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Volumn 71, Issue 9, 2005, Pages 4966-4971

Pyruvate fermentation by Oenococcus oeni and Leuconostoc mesenteroides and role of pyruvate dehydrogenase in anaerobic fermentation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CARBON; ENZYME KINETICS; GENES; TOXICITY;

EID: 25144438914     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.9.4966-4971.2005     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 0034965129 scopus 로고    scopus 로고
    • Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli
    • Abdel-Hamid, A. M., M. M. Attwood, and J. R. Guest. 2001. Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli. Microbiology 147:1483-1498.
    • (2001) Microbiology , vol.147 , pp. 1483-1498
    • Abdel-Hamid, A.M.1    Attwood, M.M.2    Guest, J.R.3
  • 2
    • 0003099824 scopus 로고
    • Acetate kinase from Escherichia coli
    • H. U. Bergmeyer (ed.). Verlag Chemie, Weinheim, Germany
    • Bergmeyer, H. U. 1983. Acetate kinase from Escherichia coli, p. 126-129. In H. U. Bergmeyer (ed.), Methods of enzymatic analysis, 3rd ed., vol. II. Verlag Chemie, Weinheim, Germany.
    • (1983) Methods of Enzymatic Analysis, 3rd Ed. , vol.2 , pp. 126-129
    • Bergmeyer, H.U.1
  • 3
    • 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
  • 4
    • 0000746045 scopus 로고
    • Medium for screening Leuconostoc oenos strains defective in malolactic fermentation
    • Cavin, J. F., H. Prevost, J. Lin, P. Schmitt, and C. Davies. 1989. Medium for screening Leuconostoc oenos strains defective in malolactic fermentation. Appl. Environ. Microbiol. 55:751-753.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 751-753
    • Cavin, J.F.1    Prevost, H.2    Lin, J.3    Schmitt, P.4    Davies, C.5
  • 6
    • 0028936112 scopus 로고
    • Proposal to reclassify Leuconostoc oenos as Oenococcus oeni [corrig.] gen. nov., comb. nov.
    • Dicks, L. M., F. Dellaglio, and M. Collins. 1995. Proposal to reclassify Leuconostoc oenos as Oenococcus oeni [corrig.] gen. nov., comb. nov. Int. J. Syst. Bacteriol. 45:395-397.
    • (1995) Int. J. Syst. Bacteriol. , vol.45 , pp. 395-397
    • Dicks, L.M.1    Dellaglio, F.2    Collins, M.3
  • 7
    • 0021201011 scopus 로고
    • Regulation of product formation during glucose or lactose limitation in nongrowing cells of Streptococcus lactis
    • Fordyce, A. M., V. L. Crow, and T. D. Thomas. 1984. Regulation of product formation during glucose or lactose limitation in nongrowing cells of Streptococcus lactis. Appl. Environ. Microbiol. 48:332-337.
    • (1984) Appl. Environ. Microbiol. , vol.48 , pp. 332-337
    • Fordyce, A.M.1    Crow, V.L.2    Thomas, T.D.3
  • 8
    • 0014126092 scopus 로고
    • Leuconostoc oenos sp. nov.
    • Garvie, E. I. 1967. Leuconostoc oenos sp. nov. J. Gen. Microbiol. 48:431-438.
    • (1967) J. Gen. Microbiol. , vol.48 , pp. 431-438
    • Garvie, E.I.1
  • 9
    • 0002831112 scopus 로고
    • Genus Leuconostoc
    • P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt (ed.). Williams & Wilkins, Baltimore, Md.
    • Garvie, E. I. 1986. Genus Leuconostoc, p. 1071-1975. In P. H. A. Sneath, N. S. Mair, M. E. Sharpe, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, vol. 2. Williams & Wilkins, Baltimore, Md.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1071-1975
    • Garvie, E.I.1
  • 11
    • 0019227505 scopus 로고
    • Purification of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and resolution of its four component polypeptides
    • Henderson, C. E., and R. N. Perham. 1980. Purification of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and resolution of its four component polypeptides. Biochem. J. 189:161-172.
