메뉴 건너뛰기




Volumn 70, Issue 9, 2004, Pages 5477-5484

The pool of ADP and ATP regulates anaerobic product formation in resting cells of Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CELL CULTURE; CONCENTRATION (PROCESS); DEHYDROGENATION; ETHANOL; FERMENTATION; FRUCTOSE; GLUCOSE; MALTOSE; MICROBIOLOGY; PHOSPHATES;

EID: 4644301904     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.9.5477-5484.2004     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 0043131950 scopus 로고    scopus 로고
    • +-isocitrate dehydrogenase from Saccharopolyspora erythraea
    • +-isocitrate dehydrogenase from Saccharopolyspora erythraea. Biotechnol. Lett. 25:1175-1178.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1175-1178
    • Alvarado, A.1    Flores, M.E.2
  • 2
    • 0035900670 scopus 로고    scopus 로고
    • Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis
    • Andersson, U., F. Levander, and P. Rådström. 2001. Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. J. Biol. Chem. 276:42707-42713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42707-42713
    • Andersson, U.1    Levander, F.2    Rådström, P.3
  • 3
    • 0031777832 scopus 로고    scopus 로고
    • Cloning of the Lactococcus lactis adhE gene, encoding a multifunctional alcohol dehydrogenase, by complementation of a fermentative mutant of Escherichia coli
    • Arnau, J., F. Jorgensen, S. M. Madsen, A. Vrang, and H. Israelsen. 1998. Cloning of the Lactococcus lactis adhE gene, encoding a multifunctional alcohol dehydrogenase, by complementation of a fermentative mutant of Escherichia coli. J. Bacteriol. 180:3049-3055.
    • (1998) J. Bacteriol. , vol.180 , pp. 3049-3055
    • Arnau, J.1    Jorgensen, F.2    Madsen, S.M.3    Vrang, A.4    Israelsen, H.5
  • 4
    • 0030924033 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase
    • Arnau, J., F. Jorgensen, S. M. Madsen, A. Vrang, and H. Israelsen, H. 1997. Cloning, expression, and characterization of the Lactococcus lactis pfl gene, encoding pyruvate formate-lyase. J. Bacteriol. 179:5884-5891.
    • (1997) J. Bacteriol. , vol.179 , pp. 5884-5891
    • Arnau, J.1    Jorgensen, F.2    Madsen, S.M.3    Vrang, A.4    Israelsen, H.H.5
  • 5
    • 0003443846 scopus 로고
    • Academic Press, Inc., New York, N.Y.
    • Bergmeyer, H. U. 1974. Methods of enzymatic analysis, vol. 3, p. 1314-1319. Academic Press, Inc., New York, N.Y.
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1314-1319
    • Bergmeyer, H.U.1
  • 6
    • 0015987389 scopus 로고
    • Lactose and D-galactose metabolism in group N streptococci: Presence of enzymes for both the D-galactose 1-phosphate and D-tagatose 6-phosphate pathways
    • Bissett, D. L., and R. L. Anderson. 1974. Lactose and D-galactose metabolism in group N streptococci: presence of enzymes for both the D-galactose 1-phosphate and D-tagatose 6-phosphate pathways. J. Bacteriol. 117:318-320.
    • (1974) J. Bacteriol. , vol.117 , pp. 318-320
    • Bissett, D.L.1    Anderson, R.L.2
  • 7
    • 0031932855 scopus 로고    scopus 로고
    • Relationship between intracellular phosphate, proton motive force, and rate of nongrowth energy dissipation (energy spilling) in Streptococcus bovis JB1
    • Bond, D. R., and J. B. Russell. 1998. Relationship between intracellular phosphate, proton motive force, and rate of nongrowth energy dissipation (energy spilling) in Streptococcus bovis JB1. Appl. Environ. Microbiol. 64:976-981.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 976-981
    • Bond, D.R.1    Russell, J.B.2
  • 8
    • 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
  • 9
    • 0021209585 scopus 로고
    • Two plasmid-determined restriction and modification systems in Streptococcus lactis
    • Chopin, A., M. C. Chopin, A. Moillo-Batt, and P. Langella. 1984. Two plasmid-determined restriction and modification systems in Streptococcus lactis. Plasmid 11:260-263.
