메뉴 건너뛰기




Volumn 181, Issue 19, 1999, Pages 5940-5947

Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; CUMENE HYDROPEROXIDE; DNA; FLAVOPROTEIN; HYDROGEN PEROXIDE; LACTIC ACID; MANNITOL; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0032871251     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.19.5940-5947.1999     Document Type: Article
Times cited : (116)

References (31)
  • 1
    • 0020433094 scopus 로고
    • Involvement of oxygen-sensitive pyruvate formate-lyase in mixed-acid fermentation by Streptococcus mutans under strictly anaerobic conditions
    • Abbe, K., S. Takahashi, and T. Yamada. 1982. Involvement of oxygen-sensitive pyruvate formate-lyase in mixed-acid fermentation by Streptococcus mutans under strictly anaerobic conditions. J. Bacteriol. 152:175-182.
    • (1982) J. Bacteriol. , vol.152 , pp. 175-182
    • Abbe, K.1    Takahashi, S.2    Yamada, T.3
  • 2
    • 0022467287 scopus 로고
    • Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis
    • Aoki, H., T. Shiroza, M. Hayakawa, S. Sato, and H. K. Kuramitsu. 1986. Cloning of a Streptococcus mutans glucosyltransferase gene coding for insoluble glucan synthesis. Infect. Immun. 53:587-594.
    • (1986) Infect. Immun. , vol.53 , pp. 587-594
    • Aoki, H.1    Shiroza, T.2    Hayakawa, M.3    Sato, S.4    Kuramitsu, H.K.5
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive methods 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
  • 4
    • 0345631656 scopus 로고
    • Fructose 1,6-diphosphate-dependent lactate dehydrogenase from a cariogenic streptococcus: Purification and regulatory properties
    • Brown, A. T., and C. T. Wittenberger. 1972. Fructose 1,6-diphosphate-dependent lactate dehydrogenase from a cariogenic streptococcus: purification and regulatory properties. J. Bacteriol. 122:1126-1135.
    • (1972) J. Bacteriol. , vol.122 , pp. 1126-1135
    • Brown, A.T.1    Wittenberger, C.T.2
  • 5
    • 0021828778 scopus 로고
    • Pyruvate dehydrogenase activity in Streptococcus mutons
    • Carlsson, J., U. Kujala, and M. B. K. Edlund. 1985. Pyruvate dehydrogenase activity in Streptococcus mutons. Infect. Immun. 49:674-678.
    • (1985) Infect. Immun. , vol.49 , pp. 674-678
    • Carlsson, J.1    Kujala, U.2    Edlund, M.B.K.3
  • 6
    • 0028226006 scopus 로고
    • Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes
    • Chae, H. Z., K. Robison, L. B. Poolr, G. Church, G. Storz, and S. G. Rhee. 1994. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA 91:7017-7021.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7017-7021
    • Chae, H.Z.1    Robison, K.2    Poolr, L.B.3    Church, G.4    Storz, G.5    Rhee, S.G.6
  • 7
    • 0030822346 scopus 로고    scopus 로고
    • Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from salmonella typhimurium
    • Ellis, H. R., and L. B. Poole. 1997. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 34:13349-13356.
    • (1997) Biochemistry , vol.34 , pp. 13349-13356
    • Ellis, H.R.1    Poole, L.B.2
  • 8
    • 0019255349 scopus 로고
    • Biology, immunology, and cariogenicity of Streptococcus mutans
    • Hamada, S., and H. D. Slade. 1980. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol. Rev. 44:331-384.
    • (1980) Microbiol. Rev. , vol.44 , pp. 331-384
    • Hamada, S.1    Slade, H.D.2
  • 9
    • 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.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557
    • Hanahan, D.1
  • 10
    • 0021229457 scopus 로고
    • Effect of oxygen on the growth and mannitol metabolism of Streptococcus mutans
    • Higuchi, M. 1984. Effect of oxygen on the growth and mannitol metabolism of Streptococcus mutans. J. Gen. Microbiol. 130:1819-1826.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 1819-1826
    • Higuchi, M.1
  • 11
    • 0026936304 scopus 로고
    • Reduced nicotinamide adenine dinucleotide oxidase involvement in defense against oxygen toxicity of Streptococcus mutans
    • Higuchi, M. 1992. Reduced nicotinamide adenine dinucleotide oxidase involvement in defense against oxygen toxicity of Streptococcus mutans. Oral Microbiol. Immunol. 7:309-314.
    • (1992) Oral Microbiol. Immunol. , vol.7 , pp. 309-314
    • Higuchi, M.1
  • 14
    • 0024599904 scopus 로고
    • An alkyl hydroperoxide reductase involved in the defense of DNA against oxidative damage: Purification and properties
    • Jacobson, F. S., R. W. Morgan, M. F. Christman, and B. N. Ames. 1989. An alkyl hydroperoxide reductase involved in the defense of DNA against oxidative damage: purification and properties. J. Biol. Chem. 264:1488-1496.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1488-1496
    • Jacobson, F.S.1    Morgan, R.W.2    Christman, M.F.3    Ames, B.N.4
  • 15
    • 0025886123 scopus 로고
    • Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis
    • LeBlanc, D. J., L. N. Lee, and J. M. Inamine. 1991. Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis. Antimicrob. Agents Chemother. 35:1804-1810.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1804-1810
    • LeBlanc, D.J.1    Lee, L.N.2    Inamine, J.M.3
  • 16
    • 0022993292 scopus 로고
    • Role of Streptococcus mutans in human dental decay