    • (1980) Biochem. J. , vol.189 , pp. 161-172
    • Henderson, C.E.1    Perham, R.N.2
  • 12
    • 0035380714 scopus 로고    scopus 로고
    • Metabolic behaviour 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 behaviour 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
  • 13
    • 0000859908 scopus 로고
    • Phosphotransacetylase from Clostridium kluyveri
    • Klotzsch, H. R. 1969. Phosphotransacetylase from Clostridium kluyveri. Methods Enzymol. 13:381-386.
    • (1969) Methods Enzymol. , vol.13 , pp. 381-386
    • Klotzsch, H.R.1
  • 14
    • 0002394619 scopus 로고
    • A specific micromethod for determination of acyl phosphates
    • Lipmann, F., and C. Tuttle. 1945. A specific micromethod for determination of acyl phosphates. J. Biol. Chem. 159:21-28.
    • (1945) J. Biol. Chem. , vol.159 , pp. 21-28
    • Lipmann, F.1    Tuttle, C.2
  • 15
    • 2942544264 scopus 로고    scopus 로고
    • Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum
    • Lorquet, F., P. Goffin, L. Muscariello, J. Baudry, V. Ladero, M. Sacco, M. Kleerebezem, and P. Hols. 2004. Characterization and functional analysis of the poxB gene, which encodes pyruvate oxidase in Lactobacillus plantarum. J. Bacteriol. 186:3749-3759.
    • (2004) J. Bacteriol. , vol.186 , pp. 3749-3759
    • Lorquet, F.1    Goffin, P.2    Muscariello, L.3    Baudry, J.4    Ladero, V.5    Sacco, M.6    Kleerebezem, M.7    Hols, P.8
  • 16
    • 0036150419 scopus 로고    scopus 로고
    • NAD(P)H regeneration is the key for heterolactic fermentation of hexoses in Oenococcus oeni
    • Maicas, S., S. Ferrer, and I. Pardo. 2002. NAD(P)H regeneration is the key for heterolactic fermentation of hexoses in Oenococcus oeni. Microbiology 148:325-332.
    • (2002) Microbiology , vol.148 , pp. 325-332
    • Maicas, S.1    Ferrer, S.2    Pardo, I.3
  • 17
    • 0036189303 scopus 로고    scopus 로고
    • The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis
    • Melchiorsen, C. R., K. Jokumsen, J. Villadsen, H. Israelsen, and J. Arnau. 2001. The level of pyruvate-formate lyase controls the shift from homolactic to mixed-acid product formation in Lactococcus lactis. Appl. Microbiol. Biotechnol. 58:338-344.
    • (2001) Appl. Microbiol. Biotechnol. , vol.58 , pp. 338-344
    • Melchiorsen, C.R.1    Jokumsen, K.2    Villadsen, J.3    Israelsen, H.4    Arnau, J.5
  • 19
    • 0021256733 scopus 로고
    • Correlation of oxygen utilization and hydrogen peroxide accumulation with oxygen induced enzymes in Lactobacillus plantarum cultures
    • Murphy, M. G., and S. Condon. 1984. Correlation of oxygen utilization and hydrogen peroxide accumulation with oxygen induced enzymes in Lactobacillus plantarum cultures. Arch. Microbiol. 138:44-48.
    • (1984) Arch. Microbiol. , vol.138 , pp. 44-48
    • Murphy, M.G.1    Condon, S.2
  • 20
    • 0021983734 scopus 로고
    • Oxygen dependent lactate utilization by Lactobacillus plantarum
    • Murphy, M. G., L. O'Connor, D. Walsh, and S. Condon. 1985. Oxygen dependent lactate utilization by Lactobacillus plantarum. Arch. Microbiol. 141:75-79.
    • (1985) Arch. Microbiol. , vol.141 , pp. 75-79
    • Murphy, M.G.1    O'Connor, L.2    Walsh, D.3    Condon, S.4
  • 21
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth in Bacillus subtilis: Identification of fermentation end products and genes required for growth
    • Nakano, M. M., Y. Dailly, P. Zuber, and D. P. Clark. 1997. Characterization of anaerobic fermentative growth in Bacillus subtilis: identification of fermentation end products and genes required for growth. J. Bacteriol. 179:6749-6755.
