메뉴 건너뛰기




Volumn 279, Issue 7, 2012, Pages 1274-1290

Role of phosphate in the central metabolism of two lactic acid bacteria - A comparative systems biology approach

Author keywords

glycolysis; kinetic modelling; Lactococcus lactis; phosphate uptake; Streptococcus pyogenes

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUCOSE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; LACTATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHATE; PHOSPHATE TRANSPORTER; PYRUVATE KINASE;

EID: 84859103859     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08523.x     Document Type: Article
Times cited : (47)

References (72)
  • 1
    • 0001780077 scopus 로고    scopus 로고
    • Lars Axelsson: Lactic Acid Bacteria: Classification and Physiology
    • (Salminen S. von Wright A. & Ouwehan A.C. eds), Marcel Dekker, Inc., New York
    • Salminen S, (2004) Lars Axelsson: Lactic Acid Bacteria: Classification and Physiology. In Lactic Acid Bacteria: Microbiological and Functional Aspects (, Salminen S, von Wright A, &, Ouwehan AC, eds), pp. 1-66. Marcel Dekker, Inc., New York.
    • (2004) Lactic Acid Bacteria: Microbiological and Functional Aspects , pp. 1-66
    • Salminen, S.1
  • 2
    • 0035519262 scopus 로고    scopus 로고
    • Comparative genomics and bioenergetics
    • Castresana J, (2001) Comparative genomics and bioenergetics. Biochim Biophys Acta 1506, 147-162.
    • (2001) Biochim Biophys Acta , vol.1506 , pp. 147-162
    • Castresana, J.1
  • 7
    • 80052252679 scopus 로고    scopus 로고
    • Functional genomics for food fermentation processes
    • Smid EJ, &, Hugenholtz J, (2010) Functional genomics for food fermentation processes. Annu Rev Food Sci Technol 1, 497-519.
    • (2010) Annu Rev Food Sci Technol , vol.1 , pp. 497-519
    • Smid, E.J.1    Hugenholtz, J.2
  • 8
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW, (2000) Pathogenesis of group A streptococcal infections. Clin Microbiol Rev 13, 470-511.
    • (2000) Clin Microbiol Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 9
    • 0023945810 scopus 로고
    • Lactic acid bacteria: Model systems for in vivo studies of sugar transport and metabolism in Gram-positive organisms
    • Thompson J, (1988) Lactic acid bacteria: model systems for in vivo studies of sugar transport and metabolism in Gram-positive organisms. Biochemie 70, 325-336.
    • (1988) Biochemie , vol.70 , pp. 325-336
    • Thompson, J.1
  • 10
    • 0018357964 scopus 로고
    • Change from homo- to heterolactic fermentation by Streptococcus lactis resulting from glucose limitation in anaerobic chemostat cultures
    • Thomas TD, Ellwood EC, &, Longyear VM, (1979) Change from homo- to heterolactic fermentation by Streptococcus lactis resulting from glucose limitation in anaerobic chemostat cultures. J Bacteriol 138, 109-117.
    • (1979) J Bacteriol , vol.138 , pp. 109-117
    • Thomas, T.D.1    Ellwood, E.C.2    Longyear, V.M.3
  • 11
    • 79551474189 scopus 로고    scopus 로고
    • Characterization of three lactic acid bacteria and their isogenic ldh deletion mutants shows optimization for YATP (cell mass produced per mole of ATP) at their physiological pHs
    • Fiedler T, Bekker M, Jonsson M, Mehmeti I, Pritzschke A, Siemens N, Nes I, Hugenholtz J, &, Kreikemeyer B, (2011) Characterization of three lactic acid bacteria and their isogenic ldh deletion mutants shows optimization for YATP (cell mass produced per mole of ATP) at their physiological pHs. Appl Environ Microbiol 77, 612-617.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 612-617
    • Fiedler, T.1    Bekker, M.2    Jonsson, M.3    Mehmeti, I.4    Pritzschke, A.5    Siemens, N.6    Nes, I.7    Hugenholtz, J.8    Kreikemeyer, B.9
  • 13
    • 0036037732 scopus 로고    scopus 로고
    • Time dependent responses of glycolytic intermediates in a detailed glycolytic model of Lactococcus lactis during glucose run-out experiments
    • Hoefnagel MH, van der Burgt A, Martens DE, Hugenholtz J, &, Snoep JL, (2002) Time dependent responses of glycolytic intermediates in a detailed glycolytic model of Lactococcus lactis during glucose run-out experiments. Mol Biol Rep 29, 157-161.
