메뉴 건너뛰기




Volumn 166, Issue 1, 1998, Pages 155-163

Enterococcus faecalis glutathione reductase: purification, characterization and expression under normal and hyperbaric O2 conditions

Author keywords

Enterococcus faecalis; Glutathione reductase; Oxidative stress; Thiol content

Indexed keywords

GLUTATHIONE REDUCTASE;

EID: 0031656590     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00325-5     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric reductase - A family of flavoenzyme transhydrogenases
    • Muller, F., Ed.
    • Williams, C.H. Jr. (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric reductase - a family of flavoenzyme transhydrogenases. In: Chemistry and Biochemistry of Flavoenzymes, Vol III (Muller, F., Ed.), pp. 121-195.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 121-195
    • Williams C.H., Jr.1
  • 2
    • 0029006932 scopus 로고
    • Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNR2368
    • Pebay, M., Holl, A.C., Simonet, J.M. and Decaris, B. (1995) Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNR2368. J. Bacteriol. 146, 371-383.
    • (1995) J. Bacteriol. , vol.146 , pp. 371-383
    • Pebay, M.1    Holl, A.C.2    Simonet, J.M.3    Decaris, B.4
  • 7
    • 0030751187 scopus 로고    scopus 로고
    • Beyond vancomycin: New therapies to meet the challenge of glycopeptide resistance
    • Nicas, T.I., Zeckel, M.L. and Braun, D.K. (1997) Beyond vancomycin: new therapies to meet the challenge of glycopeptide resistance. Trends Microbiol. 5, 240-249.
    • (1997) Trends Microbiol. , vol.5 , pp. 240-249
    • Nicas, T.I.1    Zeckel, M.L.2    Braun, D.K.3
  • 8
    • 0021158356 scopus 로고
    • The role of oxygen and its derivatives in microbial pathogenesis and host defense
    • Beaman, L. and Beaman, B.L. (1984) The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu. Rev. Microbiol. 38, 27-48.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 27-48
    • Beaman, L.1    Beaman, B.L.2
  • 9
    • 0008225510 scopus 로고
    • The Streptococcus faecalis oxidases for reduced adenine diphosphate pyridine nucleotide
    • Dolin, M.I. (1957) The Streptococcus faecalis oxidases for reduced adenine diphosphate pyridine nucleotide. J. Biol. Chem. 225, 557-573.
    • (1957) J. Biol. Chem. , vol.225 , pp. 557-573
    • Dolin, M.I.1
  • 12
    • 0016442549 scopus 로고
    • Changes in the glutathione thiol disulfide status of Neurospora crassa conidia during germination and aging
    • Fahey, R.C., Brody, S. and Mikolajczyk, S.D. (1975) Changes in the glutathione thiol disulfide status of Neurospora crassa conidia during germination and aging. J. Bacteriol. 121, 144-151.
    • (1975) J. Bacteriol. , vol.121 , pp. 144-151
    • Fahey, R.C.1    Brody, S.2    Mikolajczyk, S.D.3
  • 13
    • 0014481378 scopus 로고
    • Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione
    • Tietze, F. (1969) Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Anal. Biochem. 27, 502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 14
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W.W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 15
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohe, L. and Gunzler, W.A. (1984) Assays of glutathione peroxidase. Methods Enzymol. 105, 114-121.
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 16
    • 0013812984 scopus 로고
    • On the reaction mechanism of glutathione reductase
    • Massey, V. and Williams, C.H. Jr. (1965) On the reaction mechanism of glutathione reductase. J. Biol. Chem. 240, 4470-4480.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4470-4480
    • Massey, V.1    Williams C.H., Jr.2
  • 19
    • 77956936983 scopus 로고
    • Flavin-containing dehydrogenases
    • Williams, C.H. Jr. (1976) Flavin-containing dehydrogenases. Enzymes 13, 89-173.
    • (1976) Enzymes , vol.13 , pp. 89-173
    • Williams C.H., Jr.1
  • 20
    • 0025329396 scopus 로고
    • Glutathione reductase: Comparison of steady-state and rapid reaction primary kinetic isotope effects exhibited by the yeast, spinach, and Escherichia coli enzymes
    • Vanoni, M.A., Wong, K.K., Ballou, D.P. and Blanchard, J.S. (1990) Glutathione reductase: comparison of steady-state and rapid reaction primary kinetic isotope effects exhibited by the yeast, spinach, and Escherichia coli enzymes. Biochemistry 29, 5790-5796.
