메뉴 건너뛰기




Volumn 73, Issue 20, 2007, Pages 6551-6556

Membrane-bound, 2-keto-D-gluconate-yielding D-gluconate dehydrogenase from "Gluconobacter dioxyacetonicus" IFO 3271: Molecular properties and gene disruption

Author keywords

[No Author keywords available]

Indexed keywords

FERRICYANIDE REDUCTASE ACTIVITY; LACTONASE; MOLECULAR PROPERTIES;

EID: 35449004453     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00493-07     Document Type: Article
Times cited : (38)

References (25)
  • 1
    • 0013147865 scopus 로고
    • 33] 5-Keto-D-gluconate reductase from Gluconobacter suboxydans
    • Ameyama, M., O. Adachi, and A. W. Willis. 1982. [33] 5-Keto-D-gluconate reductase from Gluconobacter suboxydans. Methods Enzymol. 89:198-202.
    • (1982) Methods Enzymol , vol.89 , pp. 198-202
    • Ameyama, M.1    Adachi, O.2    Willis, A.W.3
  • 2
    • 0013098708 scopus 로고
    • 34] 2-Keto-D-gluconate reductase from acetic acid bacteria
    • Ameyama, M., O. Adachi, and A. W. Willis. 1982. [34] 2-Keto-D-gluconate reductase from acetic acid bacteria. Methods Enzymol. 89:203-210.
    • (1982) Methods Enzymol , vol.89 , pp. 203-210
    • Ameyama, M.1    Adachi, O.2    Willis, A.W.3
  • 4
    • 0016642871 scopus 로고
    • A simple technique for eliminating interference by detergents in the Lowry method of protein determination
    • Dulley, J. R., and P. A. Grieve. 1975. A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem. 64:136-141.
    • (1975) Anal. Biochem , vol.64 , pp. 136-141
    • Dulley, J.R.1    Grieve, P.A.2
  • 6
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 7
    • 0033943049 scopus 로고    scopus 로고
    • Escherichia coli translocase: The unravelling of a molecular machine
    • Manting, E. H., and A. J. Driessen. 2000. Escherichia coli translocase: the unravelling of a molecular machine. Mol. Microbiol. 37:226-238.
    • (2000) Mol. Microbiol , vol.37 , pp. 226-238
    • Manting, E.H.1    Driessen, A.J.2
  • 8
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from micro-organisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol. 3:208-218.
    • (1961) J. Mol. Biol , vol.3 , pp. 208-218
    • Marmur, J.1
  • 10
    • 0037393281 scopus 로고    scopus 로고
    • Matsushita, K., Y. Fujii, Y. Ano, H. Toyama, M. Shinjoh, N. Tomiyama, T. Miyazaki, T. Sugisawa, T. Hoshino, and O. Adachi. 2003. 5-Keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species. Appl. Environ. Microbiol. 69:1959-1966.
    • Matsushita, K., Y. Fujii, Y. Ano, H. Toyama, M. Shinjoh, N. Tomiyama, T. Miyazaki, T. Sugisawa, T. Hoshino, and O. Adachi. 2003. 5-Keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species. Appl. Environ. Microbiol. 69:1959-1966.
  • 11
    • 0020390361 scopus 로고    scopus 로고
    • Matsushita, K., E. Shinagawa, and M. Ameyama. 1982. D-Gluconate dehydrogenase from bacteria, 2-keto-D-gluconate- yielding, membrane-bound. Methods Enzymol. 89:187-193.
    • Matsushita, K., E. Shinagawa, and M. Ameyama. 1982. D-Gluconate dehydrogenase from bacteria, 2-keto-D-gluconate- yielding, membrane-bound. Methods Enzymol. 89:187-193.
  • 12
    • 0028202832 scopus 로고
    • Respiratory chains and bioenergetics of acetic acid bacteria
    • Matsushita, K., H. Toyama, and O. Adachi. 1994. Respiratory chains and bioenergetics of acetic acid bacteria. Adv. Microb. Physiol. 36:247-301.
    • (1994) Adv. Microb. Physiol , vol.36 , pp. 247-301
    • Matsushita, K.1    Toyama, H.2    Adachi, O.3
  • 13
    • 0032942617 scopus 로고    scopus 로고
    • The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site
    • Matsushita, K., T. Yakushi, H. Toyama, O. Adachi, H. Miyoshi, E. Tagami, and K. Sakamoto, 1999. The quinohemoprotein alcohol dehydrogenase of Gluconobacter suboxydans has ubiquinol oxidation activity at a site different from the ubiquinone reduction site. Biochim. Biophys. Acta 1409:154-164.
    • (1999) Biochim. Biophys. Acta , vol.1409 , pp. 154-164
    • Matsushita, K.1    Yakushi, T.2    Toyama, H.3    Adachi, O.4    Miyoshi, H.5    Tagami, E.6    Sakamoto, K.7
  • 14
    • 0022401751 scopus 로고
    • Identification of the covalently bound flavins of D-gluconate dehydrogenases from Pseudomonas aeruginosa and Pseudomonas fluoresces and of 2-keto-D-gluconate dehydrogenase from Gluconobacter melanogenus
    • McIntire, W., T. P. Singer, M. Ameyama, O. Adachi, K. Matsushita, and E. Shinagawa. 1985. Identification of the covalently bound flavins of D-gluconate dehydrogenases from Pseudomonas aeruginosa and Pseudomonas fluoresces and of 2-keto-D-gluconate dehydrogenase from Gluconobacter melanogenus. Biochem. J. 231:651-654.