    • (2002) Mol Biol Rep , vol.29 , pp. 157-161
    • Hoefnagel, M.H.1    Van Der Burgt, A.2    Martens, D.E.3    Hugenholtz, J.4    Snoep, J.L.5
  • 15
    • 79952404792 scopus 로고    scopus 로고
    • Dynamic modeling of lactic acid fermentation metabolism with Lactococcus lactis
    • Oh E, Lu M, Park C, Oh HB, Lee SY, &, Lee J, (2011) Dynamic modeling of lactic acid fermentation metabolism with Lactococcus lactis. J Microbiol Biotechnol 21, 162-169.
    • (2011) J Microbiol Biotechnol , vol.21 , pp. 162-169
    • Oh, E.1    Lu, M.2    Park, C.3    Oh, H.B.4    Lee, S.Y.5    Lee, J.6
  • 16
    • 57749192247 scopus 로고    scopus 로고
    • The metabolic pH response in Lactococcus lactis: An integrative experimental and modelling approach
    • Andersen AZ, Carvalho AL, Neves AR, Santos H, Kummer U, &, Olsen LF, (2009) The metabolic pH response in Lactococcus lactis: an integrative experimental and modelling approach. Comput Biol Chem 33, 71-83.
    • (2009) Comput Biol Chem , vol.33 , pp. 71-83
    • Andersen, A.Z.1    Carvalho, A.L.2    Neves, A.R.3    Santos, H.4    Kummer, U.5    Olsen, L.F.6
  • 17
    • 0037008786 scopus 로고    scopus 로고
    • Is the glycolytic flux in Lactococcus lactis primarily controlled by the redox charge? Kinetics of NAD+ and NADH pools determined in vivo by 13C NMR
    • Neves AR, Ventura R, Mansour N, Shearman C, Gasson MJ, Maycock C, Ramos A, &, Santos H, (2002) Is the glycolytic flux in Lactococcus lactis primarily controlled by the redox charge? Kinetics of NAD+ and NADH pools determined in vivo by 13C NMR. J Biol Chem 277, 28088-28098.
    • (2002) J Biol Chem , vol.277 , pp. 28088-28098
    • Neves, A.R.1    Ventura, R.2    Mansour, N.3    Shearman, C.4    Gasson, M.J.5    Maycock, C.6    Ramos, A.7    Santos, H.8
  • 18
    • 0032843651 scopus 로고    scopus 로고
    • New aspects of inorganic polyphosphate metabolism and function
    • Kulaev I, Vagabov V, &, Kulakovskaya T, (1999) New aspects of inorganic polyphosphate metabolism and function. J Biosci Bioeng 88, 111-129.
    • (1999) J Biosci Bioeng , vol.88 , pp. 111-129
    • Kulaev, I.1    Vagabov, V.2    Kulakovskaya, T.3
  • 20
    • 0023917711 scopus 로고
    • Inducer expulsion in Streptococcus pyogenes: Properties and mechanism of the efflux reaction
    • Sutrina SL, Reizer J, &, Saier MH, (1988) Inducer expulsion in Streptococcus pyogenes: properties and mechanism of the efflux reaction. J Bacteriol 170, 1874-1877.