    • (1984) Plasmid , vol.11 , pp. 260-263
    • Chopin, A.1    Chopin, M.C.2    Moillo-Batt, A.3    Langella, P.4
  • 10
    • 0016205822 scopus 로고
    • Pyruvate kinase of Streptococcus lactis
    • Collins, L. B., and T. D. Thomas. 1974. Pyruvate kinase of Streptococcus lactis. J. Bacteriol. 120:52-58.
    • (1974) J. Bacteriol. , vol.120 , pp. 52-58
    • Collins, L.B.1    Thomas, T.D.2
  • 11
    • 0017407960 scopus 로고
    • Fructose 1,6-diphosphate-activated L-lactate dehydrogenase from Streptococcus lactis: Kinetic properties and factors affecting activation
    • Crow, V. L., and G. G. Pritchard. 1977. Fructose 1,6-diphosphate- activated L-lactate dehydrogenase from Streptococcus lactis: kinetic properties and factors affecting activation. J. Bacteriol. 131:82-91.
    • (1977) J. Bacteriol. , vol.131 , pp. 82-91
    • Crow, V.L.1    Pritchard, G.G.2
  • 12
    • 0020314359 scopus 로고
    • Arginine metabolism in lactic streptococci
    • Crow, V. L., and T. D. Thomas. 1982. Arginine metabolism in lactic streptococci. J. Bacteriol. 150:1024-1032.
    • (1982) J. Bacteriol. , vol.150 , pp. 1024-1032
    • Crow, V.L.1    Thomas, T.D.2
  • 13
    • 1642441286 scopus 로고    scopus 로고
    • Engineering metabolic highways in lactococci and other lactic acid bacteria
    • de Vos, W. M., and J. Hugenhollz. 2004. Engineering metabolic highways in lactococci and other lactic acid bacteria. Trends Biotechnol. 22:72-79.
    • (2004) Trends Biotechnol. , vol.22 , pp. 72-79
    • De Vos, W.M.1    Hugenhollz, J.2
  • 14
    • 0033156414 scopus 로고    scopus 로고
    • Pyruvate metabolism in Lactococcus lactis is dependent upon glyceraldehyde-3-phosphate dehydrogenase activity
    • Even, S., C. Garrigues, P. Loubiere, N. D. Lindley, and M. Cocaign-Bousquet. 1999. Pyruvate metabolism in Lactococcus lactis is dependent upon glyceraldehyde-3-phosphate dehydrogenase activity. Metab. Eng. 1:198-205.
    • (1999) Metab. Eng. , vol.1 , pp. 198-205
    • Even, S.1    Garrigues, C.2    Loubiere, P.3    Lindley, N.D.4    Cocaign-Bousquet, M.5
  • 15
    • 0034967213 scopus 로고    scopus 로고
    • Molecular physiology of sugar catabolism in Lactococcus lactis IL1403
    • Even, S., N. D. Lindley, and M. Cocaign-Bousquet. 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
  • 17
    • 0035919866 scopus 로고    scopus 로고
    • Regulation of pyruvate metabolism in Lactococcus lactis depends on the imbalance between catabolism and anabolism
    • Garrigues, C., M. Mercade, M. Cocaign-Bousquet, N. D. Lindley, and P. Loubiere, P. 2001. Regulation of pyruvate metabolism in Lactococcus lactis depends on the imbalance between catabolism and anabolism. Biotechnol. Bioeng. 74:108-115.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 108-115
    • Garrigues, C.1    Mercade, M.2    Cocaign-Bousquet, M.3    Lindley, N.D.4    Loubiere, P.P.5
  • 18
    • 1642296584 scopus 로고    scopus 로고
    • Engineering Lactococcus lactis for production of mannitol: High yields from food-grade strains deficient in lactate dehydrogenase and the mannitol transport system
    • Gaspar. P., A. R. Neves, A. Ramos, M. J. Gasson, C. A. Shearman, and H. Santos. 2004. Engineering Lactococcus lactis for production of mannitol: high yields from food-grade strains deficient in lactate dehydrogenase and the mannitol transport system. Appl. Environ. Microbiol. 70:1466-1474.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1466-1474
    • Gaspar, P.1    Neves, A.R.2    Ramos, A.3    Gasson, M.J.4    Shearman, C.A.5    Santos, H.6
  • 19
    • 0020600404 scopus 로고
    • Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing
    • Gasson, M. J. 1983. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154:1-9.