    • (1990) Biochemistry , vol.29 , pp. 5790-5796
    • Vanoni, M.A.1    Wong, K.K.2    Ballou, D.P.3    Blanchard, J.S.4
  • 22
    • 0021099182 scopus 로고
    • The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates
    • Pai, E.F. and Schulz, G.E. (1983) The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. J. Biol. Chem. 258, 1752-1757.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1752-1757
    • Pai, E.F.1    Schulz, G.E.2
  • 23
    • 0344930672 scopus 로고
    • Identification and molecular analysis of oxy-R-regulated promoters important for the bacterial adaptation to oxidative stress
    • Tartaglia, L.A., Storz, G. and Ames, B.N. (1989) Identification and molecular analysis of oxy-R-regulated promoters important for the bacterial adaptation to oxidative stress. J. Biol. Chem. 258, 1752-1757.
    • (1989) J. Biol. Chem. , vol.258 , pp. 1752-1757
    • Tartaglia, L.A.1    Storz, G.2    Ames, B.N.3
  • 24
    • 0021930684 scopus 로고
    • Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium
    • Christman, M.F., Morgan, R.W., Jacobson, F.S. and Ames, B.N. (1985) Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 41, 753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 25
    • 0343990840 scopus 로고    scopus 로고
    • Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR
    • Ross, P.R. and Claiborne, A. (1998) Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR. FEMS Microbiol. Lett. 151, 177-183.
    • (1998) FEMS Microbiol. Lett. , vol.151 , pp. 177-183
    • Ross, P.R.1    Claiborne, A.2
  • 26
    • 0026540835 scopus 로고
    • Multidegenerate DNA recognition by the OxyR transcriptional regulator
    • Tartaglia, L.A., Gimenco, C.J., Storz, G. and Ames, B.N. (1992) Multidegenerate DNA recognition by the OxyR transcriptional regulator. J. Biol. Chem. 267, 2038-2045.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2038-2045
    • Tartaglia, L.A.1    Gimenco, C.J.2    Storz, G.3    Ames, B.N.4
  • 27
    • 0024446668 scopus 로고
    • Evolution of antioxidant mechanisms: Thiol-dependent peroxidases and thiol transferases among procaryotes
    • Sundquist, A.R. and Fahey, R.C. (1989) Evolution of antioxidant mechanisms: thiol-dependent peroxidases and thiol transferases among procaryotes. J. Mol. Evol. 29, 429-435.
    • (1989) J. Mol. Evol. , vol.29 , pp. 429-435
    • Sundquist, A.R.1    Fahey, R.C.2
  • 30
    • 0022446871 scopus 로고
    • Glutathione reductase from Escherichia coli: Cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidore-ductases
    • Greer, S. and Perham, R.N. (1986) Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidore-ductases. Biochemistry 25, 2736-2742.
    • (1986) Biochemistry , vol.25 , pp. 2736-2742
    • Greer, S.1    Perham, R.N.2
  • 31
    • 0028960573 scopus 로고
    • Isolation, characterization and overexpression of the yeast gene, glr1, encoding glutathione reductase
    • Collinson, L.P. and Dawes, I.W. (1995) Isolation, characterization and overexpression of the yeast gene, glr1, encoding glutathione reductase. Gene 156, 123-127.
    • (1995) Gene , vol.156 , pp. 123-127
    • Collinson, L.P.1    Dawes, I.W.2
  • 33
    • 0026081456 scopus 로고
    • Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: Determinants of substrate specificity among pyridine nucleotide-disulfide oxidoreductases
    • Perry, A.C., Ni Bhriain, N., Brown, N.L. and Rouch, D.A. (1991) Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulfide oxidoreductases. Mol. Microbiol. 5, 163-171.
    • (1991) Mol. Microbiol. , vol.5 , pp. 163-171
    • Perry, A.C.1    Ni Bhriain, N.2    Brown, N.L.3    Rouch, D.A.4
  • 34
    • 0028960992 scopus 로고
    • Sequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100
    • Daubaras, D.L., Hershberger, C.D., Kitano, K. Chakrabarty, A.M. (1995) Sequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100. Appl. Environ. Microbiol. 61, 1279-1289.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1279-1289
    • Daubaras, D.L.1    Hershberger, C.D.2    Kitano, K.3    Chakrabarty, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.