    • (1988) J Bacteriol , vol.170 , pp. 1874-1877
    • Sutrina, S.L.1    Reizer, J.2    Saier, M.H.3
  • 21
    • 0019476463 scopus 로고
    • The importance of inorganic phosphate in regulation of energy metabolism of Streptococcus lactis
    • Mason PW, Carbone DP, Cushman RA, &, Waggoner AS, (1981) The importance of inorganic phosphate in regulation of energy metabolism of Streptococcus lactis. J Biol Chem 256, 1861-1866.
    • (1981) J Biol Chem , vol.256 , pp. 1861-1866
    • Mason, P.W.1    Carbone, D.P.2    Cushman, R.A.3    Waggoner, A.S.4
  • 23
    • 23944486891 scopus 로고    scopus 로고
    • Overview on sugar metabolism and its control in Lactococcus lactis- the input from in vivo NMR
    • Neves AR, Pool WA, Kok J, Kuipers OP, &, Santos H, (2005) Overview on sugar metabolism and its control in Lactococcus lactis- the input from in vivo NMR. FEMS Microbiol Rev 29, 531-554.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 531-554
    • Neves, A.R.1    Pool, W.A.2    Kok, J.3    Kuipers, O.P.4    Santos, H.5
  • 24
    • 33845626641 scopus 로고    scopus 로고
    • How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria
    • Deutscher J, Francke C, &, Postma PW, (2006) How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Microbiol Mol Biol Rev 70, 939-1031.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 939-1031
    • Deutscher, J.1    Francke, C.2    Postma, P.W.3
  • 25
    • 58449116696 scopus 로고    scopus 로고
    • Characterization of the individual glucose uptake systems of Lactococcus lactis: Mannose-PTS, cellobiose-PTS and the novel GlcU permease
    • Castro R, Neves AR, Fonseca LL, Pool WA, Kok J, Kuipers OP, &, Santos H, (2008) Characterization of the individual glucose uptake systems of Lactococcus lactis: mannose-PTS, cellobiose-PTS and the novel GlcU permease. Mol Microbiol 71, 795-806.
    • (2008) Mol Microbiol , vol.71 , pp. 795-806
    • Castro, R.1    Neves, A.R.2    Fonseca, L.L.3    Pool, W.A.4    Kok, J.5    Kuipers, O.P.6    Santos, H.7
  • 26
    • 0017134223 scopus 로고
    • Purification and properties of pyruvate kinase from Streptococcus lactis
    • Crow VL, &, Pritchard GG, (1976) Purification and properties of pyruvate kinase from Streptococcus lactis. Biochim Biophys Acta 438, 90-101.
    • (1976) Biochim Biophys Acta , vol.438 , pp. 90-101
    • Crow, V.L.1    Pritchard, G.G.2
  • 28
    • 0033831855 scopus 로고    scopus 로고
    • Effects of pH and energy supply on activity and amount of pyruvate formate-lyase in Streptococcus bovis
    • Asanuma N, &, Hino T, (2000) Effects of pH and energy supply on activity and amount of pyruvate formate-lyase in Streptococcus bovis. Appl Environ Microbiol 66, 3773-3777.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3773-3777
    • Asanuma, N.1    Hino, T.2
  • 29
    • 47649086915 scopus 로고    scopus 로고
    • Control analysis of the role of triosephosphate isomerase in glucose metabolism in Lactococcus lactis
    • Solem C, Koebmann B, &, Jensen PR, (2008) Control analysis of the role of triosephosphate isomerase in glucose metabolism in Lactococcus lactis. IET Syst Biol 2, 64-72.
    • (2008) IET Syst Biol , vol.2 , pp. 64-72
    • Solem, C.1    Koebmann, B.2    Jensen, P.R.3
  • 30
    • 0023589202 scopus 로고
    • Dependence of Streptococcus lactis phosphate transport on internal phosphate concentration and internal pH
    • Poolman B, Nijssen RM, &, Konings WN, (1987) Dependence of Streptococcus lactis phosphate transport on internal phosphate concentration and internal pH. J Bacteriol 169, 5373-5378.
