메뉴 건너뛰기




Volumn 63, Issue 3, 1997, Pages 1131-1138

Characterization of the genes encoding the three-component membrane- bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; CYTOCHROME C;

EID: 0031018070     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.63.3.1131-1138.1997     Document Type: Article
Times cited : (52)

References (42)
  • 1
    • 0001045654 scopus 로고
    • Purification and properties of particulate alcohol dehydrogenase from Acetobacter aceti
    • Adachi, O., E. Miyagawa, E. Shinagawa, K. Matsushita, and M. Ameyama. 1978. Purification and properties of particulate alcohol dehydrogenase from Acetobacter aceti. Agric. Biol. Chem. 42:2331-2340.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2331-2340
    • Adachi, O.1    Miyagawa, E.2    Shinagawa, E.3    Matsushita, K.4    Ameyama, M.5
  • 2
    • 0001045653 scopus 로고
    • Purification and characterization of particulate alcohol dehydrogenase from Gluconobacter suboxydans
    • Adachi, O., K. Tayama, E. Shinagawa, K. Matsushita, and M. Ameyama. 1978. Purification and characterization of particulate alcohol dehydrogenase from Gluconobacter suboxydans. Agric. Biol. Chem. 42:2045-2056.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2045-2056
    • Adachi, O.1    Tayama, K.2    Shinagawa, E.3    Matsushita, K.4    Ameyama, M.5
  • 3
    • 0000333511 scopus 로고
    • Purification and characterization of membrane-hound aldehyde dehydrogenase from Gluconobacter suboxydan
    • Adachi, O., K. Tayama, E. Shinagawa, K. Matsushita, and M. Ameyama. 1980. Purification and characterization of membrane-hound aldehyde dehydrogenase from Gluconobacter suboxydan. Agric. Biol. Chem. 44:503-515.
    • (1980) Agric. Biol. Chem. , vol.44 , pp. 503-515
    • Adachi, O.1    Tayama, K.2    Shinagawa, E.3    Matsushita, K.4    Ameyama, M.5
  • 5
    • 77957025803 scopus 로고
    • Alcohol dehydrogenase from acetic acid bacteria, membrane-bound
    • Ameyama, M., and O. Adachi. 1982. Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol. 89:450-457.
    • (1982) Methods Enzymol. , vol.89 , pp. 450-457
    • Ameyama, M.1    Adachi, O.2
  • 6
    • 0000388332 scopus 로고
    • Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound
    • Ameyama, M., and O. Adachi. 1982. Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol. 89:491-497.
    • (1982) Methods Enzymol. , vol.89 , pp. 491-497
    • Ameyama, M.1    Adachi, O.2
  • 7
    • 0000089402 scopus 로고
    • Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti
    • Ameyama, M., K. Osada, E. Shinagawa, K. Matsushita, and O. Adachi. 1981. Purification and characterization of aldehyde dehydrogenase of Acetobacter aceti. Agric. Biol. Chem. 45:1889-1890.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 1889-1890
    • Ameyama, M.1    Osada, K.2    Shinagawa, E.3    Matsushita, K.4    Adachi, O.5
  • 8
    • 85010145048 scopus 로고
    • Sugar- Oxidizing respiratory chain of Gluconobacter suboxydans. Evidence for a branched respiratory chain and characterization of respiratory chain-linked cytochromes
    • Ameyama, M., K. Matsushita, E. Shinagawa, and O. Adachi. 1987. Sugar-oxidizing respiratory chain of Gluconobacter suboxydans. Evidence for a branched respiratory chain and characterization of respiratory chain-linked cytochromes. Agric. Biol. Chem. 51:2943-2950.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2943-2950
    • Ameyama, M.1    Matsushita, K.2    Shinagawa, E.3    Adachi, O.4
  • 9
    • 0025369520 scopus 로고
    • Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxI genes involved in methanol oxidation
    • Anderson, D. J., C. J. Morris, D. N. Nunn, C. Anthony, and M. E. Lidstrom. 1990. Nucleotide sequence of the Methylobacterium extorquens AM1 moxF and moxI genes involved in methanol oxidation. Gene 90:173-176.
