메뉴 건너뛰기




Volumn 179, Issue 20, 1997, Pages 6285-6293

Dual role of α-acetolactate decarboxylase in Lactococcus lactis subsp. lactis

Author keywords

[No Author keywords available]

Indexed keywords

ACETOLACTATE SYNTHASE; CARBOXYLYASE; ISOLEUCINE; LEUCINE;

EID: 0030818011     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.20.6285-6293.1997     Document Type: Article
Times cited : (85)

References (61)
  • 1
    • 0022486410 scopus 로고
    • Biochemical comparison of the Neurospora crassa wild-type and the temperature-sensitive leucine-auxotroph mutant leu-5
    • Airas, R. K., J. Schischkoff, and F. Cramer. 1986. Biochemical comparison of the Neurospora crassa wild-type and the temperature-sensitive leucine-auxotroph mutant leu-5. Eur. J. Biochem. 158:51-56.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 51-56
    • Airas, R.K.1    Schischkoff, J.2    Cramer, F.3
  • 2
    • 0001246049 scopus 로고
    • Linkage map of Escherichia coli K-12, edition 7
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Bachmann, B. J. 1987. Linkage map of Escherichia coli K-12, edition 7, p. 807-876. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol. 2. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.2 , pp. 807-876
    • Bachmann, B.J.1
  • 3
    • 0027160241 scopus 로고
    • Effect of initial oxygen concentration on diacetyl and acetoin production by Lactococcus lactis subsp. lactis biovar. diacetylactis
    • Bassit, N., C. Y. Boquien, D. Picque, and G. Corrieu. 1993. Effect of initial oxygen concentration on diacetyl and acetoin production by Lactococcus lactis subsp. lactis biovar. diacetylactis. Appl. Environ. Microbiol. 59:1893-1897.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1893-1897
    • Bassit, N.1    Boquien, C.Y.2    Picque, D.3    Corrieu, G.4
  • 4
    • 0029867882 scopus 로고    scopus 로고
    • Effect of ilvBN-encoded α-acetolactate synthase expression on diacetyl production in Lactococcus lactis
    • Benson, K. H., J. J. Godon, P. Renault, H. G. Griffin, and M. J. Gasson. 1996. Effect of ilvBN-encoded α-acetolactate synthase expression on diacetyl production in Lactococcus lactis. Appl. Microbiol. Biotechnol. 45:107-111.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 107-111
    • Benson, K.H.1    Godon, J.J.2    Renault, P.3    Griffin, H.G.4    Gasson, M.J.5
  • 6
    • 0027151798 scopus 로고
    • High-efficiency gene inactivation and replacement system for gram-positive bacteria
    • Biswas, I., A. Gruss, S. D. Ehrlich, and E. Maguin. 1993. High-efficiency gene inactivation and replacement system for gram-positive bacteria. J. Bacteriol. 175:3628-3635.
    • (1993) J. Bacteriol. , vol.175 , pp. 3628-3635
    • Biswas, I.1    Gruss, A.2    Ehrlich, S.D.3    Maguin, E.4
  • 8
    • 0007849365 scopus 로고
    • Leucine biosynthesis in prokaryotes
    • K. M. Herrman and R. L. Somerville (ed.), Addison-Wesley, Reading, Mass.
    • Calvo, J. M. 1983. Leucine biosynthesis in prokaryotes, p. 267-284. In K. M. Herrman and R. L. Somerville (ed.), Amino-acid biosynthesis and genetic regulation. Addison-Wesley, Reading, Mass.
    • (1983) Amino-acid Biosynthesis and Genetic Regulation , pp. 267-284
    • Calvo, J.M.1
  • 9
    • 0019498353 scopus 로고
    • Effects of pH and sugar on acetoin production from citrate by Leuconostoc lactis
    • Cogan, T. M., M. O'Dowd, and D. Mellerick. 1981. Effects of pH and sugar on acetoin production from citrate by Leuconostoc lactis. Appl. Environ. Microbiol. 41:1-8.
    • (1981) Appl. Environ. Microbiol. , vol.41 , pp. 1-8
    • Cogan, T.M.1    O'Dowd, M.2    Mellerick, D.3
  • 10