    • (1983) J. Bacteriol. , vol.154 , pp. 1-9
    • Gasson, M.J.1
  • 20
    • 0024278871 scopus 로고
    • Extended monod kinetics for substrate, product and cell inhibition
    • Han, K., and O. Levenspiel. 1988. Extended monod kinetics for substrate, product and cell inhibition. Biotechnol. Bioeng. 32:430-437.
    • (1988) Biotechnol. Bioeng. , vol.32 , pp. 430-437
    • Han, K.1    Levenspiel, O.2
  • 21
    • 0016631203 scopus 로고
    • Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range
    • Hess, H. H., and J. E. Derr. 1975. Assay of inorganic and organic phosphorus in the 0.1-5 nanomole range. Anal. Biochem. 63:607-613.
    • (1975) Anal. Biochem. , vol.63 , pp. 607-613
    • Hess, H.H.1    Derr, J.E.2
  • 23
    • 18344414729 scopus 로고    scopus 로고
    • L-Lactic acid production from whole wheat flour hydrolysate using strains of lactobacilli and lactococci
    • Hofvendahl, K., and B. Hahn-Hägerdal. 1997. L-Lactic acid production from whole wheat flour hydrolysate using strains of lactobacilli and lactococci. Enzyme Microb. Technol. 20:301-307.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 301-307
    • Hofvendahl, K.1    Hahn-Hägerdal, B.2
  • 24
    • 0033066096 scopus 로고    scopus 로고
    • Effect of temperature and pH on growth and product formation of Lactococcus lactis ssp. lactis ATCC 19435 growing on maltose
    • Hofvendahl, K., E. W. J. van Niel, and B. Hahn-Hägerdal. 1999. Effect of temperature and pH on growth and product formation of Lactococcus lactis ssp. lactis ATCC 19435 growing on maltose. Appl. Microbiol. Biotechnol. 51:669-672.
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 669-672
    • Hofvendahl, K.1    Van Niel, E.W.J.2    Hahn-Hägerdal, B.3
  • 25
  • 27
    • 0015380759 scopus 로고
    • Factors affecting the activity of the lactate dehydrognease of Streptococcus cremoris
    • Jonas, H. A., R. F. Anders, and G. R. Jago. 1972. Factors affecting the activity of the lactate dehydrognease of Streptococcus cremoris. J. Bacteriol. 111:397-403.
    • (1972) J. Bacteriol. , vol.111 , pp. 397-403
    • Jonas, H.A.1    Anders, R.F.2    Jago, G.R.3
  • 28
    • 0036694240 scopus 로고    scopus 로고
    • Experimental determination of control of glycolysis in Lactococcus lactis
    • Koebmann, B. J., H. W. Andersen, C. Solem, and P. R. Jensen. 2002. Experimental determination of control of glycolysis in Lactococcus lactis. Antonie Leeuwenhoek 82:237-248.