    • (1987) J Bacteriol , vol.169 , pp. 5373-5378
    • Poolman, B.1    Nijssen, R.M.2    Konings, W.N.3
  • 33
    • 0022979375 scopus 로고
    • Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: Amino acid sequence and site of ATP-dependent phosphorylation of HPr
    • Deutscher J, Pevec B, Beyreuther K, Kiltz HH, &, Hengstenberg W, (1986) Streptococcal phosphoenolpyruvate-sugar phosphotransferase system: amino acid sequence and site of ATP-dependent phosphorylation of HPr. Biochemistry 25, 6543-6551.
    • (1986) Biochemistry , vol.25 , pp. 6543-6551
    • Deutscher, J.1    Pevec, B.2    Beyreuther, K.3    Kiltz, H.H.4    Hengstenberg, W.5
  • 34
    • 0021211416 scopus 로고
    • Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system
    • Reizer J, Novotny MJ, Hengstenberg W, &, Saier MH, (1984) Properties of ATP-dependent protein kinase from Streptococcus pyogenes that phosphorylates a seryl residue in HPr, a phosphocarrier protein of the phosphotransferase system. J Bacteriol 160, 333-340.
    • (1984) J Bacteriol , vol.160 , pp. 333-340
    • Reizer, J.1    Novotny, M.J.2    Hengstenberg, W.3    Saier, M.H.4
  • 35
    • 0029863334 scopus 로고    scopus 로고
    • Inducer expulsion and the occurrence of an HPr(Ser-P)-activated sugar-phosphate phosphatase in Enterococcus faecalis and Streptococcus pyogenes
    • Ye JJ, Minarcik J, &, Saier MHJ, (1996) Inducer expulsion and the occurrence of an HPr(Ser-P)-activated sugar-phosphate phosphatase in Enterococcus faecalis and Streptococcus pyogenes. Microbiology 142, 585-592.
    • (1996) Microbiology , vol.142 , pp. 585-592
    • Ye, J.J.1    Minarcik, J.2    Saier, M.H.J.3
  • 36
    • 0020449086 scopus 로고
    • Purification and kinetic characterization of a specific glucokinase from Streptococcus mutans OMZ70 cells
    • Porter EV, Chassy BM, &, Holmlund CE, (1982) Purification and kinetic characterization of a specific glucokinase from Streptococcus mutans OMZ70 cells. Biochim Biophys Acta 709, 178-186.
    • (1982) Biochim Biophys Acta , vol.709 , pp. 178-186
    • Porter, E.V.1    Chassy, B.M.2    Holmlund, C.E.3
  • 37
    • 0038080938 scopus 로고    scopus 로고
    • Purification of recombinant non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Streptococcus pyogenes expressed in E. coli
    • Iddar A, Valverde F, Serrano A, &, Soukri A, (2003) Purification of recombinant non-phosphorylating NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Streptococcus pyogenes expressed in E. coli. Mol Cell Biochem 247, 195-203.
    • (2003) Mol Cell Biochem , vol.247 , pp. 195-203
    • Iddar, A.1    Valverde, F.2    Serrano, A.3    Soukri, A.4
  • 38
    • 0016805412 scopus 로고
    • Glucose-6-phosphate-dependent pyruvate kinase in Streptococcus mutans
    • Yamada T, &, Carlsson J, (1975) Glucose-6-phosphate-dependent pyruvate kinase in Streptococcus mutans. J Bacteriol 124, 562-563.
    • (1975) J Bacteriol , vol.124 , pp. 562-563
    • Yamada, T.1    Carlsson, J.2
  • 39
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3- phosphate-dehydrogenase with multiple binding activity
    • Pancholi V, &, Fischetti VA, (1992) A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. J Exp Med 176, 415-426.
