Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant gluconobacter frateurii isolated from Thailand

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 6, 2005, Pages 1120-1129

  Toyama, Hirohide ^a   Soemphol, Wichai ^a   Moonmangmee, Duangtip ^b   Adachi, Osao ^a   Matsushita, Kazunobu ^a  

^a YAMAGUCHI UNIVERSITY   (Japan)

^b KING MONGKUT'S UNIVERSITY OF TECHNOLOGY THONBURI   (Thailand)

Author keywords

Acetic acid bacteria; Cytochrome c; FAD; Gluconobacter; Sorbitol dehydrogenase

Indexed keywords

AMINO ACIDS; CLONING; ENZYMES; PROSTHETICS;

CLONED GENES; MOLECULAR MASS; MOLECULAR PROPERTIES; PROSTHETIC GROUPS;

BIOLOGICAL MEMBRANES;

BACTERIAL PROTEIN; FLAVINE ADENINE NUCLEOTIDE; IDITOL DEHYDROGENASE; MEMBRANE PROTEIN; SORBITOL;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYMOLOGY; GLUCONOBACTER; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; THAILAND;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BASE SEQUENCE; CONSERVED SEQUENCE; FLAVIN-ADENINE DINUCLEOTIDE; GLUCONOBACTER; L-IDITOL 2-DEHYDROGENASE; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SORBITOL; THAILAND;

GLUCONOBACTER; GLUCONOBACTER FRATEURII; GLUCONOBACTER OXYDANS;

EID: 22444441792     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.69.1120     Document Type: Article

References (34)