    • (1997) J. Bacteriol. , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.2    Zuber, P.3    Clark, D.P.4
  • 22
    • 0031727390 scopus 로고    scopus 로고
    • Anaerobic growth of a strict aerobe (Bacillus subtilis)
    • Nakano, M. M., and P. Zuber. 1998. Anaerobic growth of a strict aerobe (Bacillus subtilis). Annu. Rev. Microbiol. 52:165-190.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 165-190
    • Nakano, M.M.1    Zuber, P.2
  • 23
  • 24
    • 1942440947 scopus 로고    scopus 로고
    • Effect of pyruvate kinase overproduction on glucose metabolism of Lactococcus lactis
    • Ramos, A., A. R. Neves, R. Ventura, C. Mayock, P. Lopez, and H. Santos. 2004. Effect of pyruvate kinase overproduction on glucose metabolism of Lactococcus lactis. Microbiology 150:1103-1111.
    • (2004) Microbiology , vol.150 , pp. 1103-1111
    • Ramos, A.1    Neves, A.R.2    Ventura, R.3    Mayock, C.4    Lopez, P.5    Santos, H.6
  • 25
    • 77956998069 scopus 로고
    • Purification of the pyruvate dehydrogenase complex (Escherichia coli)
    • Reed, L. J., and C. R. Willms. 1966. Purification of the pyruvate dehydrogenase complex (Escherichia coli). Methods Enzymol. 9:247-265.
    • (1966) Methods Enzymol. , vol.9 , pp. 247-265
    • Reed, L.J.1    Willms, C.R.2
  • 26
    • 0035106494 scopus 로고    scopus 로고
    • Significance of pantothenate for glucose fermentation by Oenococcus oeni and for suppression of the erythritol and acetate production
    • Richter, H., D. Vlad, and G. Unden. 2001. Significance of pantothenate for glucose fermentation by Oenococcus oeni and for suppression of the erythritol and acetate production. Arch. Microbiol. 175:26-31.
    • (2001) Arch. Microbiol. , vol.175 , pp. 26-31
    • Richter, H.1    Vlad, D.2    Unden, G.3
  • 27
    • 0037396454 scopus 로고    scopus 로고
    • Use of the mannitol pathway in fructose fermentation of Oenococcus oeni due to limiting redox regeneration capacity of the ethanol pathway
    • Richter, H., I. Hamann, and G. Unden. 2003. Use of the mannitol pathway in fructose fermentation of Oenococcus oeni due to limiting redox regeneration capacity of the ethanol pathway. Arch. Microbiol. 179:227-233.
    • (2003) Arch. Microbiol. , vol.179 , pp. 227-233
    • Richter, H.1    Hamann, I.2    Unden, G.3
  • 28
    • 0346364906 scopus 로고    scopus 로고
    • Significance of phosphoglucose isomerase for the shift between heterolactic and mannitol fermentation of fructose by Oenococcus oeni
    • Richter, H., A. A. De Graaf, I. Hamann, and G. Unden. 2003. Significance of phosphoglucose isomerase for the shift between heterolactic and mannitol fermentation of fructose by Oenococcus oeni. Arch. Microbiol. 180:465-470.
    • (2003) Arch. Microbiol. , vol.180 , pp. 465-470
    • Richter, H.1    De Graaf, A.A.2    Hamann, I.3    Unden, G.4
  • 29
    • 0021137019 scopus 로고
    • Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum
    • Sedewitz, B., K. H. Schleifer, and F. Götz. 1984. Purification and biochemical characterization of pyruvate oxidase from Lactobacillus plantarum. J. Bacteriol. 160:273-278.
