Effect of growth substrates on formation of alcohol dehydrogenase in Acetobacter methanolicus and Acetobacter aceti

Journal of Fermentation and Bioengineering

Volumn 83, Issue 1, 1997, Pages 21-25

  Frébortová, Jitka ^a   Matsushita, Kazunobu ^a   Adachi, Osao ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

Author keywords

Acetobacter; alcohol dehydrogenase; carbon source; quinoprotein

Indexed keywords

ACETIC ACID; BACTERIA; CATALYST ACTIVITY; COMPOSITION EFFECTS; ENZYME KINETICS; GLUCOSE; GLYCEROL; SUBSTRATES;

ALCOHOL DEHYDROGENASE; SUCCINIC ACID;

CELL CULTURE;

ACETIC ACID; ALCOHOL; ALCOHOL DEHYDROGENASE; CARBON; GLUCOSE; GLYCEROL; METHANOL; SUCCINIC ACID;

ACETOBACTER; ARTICLE; BACTERIAL GROWTH; BACTERIUM CULTURE; COLORIMETRY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME SYNTHESIS; IMMUNOBLOTTING; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS;

ACETOBACTER; ACETOBACTER ACETI; ACIDOMONAS METHANOLICA; BACTERIA (MICROORGANISMS);

EID: 0342683840     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)87321-7     Document Type: Article

References (25)

1. Steudel, K., Miethe, D., and Babel, W.: Bakterium MB58, ein methylotrophes "Essigsäurebakterium". Z. Allg. Mikrobiol., 20, 663-672 (1980).
2. Matsushita, K., Takahashi, K., Takahashi, M., Ameyama, M., and Adachi, O.: Methanol and ethanol oxidase respiratory chains of the methylotrophic acetic acid bacterium, Acetobacter methanolicus. J. Biochem. (Tokyo), 111, 739-747 (1992).
3. Matsushita, K., Takahashi, K., and Adachi, O.: A novel quinoprotein methanol dehydrogenase containing an additional 32-kilodalton peptide purified from Acetobacter methanolicus: identification of the peptide as a moxJ product. Biochemistry, 32, 5576-5582 (1993).
4. Ohmori, S., Uozumi, T., and Beppu, T.: Loss of acetic acid resistance and ethanol oxidizing ability in an Acetobacter strain. Agric. Biol. Chem., 46, 381-389 (1982).
5. Adachi, O., Miyagawa, E., Shinagawa, E., Matsushita, K., and Ameyama, M.: Purification and properties of paniculate alcohol dehydrogenase from Acetobacter aceti. Agric. Biol. Chem., 42, 2331-2340 (1978).
6. Ameyama, M. and Adachi, O.: Alcohol dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol., 89, 450-457 (1982).
7. Ameyama, M. and Adachi, O.: Aldehyde dehydrogenase from acetic acid bacteria, membrane-bound. Methods Enzymol., 89, 491-497 (1982).
8. Matsushita, K., Takaki, Y., Shinagawa, E., Ameyama, M., and Adachi, O.: 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. Biotech. Biochem., 56, 304-310 (1992).
9. Inoue, T., Sunagawa, M., Mori, A., Imai, C., Fukuda, M., Takagi, M., and Yano, K.: Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti. J. Bacteriol., 171, 3115-3122 (1989).
10. Inoue, T., Sunagawa, M., Mori, A., Imai, C., Fukuda, M., Takagi, M., and Yano, K.: Nucleotide sequence of the gene encoding the 45-kilodalton subunit of alcohol dehydrogenase from Acetobacter aceti. J. Ferment. Bioeng., 73, 419-424 (1992).
11. 1 of Acetobacter aceti is a cytochrome ba functioning as ubiquinol oxidase. Proc. Natl. Acad. Sci. USA, 87, 9863-9867 (1990).
12. 1 and cytochrome o, of Acetobacter aceti. J. Biol. Chem., 267, 24748-24753 (1992).
13. Takemura, H., Kondo, K., Horinouchi, S., and Beppu, T.: Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus. J. Bacteriol., 175, 6857-6866 (1993).
14. Uhlig, H., Karbaum, K., and Steudel, A.: Acetobacter methanolicus sp. nov., an acidophilic facultatively methylotrophic bacterium. Int. J. Syst. Bacteriol., 36, 317-322 (1986).
15. Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685 (1970).
16. Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M., and Adachi, O.: Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols. J. Bacteriol., 177, 2442-2450 (1995).
17. Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E., and Adachi, O.: Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. J. Biol. Chem., 271, 4850-4857 (1996).
18. Thomas, P.E., Ryan, D., and Levin, W.: An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem., 75, 168-176 (1976).
19. Dulley, J. R. and Grieve, P. A.: A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem., 64, 136-141 (1975).
20. De Ley, J., Swings, J., and Gosselé, F.: Acetobacter, p. 268-274. In Krieg, N. R. and Holt, J. G. (ed.), Bergey's manual of systematic bacteriology, vol. 1. Williams and Wilkins, Baltimore (1984).
21. Matsushita, K., Yakushi, T., Takaki, Y., Toyama, H., and Adachi, O.: 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).
22. Elliott, E. J. and Anthony, C.: The interaction between methanol dehydrogenase and cytochrome c in the acidophilic methylotroph Acetobacter methanolicus. J. Gen. Microbiol., 134, 369-377 (1988).
23. Loffhagen, N. and Babel, W.: Localization of primary alcohol-oxidizing enzymes in the facultative methylotroph Acetobacter sp. MB70. Z. Allg. Mikrobiol., 24, 143-149 (1984).
24. Cozier, G. E., Giles, I. G., and Anthony, C.: The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J., 308, 375-379 (1995).
25. Kondo, K., Beppu, T., and Horinouchi, S.: Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the three-component membrane-bound alcohol dehydrogenase from Acetobacter pasteurianus. J. Bacteriol., 177, 5048-5055 (1995).