    • 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
  • 11
    • 0025277025 scopus 로고
    • Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis
    • Diderichsen, B., U. Wedsted, L. Hedegaard, B. R. Jensen, and C. Sjoholm. 1990. Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis. J. Bacteriol. 172:4315-4321.
    • (1990) J. Bacteriol. , vol.172 , pp. 4315-4321
    • Diderichsen, B.1    Wedsted, U.2    Hedegaard, L.3    Jensen, B.R.4    Sjoholm, C.5
  • 12
    • 0023131480 scopus 로고
    • Regulation of acetohydroxy acid synthase in Corynebacterium glutamicum during fermentation of α-ketobutyrate to L-isoleucine
    • Eggleding, I., C. Cordes, L. Eggleding, and H. Sahm. 1987. Regulation of acetohydroxy acid synthase in Corynebacterium glutamicum during fermentation of α-ketobutyrate to L-isoleucine. Appl. Microbiol. Biotechnol. 25:346-351.
    • (1987) Appl. Microbiol. Biotechnol. , vol.25 , pp. 346-351
    • Eggleding, I.1    Cordes, C.2    Eggleding, L.3    Sahm, H.4
  • 13
    • 0030987623 scopus 로고    scopus 로고
    • Control of the shift from homolactic acid to mixed-acid fermentation in Lactococcus lactis: Predominant role of the NADH/NAD ratio
    • Garrigues, C., P. Loubière, N. D. Lindley, and M. Cocaign-Bousquet. 1997. Control of the shift from homolactic acid to mixed-acid fermentation in Lactococcus lactis: predominant role of the NADH/NAD ratio. J. Bacteriol. 179:5282-5287.
    • (1997) J. Bacteriol. , vol.179 , pp. 5282-5287
    • Garrigues, C.1    Loubière, P.2    Lindley, N.D.3    Cocaign-Bousquet, M.4
  • 14
    • 0026112862 scopus 로고
    • Purification and characterization of diacetyl reductase from chicken liver and Streptococcus lactis and enzymic determination of diacetyl and diketones
    • Gibson, T. D., S. M. Parker, and J. R. Woodward. 1991. Purification and characterization of diacetyl reductase from chicken liver and Streptococcus lactis and enzymic determination of diacetyl and diketones. Enzyme Microb. Technol. 13:171-178.
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 171-178
    • Gibson, T.D.1    Parker, S.M.2    Woodward, J.R.3
  • 15
    • 0015451865 scopus 로고
    • Biosynthesis of the parasporal inclusion of Bacillus thuringiensis: Half-life of its corresponding messenger RNA
    • Glatron, M. F., and G. Rapoport. 1972. Biosynthesis of the parasporal inclusion of Bacillus thuringiensis: half-life of its corresponding messenger RNA. Biochimie 54:1291-1301.
    • (1972) Biochimie , vol.54 , pp. 1291-1301
    • Glatron, M.F.1    Rapoport, G.2
  • 16
    • 0026781514 scopus 로고
    • Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis
    • Godon, J. J., M. C. Chopin, and S. D. Ehrlich. 1992. Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis. J. Bacteriol. 174:6580-6589.
    • (1992) J. Bacteriol. , vol.174 , pp. 6580-6589
    • Godon, J.J.1    Chopin, M.C.2    Ehrlich, S.D.3
  • 18
    • 0029949096 scopus 로고    scopus 로고
    • Imbalance of leucine flux in Lactococcus lactis and its use for the isolation of diacetyl-overproducing strains
    • Goupil, N., G. Corthier, S. D. Ehrlich, and P. Renault. 1996. Imbalance of leucine flux in Lactococcus lactis and its use for the isolation of diacetyl-overproducing strains. Appl. Environ. Microbiol. 62:2636-2640.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2636-2640
    • Goupil, N.1    Corthier, G.2    Ehrlich, S.D.3    Renault, P.4
  • 20
    • 0026643581 scopus 로고
    • Transcriptional regulation of the ilv-leu operon of Bacillus subtilis
    • Grandoni, J. A., S. A. Zahler, and J. M. Calvo. 1992. Transcriptional regulation of the ilv-leu operon of Bacillus subtilis. J. