메뉴 건너뛰기




Volumn 193, Issue 12, 2011, Pages 3000-3008

Identification of a conserved sequence in flavoproteins essential for the correct conformation and activity of the NADH oxidase NoxE of Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NOXE ENZYME; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 79958041001     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01466-10     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 10644295071 scopus 로고    scopus 로고
    • Flavoprotein disulfide reductases: advances in chemistry and function
    • Argyrou, A., and J. S. Blanchard. 2004. Flavoprotein disulfide reductases: advances in chemistry and function. Prog. Nucleic Acid Res. Mol. Biol. 78:89-142.
    • (2004) Prog. Nucleic Acid Res. Mol. Biol. , vol.78 , pp. 89-142
    • Argyrou, A.1    Blanchard, J.S.2
  • 2
    • 0033405777 scopus 로고    scopus 로고
    • The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence
    • Auzat, I., et al. 1999. The NADH oxidase of Streptococcus pneumoniae: its involvement in competence and virulence. Mol. Microbiol. 34:1018-1028.
    • (1999) Mol. Microbiol. , vol.34 , pp. 1018-1028
    • Auzat, I.1
  • 3
    • 0346364657 scopus 로고    scopus 로고
    • Amino acid properties and consequences of substitutions
    • M. R. Barnes and I. C. Gray (ed.), John Wiley and Sons Ltd., Chichester, United Kingdom
    • Betts, M. J., and R. B. Russell. 2003. Amino acid properties and consequences of substitutions, p. 289-316. In M. R. Barnes and I. C. Gray (ed.), Bioinformatics for geneticists. John Wiley and Sons Ltd., Chichester, United Kingdom.
    • (2003) Bioinformatics for geneticists , pp. 289-316
    • Betts, M.J.1    Russell, R.B.2
  • 4
    • 33748059521 scopus 로고    scopus 로고
    • Influence of starter and nonstarter lactic acid bacteria on medium redox
    • Boucher, B., C. Brothersen, and J. Broadbent. 2006. Influence of starter and nonstarter lactic acid bacteria on medium redox. Aust. J. Dairy Technol. 61:116-118.
    • (2006) Aust. J. Dairy Technol. , vol.61 , pp. 116-118
    • Boucher, B.1    Brothersen, C.2    Broadbent, J.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method 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
  • 6
    • 3142653173 scopus 로고    scopus 로고
    • Unfolding intermediate in the peroxisomal flavoprotein D-amino acid oxidase
    • Caldinelli, L., et al. 2004. Unfolding intermediate in the peroxisomal flavoprotein D-amino acid oxidase. J. Biol. Chem. 279:28426-28434.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28426-28434
    • Caldinelli, L.1
  • 7
    • 0001209457 scopus 로고
    • Responses of lactic acid bacteria to oxygen
    • Condon, S. 1987. Responses of lactic acid bacteria to oxygen. FEMS Microbiol. Lett. 46:269-280.
    • (1987) FEMS Microbiol. Lett. , vol.46 , pp. 269-280
    • Condon, S.1
  • 8
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O., and D. Eisenberg. 2001. Sequence-structure analysis of FAD-containing proteins. Protein Sci. 10:1712-1728.
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 9
    • 0141595858 scopus 로고    scopus 로고
    • CcpA regulation of aerobic and respiration growth in Lactococcus lactis
    • Gaudu, P., G. Lamberet, S. Poncet, and A. Gruss. 2003. CcpA regulation of aerobic and respiration growth in Lactococcus lactis. Mol. Microbiol. 50:183-192.
    • (2003) Mol. Microbiol. , vol.50 , pp. 183-192
    • Gaudu, P.1    Lamberet, G.2    Poncet, S.3    Gruss, A.4
  • 10
    • 0033986479 scopus 로고    scopus 로고
    • Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes
    • Gibson, C. M., T. C. Mallett, A. Claiborne, and M. G. Caparon. 2000. Contribution of NADH oxidase to aerobic metabolism of Streptococcus pyogenes. J. Bacteriol. 182:448-455.