    • (1984) J. Bacteriol. , vol.160 , pp. 273-278
    • Sedewitz, B.1    Schleifer, K.H.2    Götz, F.3
  • 30
    • 0021200188 scopus 로고
    • Physiological role of pyruvate oxidase in the aerobic metabolism of Lactobacillus plantarum
    • Sedewitz, B., K. H. Schleifer, and F. Götz. 1984. Physiological role of pyruvate oxidase in the aerobic metabolism of Lactobacillus plantarum. J. Bacteriol. 160:462-465.
    • (1984) J. Bacteriol. , vol.160 , pp. 462-465
    • Sedewitz, B.1    Schleifer, K.H.2    Götz, F.3
  • 31
    • 0026647636 scopus 로고
    • Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and α-acetolactate synthase of Lactococcus lactis subsp. lactis bv. diacetylactis
    • Snoep, J. L., M. J. Teixeira de Mattos, M. Starrenburg, and J. Hugenholtz. 1992. Isolation, characterization, and physiological role of the pyruvate dehydrogenase complex and α-acetolactate synthase of Lactococcus lactis subsp. lactis bv. diacetylactis. J. Bacteriol. 174:4838-4841.
    • (1992) J. Bacteriol. , vol.174 , pp. 4838-4841
    • Snoep, J.L.1    Teixeira De Mattos, M.J.2    Starrenburg, M.3    Hugenholtz, J.4
  • 32
    • 0027507947 scopus 로고
    • Differences in sensitivity to NADH of purified dehydrogenase complex of Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli: Implications for their activity in vivo
    • Snoep, J. L., M. R. de Graef, A. Westphal, A. de Kok, T. J. de Mattos, and O. Neijssel. 1993. Differences in sensitivity to NADH of purified dehydrogenase complex of Enterococcus faecalis, Lactococcus lactis, Azotobacter vinelandii and Escherichia coli: implications for their activity in vivo. FEMS Microbiol. Lett. 114:279-283.
    • (1993) FEMS Microbiol. Lett. , vol.114 , pp. 279-283
    • Snoep, J.L.1    De Graef, M.R.2    Westphal, A.3    De Kok, A.4    De Mattos, T.J.5    Neijssel, O.6
  • 33
    • 0019287540 scopus 로고
    • Galactose fermentation by Streptococcus lactis and Streptococcus cremoris: Pathways, products, and regulation
    • Thomas, T. D., K. W. Turner, and V. L. Crow. 1980. Galactose fermentation by Streptococcus lactis and Streptococcus cremoris: pathways, products, and regulation. J. Bacteriol. 144:672-682.
    • (1980) J. Bacteriol. , vol.144 , pp. 672-682
    • Thomas, T.D.1    Turner, K.W.2    Crow, V.L.3
  • 34
    • 0027209897 scopus 로고
    • Pathway and regulation of erythritol formation in Leuconostoc oenos
    • Veiga-da-Cunha, M., H. Santos, and E. von Schaftingen. 1993. Pathway and regulation of erythritol formation in Leuconostoc oenos. J. Bacteriol. 175:3941-3948.
    • (1993) J. Bacteriol. , vol.175 , pp. 3941-3948
    • Veiga-Da-Cunha, M.1    Santos, H.2    Von Schaftingen, E.3
  • 35
    • 0041810412 scopus 로고    scopus 로고
    • Eubacterium pyruvativorans sp. nov., a novel nori-saccharolytic anaerobe from the rumen that ferments pyruvate and amino acids, forms caproate and utilizes acetate and propionate
    • Wallace, R. J., N. McKain, N. R. McEwan, E. Miyagawa, L. C. Chaudhary, T. P. King, N. D. Walker, J. H. Apajalahti, and C. J. Newbold. 2003. Eubacterium pyruvativorans sp. nov., a novel nori-saccharolytic anaerobe from the rumen that ferments pyruvate and amino acids, forms caproate and utilizes acetate and propionate. Int. J. Syst. Evol. Microbiol. 53:965-970.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 965-970
    • Wallace, R.J.1    McKain, N.2    McEwan, N.R.3    Miyagawa, E.4    Chaudhary, L.C.5    King, T.P.6    Walker, N.D.7    Apajalahti, J.H.8    Newbold, C.J.9


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