    • (2002) Antonie Leeuwenhoek , vol.82 , pp. 237-248
    • Koebmann, B.J.1    Andersen, H.W.2    Solem, C.3    Jensen, P.R.4
  • 29
    • 0036727253 scopus 로고    scopus 로고
    • Expression of genes encoding F(1)-ATPase results in uncoupling of glycolysis from biomass production in Lactococcus lactis
    • Koebmann, B. J., C. Solem, M. B. Pedersen, D. Nilsson, and P. R. Jensen. 2002. Expression of genes encoding F(1)-ATPase results in uncoupling of glycolysis from biomass production in Lactococcus lactis. Appl. Environ. Microbiol. 68:4274-4282.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4274-4282
    • Koebmann, B.J.1    Solem, C.2    Pedersen, M.B.3    Nilsson, D.4    Jensen, P.R.5
  • 30
    • 0035486814 scopus 로고    scopus 로고
    • Physiological role of β-phosphoglucomutase in Lactococcus lactis
    • Levander, F., U. Andersson, and P. Rådström. 2001. Physiological role of β-phosphoglucomutase in Lactococcus lactis. Appl. Environ. Microbiol. 67:4546-4553.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4546-4553
    • Levander, F.1    Andersson, U.2    Rådström, P.3
  • 31
    • 0022881553 scopus 로고
    • Phosphorus-31 NMR studies of maltose and glucose metabolism in Streptococcus lactis
    • Lohmeier-Vogel, E. M., B. Hahn-Hagerdahl, and H. J. Vogel. 1986. Phosphorus-31 NMR studies of maltose and glucose metabolism in Streptococcus lactis. Appl. Microbiol. Biotechnol. 25:43-51.
    • (1986) Appl. Microbiol. Biotechnol. , vol.25 , pp. 43-51
    • Lohmeier-Vogel, E.M.1    Hahn-Hagerdahl, B.2    Vogel, H.J.3
  • 32
    • 0014687517 scopus 로고
    • Malaie utilization by a group D Streptococcus. II. Evidence for allosteric inhibition of an inducible malate dehydrogenase (decarboxylating) by ATP and glycolytic intermediate products
    • London, J., and E. Y. Meyer. 1969. Malaie utilization by a group D Streptococcus. II. Evidence for allosteric inhibition of an inducible malate dehydrogenase (decarboxylating) by ATP and glycolytic intermediate products. Biochim. Biophys. Acta 178:205-212.
    • (1969) Biochim. Biophys. Acta , vol.178 , pp. 205-212
    • London, J.1    Meyer, E.Y.2
  • 34
    • 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. V. Jokumsen, J. Villadsen, H. Israelsen, and J. Arnau. 2002. 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.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 338-344
    • Melchiorsen, C.R.1    Jokumsen, K.V.2    Villadsen, J.3    Israelsen, H.4    Arnau, J.5
  • 36
    • 0033946341 scopus 로고    scopus 로고
    • Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo
    • Moritz, B., K. Striegel, A. A. De Graaf, and H. Sahm. 2000. Kinetic properties of the glucose-6-phosphate and 6-phosphogluconate dehydrogenases from Corynebacterium glutamicum and their application for predicting pentose phosphate pathway flux in vivo. Eur. J. Biochem. 267:3442-3452.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3442-3452
    • Moritz, B.1    Striegel, K.2    De Graaf, A.A.3    Sahm, H.4
  • 38
    • 0036110805 scopus 로고    scopus 로고
    • Synchronized fresh cell bioreactor system for continuous L-(+)-lactic acid production using Lactococcus lactis IO-1 in hydrolysed sago starch
    • Nolasco-Hipolito, C., T. Matsunaka, G. Kobayashi, K. Sonomoto, and A. Ishizaki. 2002. Synchronized fresh cell bioreactor system for continuous L-(+)-lactic acid production using Lactococcus lactis IO-1 in hydrolysed sago starch. J. Biosci. Bioeng. 93:281-287.