    • (2000) J. Bacteriol. , vol.182 , pp. 448-455
    • Gibson, C.M.1    Mallett, T.C.2    Claiborne, A.3    Caparon, M.G.4
  • 11
    • 0032871251 scopus 로고    scopus 로고
    • Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans
    • Higuchi, M., et al. 1999. Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans. J. Bacteriol. 181: 5940-5947.
    • (1999) J. Bacteriol. , vol.181 , pp. 5940-5947
    • Higuchi, M.1
  • 12
    • 0024345189 scopus 로고
    • High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media
    • Holo, H., and I. F. Nes. 1989. High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media. Appl. Environ. Microbiol. 55:3119-3123.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 3119-3123
    • Holo, H.1    Nes, I.F.2
  • 13
    • 0001089362 scopus 로고
    • The reduced diphosphopyridine nucleotide oxidase of Streptococcus faecalis: purification and properties
    • Hoskins, D. D., H. R. Whiteley, and B. Mackler. 1962. The reduced diphosphopyridine nucleotide oxidase of Streptococcus faecalis: purification and properties. J. Biol. Chem. 237:2647-2651.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2647-2651
    • Hoskins, D.D.1    Whiteley, H.R.2    Mackler, B.3
  • 14
    • 0001733085 scopus 로고
    • Purification and properties of a dipeptidase from Streptococcus cremoris
    • Hwang, I., S. Kaminogawa, and K. Yamauchi. 1981. Purification and properties of a dipeptidase from Streptococcus cremoris. Agric. Biol. Chem. 45: 159-165.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 159-165
    • Hwang, I.1    Kaminogawa, S.2    Yamauchi, K.3
  • 15
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay, J. A. 2008. Cellular defenses against superoxide and hydrogen peroxide. Annu. Rev. Biochem. 77:755-776.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 16
    • 78149415620 scopus 로고    scopus 로고
    • Contribution of the NADH-oxidase (Nox) to the aerobic life of Lactobacillus sanfranciscensis DSM20451
    • Jänsch, A., S. Freiding, J. Behr, and R. F. Vogel. 2011. Contribution of the NADH-oxidase (Nox) to the aerobic life of Lactobacillus sanfranciscensis DSM20451. Food Microbiol. 28:29-37.
    • (2011) Food Microbiol , vol.28 , pp. 29-37
    • Jänsch, A.1    Freiding, S.2    Behr, J.3    Vogel, R.F.4
  • 17
    • 0035380714 scopus 로고    scopus 로고
    • Metabolic behavior of Lactococcus lactis MG1363 in microaerobic continuous cultivation at a low dilution rate
    • Jensen, N. B., C. R. Melchiorsen, K. V. Jokumsen, and J. Villadsen. 2001. Metabolic behavior of Lactococcus lactis MG1363 in microaerobic continuous cultivation at a low dilution rate. Appl. Environ. Microbiol. 67:2677-2682.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2677-2682
    • Jensen, N.B.1    Melchiorsen, C.R.2    Jokumsen, K.V.3    Villadsen, J.4
  • 18
    • 20544438578 scopus 로고    scopus 로고
    • Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435
    • Jiang, R., B. R. Riebel, and A. S. Bommarius. 2005. Comparison of alkyl hydroperoxide reductase (AhpR) and water-forming NADH oxidase from Lactococcus lactis ATCC 19435. Adv. Synthesis Catalysis. 347:1139-1146.
    • (2005) Adv. Synthesis Catalysis. , vol.347 , pp. 1139-1146
    • Jiang, R.1    Riebel, B.R.2    Bommarius, A.S.3
  • 19
    • 33748055466 scopus 로고    scopus 로고
    • Addition of oxidizing or reducing agents to the reaction medium influences amino acid conversion to aroma compounds by Lactococcus lactis
    • Kieronczyk, A., R. Cachon, G. Feron, and M. Yvon. 2006. Addition of oxidizing or reducing agents to the reaction medium influences amino acid conversion to aroma compounds by Lactococcus lactis. J. Appl. Microbiol. 101:1114-1122.