    • (1990) Gene , vol.90 , pp. 173-176
    • Anderson, D.J.1    Morris, C.J.2    Nunn, D.N.3    Anthony, C.4    Lidstrom, M.E.5
  • 10
    • 0026553672 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. 1992. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 20:2013-2018.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2013-2018
    • Bairoch, A.1
  • 11
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitro-cellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. 1981. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitro-cellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 12
    • 0023948011 scopus 로고
    • Nucleotide sequence of the gene coding for quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus
    • Cleton-Jansen, A.-M., N. Goosen, G. Odle, and P. van de Putte. 1988. Nucleotide sequence of the gene coding for quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus. Nucleic Acids Res. 16:6228.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6228
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Odle, G.3    Van De Putte, P.4
  • 13
    • 0025188604 scopus 로고
    • Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase
    • Cleton-Jansen, A.-M., N. Goosen, O. Fayet, and P. van de Putte. 1990. Cloning, mapping, and sequencing of the gene encoding Escherichia coli quinoprotein glucose dehydrogenase. J. Bacteriol. 172:6308-6315.
    • (1990) J. Bacteriol. , vol.172 , pp. 6308-6315
    • Cleton-Jansen, A.-M.1    Goosen, N.2    Fayet, O.3    Van De Putte, P.4
  • 14
    • 0000032248 scopus 로고
    • Key to the genera of the family Acetobacteraceae
    • N. R. Krieg and J. G. Holt (ed.). The Williams & Wilkins Co., Baltimore, Md.
    • De Ley, J., J. Swings, and F. Gosselé. 1984. Key to the genera of the family Acetobacteraceae, p. 268-278. In N. R. Krieg and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, vol. 1. The Williams & Wilkins Co., Baltimore, Md.
    • (1984) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 268-278
    • De Ley, J.1    Swings, J.2    Gosselé, F.3
  • 15
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and G. Begg. 1967. A protein sequenator. Eur. J. Biochem. 1:80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 16
    • 0024804727 scopus 로고
    • Purification and characterization of membrane-bound aldehyde dehydrogenase from Acetobacter polyoxogenes sp. nov.
    • Fukaya, M., K. Tayama, H. Okumura, Y. Kawamura, and T. Beppu. 1989. Purification and characterization of membrane-bound aldehyde dehydrogenase from Acetobacter polyoxogenes sp. nov. Appl. Microbiol. Biotechnol. 32:176-180.
    • (1989) Appl. Microbiol. Biotechnol. , vol.32 , pp. 176-180
    • Fukaya, M.1    Tayama, K.2    Okumura, H.3    Kawamura, Y.4    Beppu, T.5
  • 17
    • 0024586192 scopus 로고
    • Cloning of the membrane-hound aldehyde dehydrogenase gene of Acetobacter polyoxogenes and improvement of acetic acid production by use of the cloned gene
    • Fukaya, M., K. Tayama, T. Tamaki, H. Tagami, H. Okumura, Y. Kawamura, and T. Beppu. 1989. Cloning of the membrane-hound aldehyde dehydrogenase gene of Acetobacter polyoxogenes and improvement of acetic acid production by use of the cloned gene. Appl. Environ. Microbiol. 55:171-176.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 171-176
    • Fukaya, M.1    Tayama, K.2    Tamaki, T.3    Tagami, H.4    Okumura, H.5    Kawamura, Y.6    Beppu, T.7
  • 18
    • 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. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 19
    • 0024399336 scopus 로고
    • Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti
    • Inoue, T., M. Sunagawa, A. Mori, C. Imai, M. Fukuda, M. Takagi, and K. Yano. 1989. Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti. J. Bacteriol 171:3115-3122.