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 281-287
    • Nolasco-Hipolito, C.1    Matsunaka, T.2    Kobayashi, G.3    Sonomoto, K.4    Ishizaki, A.5
  • 39
    • 0033984722 scopus 로고    scopus 로고
    • 14C-labeled substrates between catabolic and anabolic pathways
    • 14C-labeled substrates between catabolic and anabolic pathways. J. Bacteriol. 182:1136-1143.
    • (2000) J. Bacteriol. , vol.182 , pp. 1136-1143
    • Novak, L.1    Loubiere, P.2
  • 40
    • 10644295535 scopus 로고    scopus 로고
    • Acidic proteome of growing and resting Lactococcus lactis metabolizing maltose
    • in press
    • Palmfeldt, J., F. Levander, B. Hahn-Hägerdal, and P. James. Acidic proteome of growing and resting Lactococcus lactis metabolizing maltose. Proteomics, in press.
    • Proteomics
    • Palmfeldt, J.1    Levander, F.2    Hahn-Hägerdal, B.3    James, P.4
  • 41
    • 0023491513 scopus 로고
    • Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis
    • Poolman, B., B. Bosman, J. Kiers, and W. N. Konings. 1987. Control of glycolysis by glyceraldehyde-3-phosphate dehydrogenase in Streptococcus cremoris and Streptococcus lactis. J. Bacteriol. 169:5887-5890.
    • (1987) J. Bacteriol. , vol.169 , pp. 5887-5890
    • Poolman, B.1    Bosman, B.2    Kiers, J.3    Konings, W.N.4
  • 42
    • 1842368457 scopus 로고    scopus 로고
    • Product formation and phosphoglucomutase activities in Lactococcus lactis: Cloning and characterization of a novel phosphoglucomutase gene
    • Qian, N., G. A. Stanley, A. Bunte, and P. Rådström. 1997. Product formation and phosphoglucomutase activities in Lactococcus lactis: cloning and characterization of a novel phosphoglucomutase gene. Microbiology 143:855-865.
    • (1997) Microbiology. , vol.143 , pp. 855-865
    • Qian, N.1    Stanley, G.A.2    Bunte, A.3    Rådström, P.4
  • 43
    • 0028021801 scopus 로고
    • Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp. lactis and their regulation in maltose-utilizing and glucose-utilizing cells
    • Qian, N., G. A. Stanley, B. Hahn-Hägerdal, and P. Rådström. 1994. Purification and characterization of two phosphoglucomutases from Lactococcus lactis subsp. lactis and their regulation in maltose-utilizing and glucose-utilizing cells. J. Bacteriol. 176:5304-5311.
    • (1994) J. Bacteriol. , vol.176 , pp. 5304-5311
    • Qian, N.1    Stanley, G.A.2    Hahn-Hägerdal, B.3    Rådström, P.4
  • 44
    • 0015856129 scopus 로고
    • Phosphotransacetylase from Bacillus subtilis: Purification and physiological studies
    • Rado, T. A., and J. A. Hoch. 1973. Phosphotransacetylase from Bacillus subtilis: purification and physiological studies. Biochim. Biophys. Acta 321:114-125.
    • (1973) Biochim. Biophys. Acta , vol.321 , pp. 114-125
    • Rado, T.A.1    Hoch, J.A.2
  • 45
    • 0028926047 scopus 로고
    • Energetics of bacterial growth: Balance of anabolic and catabolic reactions
    • Russell, J. B., and G. M. Cook. 1995. Energetics of bacterial growth: balance of anabolic and catabolic reactions. Microbiol. Rev. 59:48-62.