    • (1992) J Exp Med , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 40
    • 0015989692 scopus 로고
    • Lactic acid translocation: Terminal step in glycolysis by Streptococcus faecalis
    • Harold FM, &, Levin E, (1974) Lactic acid translocation: terminal step in glycolysis by Streptococcus faecalis. J Bacteriol 117, 1141-1148.
    • (1974) J Bacteriol , vol.117 , pp. 1141-1148
    • Harold, F.M.1    Levin, E.2
  • 41
    • 63949086417 scopus 로고    scopus 로고
    • Multiple control of the acetate pathway in Lactococcus lactis under aeration by catabolite repression and metabolites
    • Lopez de Felipe F, &, Gaudu P, (2009) Multiple control of the acetate pathway in Lactococcus lactis under aeration by catabolite repression and metabolites. Appl Microbiol Biotechnol 82, 1115-1122.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 1115-1122
    • Lopez De Felipe, F.1    Gaudu, P.2
  • 42
    • 4644301904 scopus 로고    scopus 로고
    • The pool of ADP and ATP regulates anaerobic product formation in resting cells of Lactococcus lactis
    • Palmfeldt J, Paese M, Hahn-Hägerdal B, &, Niel EWJV, (2004) The pool of ADP and ATP regulates anaerobic product formation in resting cells of Lactococcus lactis. Appl Environ Microbiol 70, 5477-5484.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 5477-5484
    • Palmfeldt, J.1    Paese, M.2    Hahn-Hägerdal, B.3    Niel, E.4
  • 43
    • 0023120321 scopus 로고
    • Mechanism and regulation of phosphate transport in Streptococcus pyogenes
    • Reizer J, &, Saier MH, (1987) Mechanism and regulation of phosphate transport in Streptococcus pyogenes. J Bacteriol 169, 297-302.
    • (1987) J Bacteriol , vol.169 , pp. 297-302
    • Reizer, J.1    Saier, M.H.2
  • 45
    • 58449116696 scopus 로고    scopus 로고
    • Characterization of the individual glucose uptake systems of Lactococcus lactis: Mannose-PTS, cellobiose-PTS and the novel GlcU permease
    • Castro R, Neves AR, Fonseca LL, Pool WA, Kok J, Kuipers OP, &, Santos H, (2009) Characterization of the individual glucose uptake systems of Lactococcus lactis: mannose-PTS, cellobiose-PTS and the novel GlcU permease. Mol Microbiol 71, 795-806.
    • (2009) Mol Microbiol , vol.71 , pp. 795-806
    • Castro, R.1    Neves, A.R.2    Fonseca, L.L.3    Pool, W.A.4    Kok, J.5    Kuipers, O.P.6    Santos, H.7
  • 47
    • 0038119517 scopus 로고
    • The alcoholic ferment of yeast-juice
    • Harden A, &, Young WJ, (1906) The alcoholic ferment of yeast-juice. Proc R S B Biol Sci 77, 405-420.
    • (1906) Proc R S B Biol Sci , vol.77 , pp. 405-420
    • Harden, A.1    Young, W.J.2
  • 48
    • 0038119533 scopus 로고
    • The alcoholic ferment of yeast-juice, part III: The function of phosphates in the fermentation of glucose by yeast-juice
    • Harden A, &, Young WJ, (1908) The alcoholic ferment of yeast-juice, part III: the function of phosphates in the fermentation of glucose by yeast-juice. Proc R Soc Lond B 80, 299-311.
    • (1908) Proc R Soc Lond B , vol.80 , pp. 299-311
    • Harden, A.1    Young, W.J.2
  • 49
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProt Consortium
    • UniProt Consortium (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 38, D142-D148.
    • (2010) Nucleic Acids Res , vol.38
  • 50
    • 0000612804 scopus 로고
    • Response of plants to phosphate concentration in solution culture: Growth and phosphorus content
    • Asher CJ, &, Loneragan JF, (1967) Response of plants to phosphate concentration in solution culture: growth and phosphorus content. Soil Sci 103, 225-233.