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 1114-1122
    • Kieronczyk, A.1    Cachon, R.2    Feron, G.3    Yvon, M.4
  • 21
    • 0142040936 scopus 로고    scopus 로고
    • Glutathione protects Lactococcus lactis against oxidative stress
    • Li, Y., J. Hugenholtz, T. Abee, and D. Molenaar. 2003. Glutathione protects Lactococcus lactis against oxidative stress. Appl. Environ. Microbiol. 69: 5739-5745.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 5739-5745
    • Li, Y.1    Hugenholtz, J.2    Abee, T.3    Molenaar, D.4
  • 22
    • 0034958892 scopus 로고    scopus 로고
    • Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis
    • Lopez de Felipe, F., and J. Hugenholtz. 2001. Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis. Int. Dairy J. 11:37-44.
    • (2001) Int. Dairy J. , vol.11 , pp. 37-44
    • Lopez de Felipe, F.1    Hugenholtz, J.2
  • 23
    • 33747497810 scopus 로고    scopus 로고
    • 2 into two water molecules by the flavoenzyme
    • 2 into two water molecules by the flavoenzyme. Biochemistry. 45:9648-9659.
    • (2006) Biochemistry , vol.45 , pp. 9648-9659
    • Lountos, G.T.1
  • 24
    • 0242353812 scopus 로고    scopus 로고
    • Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase
    • Louzada, P. R., A. Sebollela, M. E. Scaramello, and S. T. Ferreira. 2003. Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase. Biophys. J. 85:3255-3261.
    • (2003) Biophys. J. , vol.85 , pp. 3255-3261
    • Louzada, P.R.1    Sebollela, A.2    Scaramello, M.E.3    Ferreira, S.T.4
  • 25
    • 0031735564 scopus 로고    scopus 로고
    • Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA
    • Luesink, E. J., R. E. van Herpen, B. P. Grossiord, O. P. Kuipers, and W. M. de Vos. 1998. Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA. Mol. Microbiol. 30:789-798.
    • (1998) Mol. Microbiol. , vol.30 , pp. 789-798
    • Luesink, E.J.1    van Herpen, R.E.2    Grossiord, B.P.3    Kuipers, O.P.4    de Vos, W.M.5
  • 26
    • 0032537559 scopus 로고    scopus 로고
    • Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change
    • Mallett, T. C., and A. Claiborne. 1998. Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change. Biochemistry. 37:8790-8802.
    • (1998) Biochemistry , vol.37 , pp. 8790-8802
    • Mallett, T.C.1    Claiborne, A.2
  • 27
    • 27544451339 scopus 로고    scopus 로고
    • 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis
    • Mierau, I., and M. Kleerebezem. 2005. 10 years of the nisin-controlled gene expression system (NICE) in Lactococcus lactis. Appl. Microbiol. Biotechnol. 68:705-717.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 705-717
    • Mierau, I.1    Kleerebezem, M.2
  • 28
    • 0027190591 scopus 로고
    • Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs
    • Nordhoff, A., U. S. Bucheler, D. Werner, and R. H. Schirmer. 1993. Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs. Biochemistry. 32:4060-4066.
    • (1993) Biochemistry , vol.32 , pp. 4060-4066
    • Nordhoff, A.1    Bucheler, U.S.2    Werner, D.3    Schirmer, R.H.4
  • 29
    • 0030896991 scopus 로고    scopus 로고
    • Denaturation and reactivation of dimeric human glutathione reductase-an assay for folding inhibitors
    • Nordhoff, A., et al. 1997. Denaturation and reactivation of dimeric human glutathione reductase-an assay for folding inhibitors. Eur. J. Biochem. 245:273-282.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 273-282
    • Nordhoff, A.1
  • 30
    • 0027185986 scopus 로고
    • Rapid mini-prep isolation of high-quality plasmid DNA from Lactococcus and Lactobacillus spp
    • O'Sullivan, D., J., and T. R. Klaenhammer. 1993. Rapid mini-prep isolation of high-quality plasmid DNA from Lactococcus and Lactobacillus spp. Appl. Environ. Microbiol. 59:2730-2733.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2730-2733
    • O'Sullivan, D.J.1    Klaenhammer, T.R.2
  • 31
    • 47249092884 scopus 로고    scopus 로고
    • Impact of aeration and heme-activated respiration on Lactococcus lactis gene expression: identification of a heme-responsive operon
    • Pedersen, M. B., et al. 2008. Impact of aeration and heme-activated respiration on Lactococcus lactis gene expression: identification of a heme-responsive operon. J. Bacteriol. 190:4903-4911.