1. Adachi, O., Moonmangmee, D., Toyama, H., Yamada, M., Shinagawa, E., and Matsushita, K., New developments in oxidative fermentation. Appl. Microbiol. Biotechnol., 60, 643-653 (2003).
2. Matsushita, K., Toyama, H., and Adachi, O., Respiratory chain and bioenergetics of acetic acid bacteria. In "Advances in Microbial Physiology" Vol. 36, eds. Rose, A. H., and Tempest, D. W., Academic Press, Ltd., London, pp. 247-301 (1994).
3. Adachi, O., Moonmungmee, D., Shinagawa, E., Toyama, H., Yamada, M., and Matsushita, K., New quinoprotein in oxidative fermentation. Biochim. Biophys. Acta, 1647, 10-17 (2003).
4. Adachi, O., Moonmangmee, D., Toyama, H., Yamada, M., Shinagawa, E., and Matsushita, K., New developments in oxidative fermentation. Appl. Microbiol. Biotechnol., 60, 643-653 (2003).
5. Sugisawa, T., and Hoshino, T., Purification and properties of membrane-bound D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3255. Biosci. Biotechnol. Biochem., 66, 57-64 (2002).
6. Shinagawa, E., Matsushita, K., Adachi, O., and Ameyama, M., Purification and characterization of D-sorbitol dehydrogenase from membrane of Gluconobacter suboxydans var. α. Agric. Biol. Chem., 46, 135-141 (1982).
7. Miyazaki, T., Tomiyama, N., Shinjoh, M., and Hoshino, T., Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for acivity development in E. coli. Biosci. Biotechnol. Biochem., 66, 262-270 (2002).
8. Shinjoh, M., Tomiyama, N., Miyazaki, T., and Hoshino, T., Main polyol dehydrogenase of Gluconobacter suboxydans IFO 3255, membrane-bound D-sorbitol dehydrogenase, that needs product of upstream gene, sldB, for activity. Biosci. Biotechnol. Biochem., 66, 2314-2322 (2002).
9. Ameyama, M., Shinagawa, E., Matsushita, K., and Adachi, O., Solubilization, purification and properties of membrane-bound glycerol dehydrogenase from Gluconobacter industrius. Agric. Biol. Chem., 49, 1001-1010 (1985).
10. Adachi, O., Fujii, Y., Ghaly, M., Toyama, H., Shinagawa, E., and Matsushita, K., Membrane-bound quinoprotein D-arabitol dehydrogenase of Gluconobacter suboydans IFO 3257: a versatile enzyme for the oxidative fermentation of various ketoses. Biosci. Biotechnol. Biochem., 65, 2755-2762 (2001).
11. Matsushita, K., Fujii, Y., Ano, Y., Toyama, H., Shinjoh, M., Tomiyama, N., Miyazaki, T., Sugisawa, T., Hoshino, T., and Adachi, O., 5-Keto-D-guluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species. Appl. Environ. Microbiol., 69, 1959-1966 (2003).
12. Shinagawa, E., Matsushita, K., Adachi, O., and Ameyama, M., Purification and characterization of 2-keto-D-gluconate dehydrogenase from Gluconobacter melanogenus. Agric. Biol. Chem., 45, 1079-1085 (1981).
13. Bhosale, S. H., Rao, M. B., and Deshpade, V. V., Molecular and industrial aspects of glucose isomerase. Microbiol. Rev., 60, 280-300 (1996).
14. Moonmangmee, D., Adachi, O., Ano, Y., Shinagawa, E., Toyama, H., Theeragool, G., Lotong, N., and Matsushita, K., Isolation and characterization of thermotolerant Gluconobacter strains catalyzing oxidative fermentation at higher temperatures. Biosci. Biotechnol. Biochem., 65, 115-125 (2000).
15. Ameyama, M., Shinagawa, E., Matsushita, K., and Adachi, O., D-Fructose dehydrogenase of Gluconobacter suboxydans: purification, characterization, and application to enzymatic microdetermination of D-fructose. J. Bacteriol., 145, 814-823 (1981).
16. Dully, 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).
17. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriphage T4. Nature (London), 227, 680-685 (1970).
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. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory manual, 2nd edition, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. (1989).
20. Marmur, J., A procedure for the isolation of deoxyribonucleic acid from micro-organisms. J. Mol. Biol., 3, 208-218 (1961).
21. Scrutton, N. S., Identification of covalent flavoproteins and analysis of the covalent link. Methods Mol. Biol., 131, 181-193 (1999).
22. 1 and cytochrome o, of Acetobacter aceti. J. Biol. Chem., 267, 24748-24753 (1992).
23. Rhee, S., Martin, R. G., Rosner, J. L., and Davies, D. R., A novel DNA-binding motive in MarA: the first structure for an AraC family transcriptional activator. Proc. Natl. Acad. Sci. U.S.A., 18, 10413-10418 (1998).
24. Goryshin, I. Y., and Rezninoff, W. S., Tn5 in vitro transposition. J. Biol. Chem., 273, 7367-7374 (1998).
25. Berks, B. C., Sargent, F., and Palmer, T., The Tat protein export pathway. Mol. Microbiol., 35, 260-274 (2000).
26. Pugsley, A. P., The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev., 57, 50-108 (1993).
27. Adachi, O., Toyama, H., Theeragool, G., Lotong, N., and Matsushita, K., Crystallization and properties of NAD-dependent D-sorbitol dehydrogenase from Gluconobacter suboxydans IFO 3257. Biosci. Biotechnol. Biochem., 63, 1589-1595 (1999).
28. Choi, E.-S., Lee, E.-H., and Rhee, S.-K., Purification of a membrane-bound sorbitol dehydrogenase from Gluconobacter suboxydans. FEMS Microbiol. Lett., 125, 45-50 (1995).
29. Choi, J. H., and Lee, Y. S., Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol., 64, 625-635 (2004).
30. Kondo, K., Beppu, T., and Horinouchi, S., Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the three components membrane-bound alcohol dehydrogenase from Acetobacter pasteurianus. J. Bacteriol., 177, 5048-5055 (1995).
31. Thurner, C., Vela, C., Thony-Meyer, L., Meile, L., and Teuber, M., Biochemical and genetic characterization of the acetaldehyde dehydrogenase complex from Acetobacter europaeus. Arch. Microbiol., 168, 81-91 (1997).
32. Yum, D.-Y., Lee, Y.-P., and Pan, J.-G., 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).
33. Pujol, C. J., and Kado, C. I., Genetic and biochemical characterization of the pathway in Pantoea citrea leading to pink disease of pineapple. J. Bacteriol., 182, 2230-2237 (2000).
34. Matsushita, K., Yakushi, T., Toyama, H., Adachi, O., Miyoshi, H., Tagami, E., and Sakamoto, K., 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).