    • (1995) Microbiol. Rev. , vol.59 , pp. 48-62
    • Russell, J.B.1    Cook, G.M.2
  • 47
    • 0028948131 scopus 로고
    • The influence of limiting and nonlimiting growth-conditions on glucose and maltose metabolism in Lactococcus lactis ssp. lactis strains
    • Sjöberg, A., I. Persson, M. Quednau, and B. Hahn-Hägerdal. 1995. The influence of limiting and nonlimiting growth-conditions on glucose and maltose metabolism in Lactococcus lactis ssp. lactis strains. Appl. Microbiol. Biotechnol. 42:931-938.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 931-938
    • Sjöberg, A.1    Persson, I.2    Quednau, M.3    Hahn-Hägerdal, B.4
  • 48
    • 0037371326 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363
    • Solem, C., B. J. Koebmann, and P. R. Jensen. 2003. Glyceraldehyde-3- phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363. J. Bacteriol. 185:1564-1571.
    • (2003) J. Bacteriol. , vol.185 , pp. 1564-1571
    • Solem, C.1    Koebmann, B.J.2    Jensen, P.R.3
  • 49
    • 0018357964 scopus 로고
    • Change from homo-fermentation to heterolactic fermentation by Streptococcus lactis resulting from glucose limitation in anaerobic chemostat cultures
    • Thomas, T. D., D. C. Ellwood, and V. M. C. Longyear. 1979. Change from homo-fermentation 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, D.C.2    Longyear, V.M.C.3
  • 50
    • 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
  • 51
    • 0017087888 scopus 로고
    • Characteristics and energy requirements of an alpha amino isobutyric acid transport system in Streptococcus lactis
    • Thompson, J. 1976. Characteristics and energy requirements of an alpha amino isobutyric acid transport system in Streptococcus lactis. J. Bacteriol. 127:719-730.
    • (1976) J. Bacteriol. , vol.127 , pp. 719-730
    • Thompson, J.1
  • 52
    • 0021287404 scopus 로고
    • 14C fluorography in studies of glycolysis and regulation of pyruvate kinase in Streptococcus lactis
    • 14C fluorography in studies of glycolysis and regulation of pyruvate kinase in Streptococcus lactis. J. Bacteriol. 158:791-800.
    • (1984) J. Bacteriol. , vol.158 , pp. 791-800
    • Thompson, J.1    Torchia, D.A.2
  • 53
    • 0036693775 scopus 로고    scopus 로고
    • Global control of sugar metabolism: A Gram-positive solution
    • Titgemeyer, F., and W. Hillen. 2002. Global control of sugar metabolism: a Gram-positive solution. Antonie Leeuwenhoek 82:59-71.
    • (2002) Antonie Leeuwenhoek , vol.82 , pp. 59-71
    • Titgemeyer, F.1    Hillen, W.2
  • 55
    • 0036729482 scopus 로고    scopus 로고
    • Formation and conversion of oxygen metabolites by Lactococcus lactis subsp. lactis ATCC 19435 under different growth conditions
    • Van Niel, E. W. J., K. Hofrendahl, and B. Hahn-Hägerdal. 2002. Formation and conversion of oxygen metabolites by Lactococcus lactis subsp. lactis ATCC 19435 under different growth conditions. Appl. Environ. Microbiol. 68:4350-4356.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4350-4356
    • Van Niel, E.W.J.1    Hofrendahl, K.2    Hahn-Hägerdal, B.3
  • 56
    • 0014547338 scopus 로고
    • Metabolic control and structure of glycolytic enzymes. VI. Competitive inhibition of yeast glyceraldehyde 3-phosphate dehydrogenase by cyclic adenosine monophosphate, adenosine triphosphate, and other adenine-containing compounds
    • Yang, S. T., and W. C. Deal, Jr. 1969. Metabolic control and structure of glycolytic enzymes. VI. Competitive inhibition of yeast glyceraldehyde 3-phosphate dehydrogenase by cyclic adenosine monophosphate, adenosine triphosphate, and other adenine-containing compounds. Biochemistry 8:2806-2813.
    • (1969) Biochemistry , vol.8 , pp. 2806-2813
    • Yang, S.T.1    Deal Jr., W.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.