    • (1985) Biochem. J , vol.231 , pp. 651-654
    • McIntire, W.1    Singer, T.P.2    Ameyama, M.3    Adachi, O.4    Matsushita, K.5    Shinagawa, E.6
  • 16
    • 0028828710 scopus 로고
    • New plasmids carrying antibiotic-resistance cassettes
    • Reece, K. S., and G. J. Phillips. 1995. New plasmids carrying antibiotic-resistance cassettes. Gene 165:141-142.
    • (1995) Gene , vol.165 , pp. 141-142
    • Reece, K.S.1    Phillips, G.J.2
  • 17
    • 15244352843 scopus 로고    scopus 로고
    • Characterisation of a secondary alcohol dehydrogenase from Xanthomonas campestris DSM 3586
    • Salusjarvi, T., N. Hvorslev, and A. N. Miasnikov. 2005. Characterisation of a secondary alcohol dehydrogenase from Xanthomonas campestris DSM 3586. Appl. Microbiol. Biotechnol. 66:664-667.
    • (2005) Appl. Microbiol. Biotechnol , vol.66 , pp. 664-667
    • Salusjarvi, T.1    Hvorslev, N.2    Miasnikov, A.N.3
  • 18
    • 4544236547 scopus 로고    scopus 로고
    • Cloning of a gluconate/polyol dehydrogenase gene from Gluconobacter suboxydans IFO 12528, characterisation of the enzyme and its use for the production of 5-ketogluconate in a recombinant Escherichia coli strain
    • Salusjarvi, T., M. Povelainen, N. Hvorslev, E. V. Eneyskaya, A. A. Kulminskaya, K. A. Shabalin, K. N. Neustroev, N. Kalkkinen, and A. N. Miasnikov. 2004. Cloning of a gluconate/polyol dehydrogenase gene from Gluconobacter suboxydans IFO 12528, characterisation of the enzyme and its use for the production of 5-ketogluconate in a recombinant Escherichia coli strain. Appl. Microbiol. Biotechnol. 65:306-314.
    • (2004) Appl. Microbiol. Biotechnol , vol.65 , pp. 306-314
    • Salusjarvi, T.1    Povelainen, M.2    Hvorslev, N.3    Eneyskaya, E.V.4    Kulminskaya, A.A.5    Shabalin, K.A.6    Neustroev, K.N.7    Kalkkinen, N.8    Miasnikov, A.N.9
  • 20
    • 0032620031 scopus 로고    scopus 로고
    • Identification of covalent flavoproteins and analysis of the covalent link
    • Scrutton, N. S. 1999. Identification of covalent flavoproteins and analysis of the covalent link. Methods Mol. Biol. 131:181-193.
    • (1999) Methods Mol. Biol , vol.131 , pp. 181-193
    • Scrutton, N.S.1
  • 21
    • 85024302160 scopus 로고    scopus 로고
    • Shinagawa, E., K. Matsushita, O. Adachi, and M. Ameyama. 1984. D-Gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: purification and characterization. Agric. Biol. Chem. 48:1517-1522.
    • Shinagawa, E., K. Matsushita, O. Adachi, and M. Ameyama. 1984. D-Gluconate dehydrogenase, 2-keto-D-gluconate yielding, from Gluconobacter dioxyacetonicus: purification and characterization. Agric. Biol. Chem. 48:1517-1522.
  • 22
    • 0000495847 scopus 로고
    • Selective production of 5-keto-D-gluconate by Gluconobacter strains
    • Shinagawa, E., K. Matsushita, O. Adachi, and M. Ameyama. 1983. Selective production of 5-keto-D-gluconate by Gluconobacter strains. J. Ferment. Technol. 61:359-363.
    • (1983) J. Ferment. Technol , vol.61 , pp. 359-363
    • Shinagawa, E.1    Matsushita, K.2    Adachi, O.3    Ameyama, M.4
  • 23
    • 28644434662 scopus 로고    scopus 로고
    • White biotechnology for green chemistry: Fermentative 2-oxocarboxylic acids as novel building blocks for subsequent chemical syntheses
    • Stottmeister, U., A. Aurich, H. Wilde, J. Andersch, S. Schmidt, and D. Sicker. 2005. White biotechnology for green chemistry: fermentative 2-oxocarboxylic acids as novel building blocks for subsequent chemical syntheses. J. Ind. Microbiol. Biotechnol. 32:651-664.
    • (2005) J. Ind. Microbiol. Biotechnol , vol.32 , pp. 651-664
    • Stottmeister, U.1    Aurich, A.2    Wilde, H.3    Andersch, J.4    Schmidt, S.5    Sicker, D.6
  • 24
    • 22444441792 scopus 로고    scopus 로고
    • Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand
    • Toyama, H., W. Soemphol, D. Moonmangmee, O. Adachi, and K. Matsushita. 2005. Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand. Biosci. Biotechnol. Biochem. 69:1120-1129.
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1120-1129
    • Toyama, H.1    Soemphol, W.2    Moonmangmee, D.3    Adachi, O.4    Matsushita, K.5
  • 25
    • 0030668086 scopus 로고    scopus 로고
    • Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli
    • Yum, D. Y., Y. P. Lee, and J. G. Pan. 1997. Cloning and expression of a gene cluster encoding three subunits of membrane-bound gluconate dehydrogenase from Erwinia cypripedii ATCC 29267 in Escherichia coli. J. Bacteriol. 179:6566-6572.
    • (1997) J. Bacteriol , vol.179 , pp. 6566-6572
    • Yum, D.Y.1    Lee, Y.P.2    Pan, J.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.