    • (1967) Soil Sci , vol.103 , pp. 225-233
    • Asher, C.J.1    Loneragan, J.F.2
  • 52
  • 54
    • 0036041922 scopus 로고    scopus 로고
    • Dynamic response of catabolic pathways to autoacidification in Lactococcus lactis: Transcript profiling and stability in relation to metabolic and energetic constraints
    • Even S, Lindley ND, Loubière P, &, Cocaign-Bousquet M, (2002) Dynamic response of catabolic pathways to autoacidification in Lactococcus lactis: transcript profiling and stability in relation to metabolic and energetic constraints. Mol Microbiol 45, 1143-1152.
    • (2002) Mol Microbiol , vol.45 , pp. 1143-1152
    • Even, S.1    Lindley, N.D.2    Loubière, P.3    Cocaign-Bousquet, M.4
  • 55
    • 0034967213 scopus 로고    scopus 로고
    • Molecular physiology of sugar catabolism in Lactococcus lactis IL1403
    • Even S, Lindley ND, &, Cocaign-Bousquet M, (2001) Molecular physiology of sugar catabolism in Lactococcus lactis IL1403. J Bacteriol 183, 3817-3824.
    • (2001) J Bacteriol , vol.183 , pp. 3817-3824
    • Even, S.1    Lindley, N.D.2    Cocaign-Bousquet, M.3
  • 56
    • 0023822865 scopus 로고
    • The F1-ATPase from Streptococcus cremoris: Isolation, purification and partial characterization
    • Rimpiläinen MA, Mettänen TT, Niskasaari K, &, Forsén RI, (1988) The F1-ATPase from Streptococcus cremoris: isolation, purification and partial characterization. Int J Biochem 20, 1117-1124.
    • (1988) Int J Biochem , vol.20 , pp. 1117-1124
    • Rimpiläinen, M.A.1    Mettänen, T.T.2    Niskasaari, K.3    Forsén, R.I.4
  • 57
    • 0029054845 scopus 로고
    • Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system
    • Cvitkovitch DG, Boyd DA, Thevenot T, &, Hamilton IR, (1995) Glucose transport by a mutant of Streptococcus mutans unable to accumulate sugars via the phosphoenolpyruvate phosphotransferase system. J Bacteriol 177, 2251-2258.
    • (1995) J Bacteriol , vol.177 , pp. 2251-2258
    • Cvitkovitch, D.G.1    Boyd, D.A.2    Thevenot, T.3    Hamilton, I.R.4
  • 58
    • 0019846020 scopus 로고
    • Phosphofructokinases from Lactobacteriaceae. II. Purification and properties of phosphofructokinase from Streptococcus thermophilus
    • Simon WA, &, Hofer HW, (1981) Phosphofructokinases from Lactobacteriaceae. II. Purification and properties of phosphofructokinase from Streptococcus thermophilus. Biochim Biophys Acta 661, 158-163.
    • (1981) Biochim Biophys Acta , vol.661 , pp. 158-163
    • Simon, W.A.1    Hofer, H.W.2
  • 59
    • 0020347017 scopus 로고
    • Pyruvate kinase from Streptococcus lactis
    • Crow VL, &, Pritchard GG, (1982) Pyruvate kinase from Streptococcus lactis. Methods Enzymol 90 (Pt E), 165-170.
    • (1982) Methods Enzymol , vol.90 , Issue.PART E , pp. 165-170
    • Crow, V.L.1    Pritchard, G.G.2
  • 60
    • 0018800304 scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans
    • +-dependent glyceraldehyde-3-phosphate dehydrogenases from Streptococcus mutans. J Biol Chem 254, 1134-1142.
    • (1979) J Biol Chem , vol.254 , pp. 1134-1142
    • Crow, V.L.1    Wittenberger, C.L.2
  • 61
    • 0037150030 scopus 로고    scopus 로고
    • +-dependent glyceraldehyde-3- phosphate dehydrogenase in Bacillus cereus
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus. FEMS Microbiol Lett 211, 29-35.