    • (2008) J. Bacteriol. , vol.190 , pp. 4903-4911
    • Pedersen, M.B.1
  • 32
    • 67849103756 scopus 로고    scopus 로고
    • @TOME-2: a new pipeline for comparative modeling of protein-ligand complexes
    • Pons, J.-L., and G. Labesse. 2009. @TOME-2: a new pipeline for comparative modeling of protein-ligand complexes. Nucleic Acids Res. 37:W485-W491.
    • (2009) Nucleic Acids Res , vol.37
    • Pons, J.-L.1    Labesse, G.2
  • 33
    • 0034924910 scopus 로고    scopus 로고
    • Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae
    • Poyart, C., et al. 2001. Contribution of Mn-cofactored superoxide dismutase (SodA) to the virulence of Streptococcus agalactiae. Infect. Immun. 69:5098-5106.
    • (2001) Infect. Immun. , vol.69 , pp. 5098-5106
    • Poyart, C.1
  • 35
    • 77649222786 scopus 로고    scopus 로고
    • NADH oxidase NoxE and the electron transport chain are responsible for the ability of Lactococcus lactis to decrease the redox potential of milk
    • Tachon, S., H. Brandsma, and M. Yvon. 2010. NADH oxidase NoxE and the electron transport chain are responsible for the ability of Lactococcus lactis to decrease the redox potential of milk. Appl. Environ. Microbiol. 76:1311-1319.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1311-1319
    • Tachon, S.1    Brandsma, H.2    Yvon, M.3
  • 36
    • 11844259506 scopus 로고    scopus 로고
    • Roles of thioredoxin reductase during the aerobic life of Lactococcus lactis
    • Vido, K., et al. 2005. Roles of thioredoxin reductase during the aerobic life of Lactococcus lactis. J. Bacteriol. 187:601-610.
    • (2005) J. Bacteriol. , vol.187 , pp. 601-610
    • Vido, K.1
  • 37
    • 0021095474 scopus 로고
    • Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase
    • Wierenga, R. K., J. Drenth, and G. E. Schulz. 1983. Comparison of the three-dimensional protein and nucleotide structure of the FAD-binding domain of p-hydroxybenzoate hydroxylase with the FAD- as well as NADPH-binding domains of glutathione reductase. J. Mol. Biol. 167:725-739.
    • (1983) J. Mol. Biol. , vol.167 , pp. 725-739
    • Wierenga, R.K.1    Drenth, J.2    Schulz, G.E.3
  • 38
    • 33750002912 scopus 로고    scopus 로고
    • The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence
    • Yamamoto, Y., et al. 2006. The Group B Streptococcus NADH oxidase Nox-2 is involved in fatty acid biosynthesis during aerobic growth and contributes to virulence. Mol. Microbiol. 62:772-785.
    • (2006) Mol. Microbiol. , vol.62 , pp. 772-785
    • Yamamoto, Y.1
  • 39
    • 0035131745 scopus 로고    scopus 로고
    • Characterization of the Streptococcus pneumoniae NADH oxidase that is required for infection
    • Yu, J., et al. 2001. Characterization of the Streptococcus pneumoniae NADH oxidase that is required for infection. Microbiology. 147:431-438.
    • (2001) Microbiology , vol.147 , pp. 431-438
    • Yu, J.1
  • 40
    • 33846916395 scopus 로고    scopus 로고
    • Timeresolved determination of the CcpA regulon of Lactococcus lactis subsp. cremoris MG1363
    • Zomer, A. L., G. Buist, R. Larsen, J. Kok, and O. P. Kuipers. 2007. Timeresolved determination of the CcpA regulon of Lactococcus lactis subsp. cremoris MG1363. J. Bacteriol. 189:1366-1381.
    • (2007) J. Bacteriol. , vol.189 , pp. 1366-1381
    • Zomer, A.L.1    Buist, G.2    Larsen, R.3    Kok, J.4    Kuipers, O.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.