    • (1989) J. Bacteriol , vol.171 , pp. 3115-3122
    • Inoue, T.1    Sunagawa, M.2    Mori, A.3    Imai, C.4    Fukuda, M.5    Takagi, M.6    Yano, K.7
  • 20
    • 0026623341 scopus 로고
    • Nucleotide sequence of the gene encoding the 45-kilodalton subunit of alcohol dehydrogenase from Acetobacter aceti
    • Inoue, T., M. Sunagawa, A. Mori, C. Imai, M. Fukuda, M. Takagi, and K. Yano. 1992. Nucleotide sequence of the gene encoding the 45-kilodalton subunit of alcohol dehydrogenase from Acetobacter aceti. J. Ferment. Bioeng. 73:419-424.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 419-424
    • Inoue, T.1    Sunagawa, M.2    Mori, A.3    Imai, C.4    Fukuda, M.5    Takagi, M.6    Yano, K.7
  • 21
    • 0029148093 scopus 로고
    • Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the three-component membrane-hound alcohol dehydrogenase from Acetobacter pasteurianus
    • Kondo, K., T. Beppu, and S. Horinouchi. 1995. Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the three-component membrane-hound alcohol dehydrogenase from Acetobacter pasteurianus. J. Bacteriol. 177:5048-5055.
    • (1995) J. Bacteriol. , vol.177 , pp. 5048-5055
    • Kondo, K.1    Beppu, T.2    Horinouchi, S.3
  • 22
    • 2642699794 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotype selection
    • Kunkel, T. A. 1985. Rapid and efficient site-directed mutagenesis without phenotype selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 23
    • 0024233964 scopus 로고
    • Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12
    • Lahti, R., T. Pitkäranta, E. Valve, I. Ilta, E. Kukko-Kalske, and J. Heinonen. 1988. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. J. Bacteriol. 170:5901-5907.
    • (1988) J. Bacteriol. , vol.170 , pp. 5901-5907
    • Lahti, R.1    Pitkäranta, T.2    Valve, E.3    Ilta, I.4    Kukko-Kalske, E.5    Heinonen, J.6
  • 24
    • 0014105807 scopus 로고
    • Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe
    • Magnet, R. 1967. Mutants partially deficient in alcohol dehydrogenase in Schizosaccharomyces pombe. Arch. Biochem. Biophys. 121:194-201.
    • (1967) Arch. Biochem. Biophys. , vol.121 , pp. 194-201
    • Magnet, R.1
  • 25
    • 0002848216 scopus 로고
    • Ethanol oxidase respiratory chain of acetic acid bacteria: Reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans
    • Matsushita, K., Y. Takaki, E. Shinagawa, M. Ameyama, and O. Adachi. 1992. Ethanol oxidase respiratory chain of acetic acid bacteria: reactivity with ubiquinone of pyrroloquinoline quinone-dependent alcohol dehydrogenases purified from Acetobacter aceti and Gluconobacter suboxydans. Biosci. Biotechnol. Biochem. 56:304-310.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 304-310
    • Matsushita, K.1    Takaki, Y.2    Shinagawa, E.3    Ameyama, M.4    Adachi, O.5
  • 26
    • 0028872840 scopus 로고
    • Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans
    • Matsushita, K., T. Yakushi, Y. Takaki, H. Toyama, and O. Adachi. 1995. Generation mechanism and purification of an inactive form convertible in vivo to the active form of quinoprotein alcohol dehydrogenase in Gluconobacter suboxydans. J. Bacteriol. 177:6552-6559.