    • (2002) FEMS Microbiol Lett , vol.211 , pp. 29-35
    • Iddar, A.1    Serrano, A.2    Soukri, A.3
  • 62
    • 0032422012 scopus 로고    scopus 로고
    • A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis
    • Brown CK, Kuhlman PL, Mattingly S, Slates K, Calie PJ, &, Farrar WW, (1998) A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis. J Protein Chem 17, 855-866.
    • (1998) J Protein Chem , vol.17 , pp. 855-866
    • Brown, C.K.1    Kuhlman, P.L.2    Mattingly, S.3    Slates, K.4    Calie, P.J.5    Farrar, W.W.6
  • 63
    • 0020080449 scopus 로고
    • Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties
    • Takahashi S, Abbe K, &, Yamada T, (1982) Purification of pyruvate formate-lyase from Streptococcus mutans and its regulatory properties. J Bacteriol 149, 1034-1040.
    • (1982) J Bacteriol , vol.149 , pp. 1034-1040
    • Takahashi, S.1    Abbe, K.2    Yamada, T.3
  • 64
    • 0023352454 scopus 로고
    • Membrane-associated and solubilized ATPases of Streptococcus mutans and Streptococcus sanguis
    • Sutton SV, &, Marquis RE, (1987) Membrane-associated and solubilized ATPases of Streptococcus mutans and Streptococcus sanguis. J Dent Res 66, 1095-1098.
    • (1987) J Dent Res , vol.66 , pp. 1095-1098
    • Sutton, S.V.1    Marquis, R.E.2
  • 65
    • 0022000825 scopus 로고
    • Lactate dehydrogenase from Streptococcus mutans: Purification, characterization, and crossed antigenicity with lactate dehydrogenases from Lactobacillus casei, Actinomyces viscosus, and Streptococcus sanguis
    • Sommer P, Klein JP, Schöller M, &, Frank RM, (1985) Lactate dehydrogenase from Streptococcus mutans: purification, characterization, and crossed antigenicity with lactate dehydrogenases from Lactobacillus casei, Actinomyces viscosus, and Streptococcus sanguis. Infect Immun 47, 489-495.
    • (1985) Infect Immun , vol.47 , pp. 489-495
    • Sommer, P.1    Klein, J.P.2    Schöller, M.3    Frank, R.M.4
  • 66
    • 33846617808 scopus 로고    scopus 로고
    • Bringing metabolic networks to life: Convenience rate law and thermodynamic constraints
    • Liebermeister W, &, Klipp E, (2006) Bringing metabolic networks to life: convenience rate law and thermodynamic constraints. Theor Biol Med Model 3, 41.
    • (2006) Theor Biol Med Model , vol.3 , pp. 41
    • Liebermeister, W.1    Klipp, E.2
  • 67
    • 33846647495 scopus 로고    scopus 로고
    • Bringing metabolic networks to life: Integration of kinetic, metabolic, and proteomic data
    • Liebermeister W, &, Klipp E, (2006) Bringing metabolic networks to life: integration of kinetic, metabolic, and proteomic data. Theor Biol Med Model 3, 42.
    • (2006) Theor Biol Med Model , vol.3 , pp. 42
    • Liebermeister, W.1    Klipp, E.2
  • 68
    • 67650479690 scopus 로고    scopus 로고
    • Construction and characterization of three lactate dehydrogenase-negative Enterococcus faecalis V583 mutants
    • Jonsson M, Saleihan Z, Nes IF, &, Holo H, (2009) Construction and characterization of three lactate dehydrogenase-negative Enterococcus faecalis V583 mutants. Appl Environ Microbiol 75, 4901-4903.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 4901-4903
    • Jonsson, M.1    Saleihan, Z.2    Nes, I.F.3    Holo, H.4
  • 72


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.