    • Loesche, W. J. 1986. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50:353-380.
    • (1986) Microbiol. Rev. , vol.50 , pp. 353-380
    • Loesche, W.J.1
  • 17
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: A novel approach to metabolic engineering in lactococcus lactis by controlled expression of NADH oxidase
    • Lopez de Felipe, F., M. Kleerebezem, W. M. de Vos, and J. Hugenholtz. 1998. Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J. Bacteriol. 180: 3804-3808.
    • (1998) J. Bacteriol. , vol.180 , pp. 3804-3808
    • Lopez De Felipe, F.1    Kleerebezem, M.2    De Vos, W.M.3    Hugenholtz, J.4
  • 20
    • 0013828826 scopus 로고
    • Studies on erythrocyte glycolysis. I. Determination of the glycolytic intermediates in human erythrocytes
    • Minakami, S., C. Suzuki, T. Saito, and H. Yoshikawa. 1965. Studies on erythrocyte glycolysis. I. Determination of the glycolytic intermediates in human erythrocytes. J. Biochem. 58:543-550.
    • (1965) J. Biochem. , vol.58 , pp. 543-550
    • Minakami, S.1    Suzuki, C.2    Saito, T.3    Yoshikawa, H.4
  • 21
    • 0031899593 scopus 로고    scopus 로고
    • Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli
    • Mongkolsuk, S., W. Praituan, S. Loprasert, M. Fuangthong, and S. Chamnongpol. 1998. Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli. J. Bacteriol. 180:2636-2643.
    • (1998) J. Bacteriol. , vol.180 , pp. 2636-2643
    • Mongkolsuk, S.1    Praituan, W.2    Loprasert, S.3    Fuangthong, M.4    Chamnongpol, S.5
  • 22
    • 0019482395 scopus 로고
    • Genetic transformation of Streptococcus mutans
    • Perry, D., and H. K. Kuramitsu. 1981. Genetic transformation of Streptococcus mutans. Infect. Immun. 32:1295-1297.
    • (1981) Infect. Immun. , vol.32 , pp. 1295-1297
    • Perry, D.1    Kuramitsu, H.K.2
  • 23
    • 0030032612 scopus 로고    scopus 로고
    • Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins
    • Poole, L. B., and H. R. Ellis. 1996. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35:56-64.
    • (1996) Biochemistry , vol.35 , pp. 56-64
    • Poole, L.B.1    Ellis, H.R.2
  • 24
    • 0002254195 scopus 로고    scopus 로고
    • NADH oxidase-1 and a second component encoded upstream of nox-1 comprise an alkyl hydroperoxide reductase system in Streptococcus mutans
    • K. J. Stevenson, V. Massey, and C. H. Williams, Jr. (ed.). University of Calgary Press, Calgary, Alberta, Canada
    • Poole, L. B., M. Shimada, and M. Higuchi. 1997. NADH oxidase-1 and a second component encoded upstream of nox-1 comprise an alkyl hydroperoxide reductase system in Streptococcus mutans, p. 769-772. In K. J. Stevenson, V. Massey, and C. H. Williams, Jr. (ed.), Flavins and flavoproteins 1996. University of Calgary Press, Calgary, Alberta, Canada.
    • (1997) Flavins and Flavoproteins 1996 , pp. 769-772
    • Poole, L.B.1    Shimada, M.2    Higuchi, M.3
  • 25
    • 0344769188 scopus 로고    scopus 로고
    • Unpublished observations
    • Poole, L. B. Unpublished observations.
    • Poole, L.B.1
  • 27
    • 0024604234 scopus 로고
    • An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp
    • Storz, G., F. S. Jacobson, L. A. Tartaglia, R. W. Morgan, L. A. Silveira, and B. N. Ames. 1989. An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp. J. Bacteriol. 171:2049-2055.
    • (1989) J. Bacteriol. , vol.171 , pp. 2049-2055
    • Storz, G.1    Jacobson, F.S.2    Tartaglia, L.A.3    Morgan, R.W.4    Silveira, L.A.5    Ames, B.N.6
  • 28
    • 0023093662 scopus 로고
    • Oxygen sensitivity of sugar metabolism and interconversion of pyruvate formate-lyase in intact cells of Streptococcus mutans and Streptococcus sanguis
    • Takahashi, N., K. Abbe, S. Takahashi-Abbe, and T. Yamada. 1987. Oxygen sensitivity of sugar metabolism and interconversion of pyruvate formate-lyase in intact cells of Streptococcus mutans and Streptococcus sanguis. Infect. Immun. 55:652-656.
    • (1987) Infect. Immun. , vol.55 , pp. 652-656
    • Takahashi, N.1    Abbe, K.2    Takahashi-Abbe, S.3    Yamada, T.4
  • 29
    • 0030061538 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the pfl gene encoding pyruvate formate-lyase from Streptococcus mutans
    • Yamamoto, Y., Y. Sato, S. Takahashi-Abbe, K. Abbe, T. Yamada, and H. Kizaki. 1996. Cloning and sequence analysis of the pfl gene encoding pyruvate formate-lyase from Streptococcus mutans. Infect. Immun. 64:385-391.
    • (1996) Infect. Immun. , vol.64 , pp. 385-391
    • Yamamoto, Y.1    Sato, Y.2    Takahashi-Abbe, S.3    Abbe, K.4    Yamada, T.5    Kizaki, H.6
  • 30
    • 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.
    • (1985) Gene , vol.33 , pp. 103
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 31
    • 0016678459 scopus 로고
    • Antigens of Streptococcus mutans: Characterization of a polysaccharide antigen from walls of strain GS-5
    • Wetherell, J. R., Jr., and A. S. Bleiweis. 1975. Antigens of Streptococcus mutans: characterization of a polysaccharide antigen from walls of strain GS-5. Infect. Immun. 12:1341-1348.
    • (1975) Infect. Immun. , vol.12 , pp. 1341-1348
    • Wetherell J.R., Jr.1    Bleiweis, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.