechanism of phase variation of H influenzae lipopolysaccharide. Cell 59:657-665.
    • (1989) Cell , vol.59 , pp. 657-665
    • Weiser, J.N.1    Love, J.M.2    Moxon, E.R.3
  • 53
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpstra, and W. G. J. Hol. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint J Mol. Biol 187:101-107.
    • (1986) J Mol. Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 54
    • 0023404237 scopus 로고
    • Homology of the Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis
    • Williamson, V. M., and C. E. Paquin. 1987. Homology of the Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis. Mol. Gen. Genet 209:374-381.
    • (1987) Mol. Gen. Genet , vol.209 , pp. 374-381
    • Williamson, V.M.1    Paquin, C.E.2
  • 55
    • 0027311122 scopus 로고
    • Dehydrogenases involved in the conversion of succinate to 4-hydroxybutanoate by Clostridium kluyveri
    • Wolff, R. A., G. W. Urben, S. M. O'Herrin, and W. R. Kenealy. 1993. Dehydrogenases involved in the conversion of succinate to 4-hydroxybutanoate by Clostridium kluyveri. Appl Environ. Microbiol. 59:1876-1882.
    • (1993) Appl Environ. Microbiol. , vol.59 , pp. 1876-1882
    • Wolff, R.A.1    Urben, G.W.2    O'Herrin, S.M.3    Kenealy, W.R.4
  • 56
    • 0025144306 scopus 로고
    • Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592
    • Yan, R.-T., and J.-S. Chen. 1990. Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592. Appl. Environ. Microbiol. 56:2591-2599.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2591-2599
    • Yan, R.-T.1    Chen, J.-S.2
  • 57
    • 0028356258 scopus 로고
    • Entamoeba lustolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli
    • Yang, W., E. Li, T. Kairong, and S. L. Stanley, Jr. 1994. Entamoeba lustolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol Biochem. Parasitol. 64:253-260.
    • (1994) Mol Biochem. Parasitol. , vol.64 , pp. 253-260
    • Yang, W.1    Li, E.2    Kairong, T.3    Stanley Jr., S.L.4
  • 58
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the 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
  • 59
    • 0025037686 scopus 로고
    • Nucleotide sequence of the Zymomonas mobilis alcohol dehydrogenase II gene
    • Yoon, K. H., and M. Y. Pack. 1990. Nucleotide sequence of the Zymomonas mobilis alcohol dehydrogenase II gene. Nucleic Acids Res. 18:187.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 187
    • Yoon, K.H.1    Pack, M.Y.2
  • 61
    • 0024342186 scopus 로고
    • Molecular analysis and nucleotide sequence of the adh1 gene encoding an NADPH-dependent butanol dehydrogenase in the gram-positive anaerobe Clostridium acetobutylicum
    • Youngleson, J. S., W. A. Jones, D. T. Jones, and D. R. Woods. 1989. Molecular analysis and nucleotide sequence of the adh1 gene encoding an NADPH-dependent butanol dehydrogenase in the gram-positive anaerobe Clostridium acetobutylicum. Gene 78:355-364.
    • (1989) Gene , vol.78 , pp. 355-364
    • Youngleson, J.S.1    Jones, W.A.2    Jones, D.T.3    Woods, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.