    • (1995) J. Bacteriol. , vol.177 , pp. 6552-6559
    • Matsushita, K.1    Yakushi, T.2    Takaki, Y.3    Toyama, H.4    Adachi, O.5
  • 27
    • 0029883559 scopus 로고    scopus 로고
    • Function of multiple heme c moieties in intramolecular electron transport and uhiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans
    • Matsushita, K., T. Yakushi, H. Toyama, E. Shinagawa, and O. Adachi. 1996. Function of multiple heme c moieties in intramolecular electron transport and uhiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem. 271: 4850-4857.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4850-4857
    • Matsushita, K.1    Yakushi, T.2    Toyama, H.3    Shinagawa, E.4    Adachi, O.5
  • 28
    • 0020453669 scopus 로고
    • New perspectives on c-type cytochromes
    • Meyer, T. E., and M. D. Kamen. 1982. New perspectives on c-type cytochromes. Adv. Protein Chem. 35:105-212.
    • (1982) Adv. Protein Chem. , vol.35 , pp. 105-212
    • Meyer, T.E.1    Kamen, M.D.2
  • 29
    • 0001740754 scopus 로고
    • Construction of plasmid vector and genetic transformation system for Acetobacter aceti
    • Okumura, H., T. Uozumi, and T. Beppu. 1985. Construction of plasmid vector and genetic transformation system for Acetobacter aceti. Agric. Biol. Chem. 490:1011-1017.
    • (1985) Agric. Biol. Chem. , vol.490 , pp. 1011-1017
    • Okumura, H.1    Uozumi, T.2    Beppu, T.3
  • 30
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg, M., and D. Court. 1979. Regulatory sequences involved in the promotion and termination of RNA transcription. Annu. Rev. Genet. 13: 319-353.
    • (1979) Annu. Rev. Genet. , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 33
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosomal binding sites
    • Shine, J., and L. Dalgarno. 1974. The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosomal 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, L.2
  • 34
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 35
    • 0025816967 scopus 로고
    • Cloning and sequencing of the gene encoding cytochrome c-553 (CO) from Gluconobacter suboxydans
    • Takeda, Y., and T. Shimizu. 1991. Cloning and sequencing of the gene encoding cytochrome c-553 (CO) from Gluconobacter suboxydans. J. Ferment. Bioeng. 72:1-6.
    • (1991) J. Ferment. Bioeng. , vol.72 , pp. 1-6
    • Takeda, Y.1    Shimizu, T.2
  • 36
    • 0026589312 scopus 로고
    • Expression of cytochrome c-553 (CO) gene that complements the second subunit deficiency of membrane-bound alcohol dehydrogenase in Gluconobacter suboxydans subsp. α
    • Takeda, Y., and T. Shimizu. 1992. Expression of cytochrome c-553 (CO) gene that complements the second subunit deficiency of membrane-bound alcohol dehydrogenase in Gluconobacter suboxydans subsp. α. J. Ferment. Bioeng. 73:89-93.
    • (1992) J. Ferment. Bioeng. , vol.73 , pp. 89-93
    • Takeda, Y.1    Shimizu, T.2
  • 37
    • 0027428003 scopus 로고
    • Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus
    • Takemura, H., K. Kondo, S. Horinouchi, and T. Beppu. 1993. Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus. J. Bacteriol. 175:6857-6866.
    • (1993) J. Bacteriol. , vol.175 , pp. 6857-6866
    • Takemura, H.1    Kondo, K.2    Horinouchi, S.3    Beppu, T.4
  • 39
    • 0024847259 scopus 로고
    • Purification and characterization of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes sp. nov.
    • Tayama, K., M. Fukaya, H. Okumura, Y. Kawamura, and T. Beppu. 1989. Purification and characterization of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes sp. nov. Appl. Microbiol. Biotechnol. 32:181-185.
    • (1989) Appl. Microbiol. Biotechnol. , vol.32 , pp. 181-185
    • Tayama, K.1    Fukaya, M.2    Okumura, H.3    Kawamura, Y.4    Beppu, T.5
  • 40
    • 0021856417 scopus 로고
    • Signal sequence, the limits of variation
    • von Heijne, G. 1985. Signal sequence, the limits of variation. J. Mol. Biol. 184:99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 42
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.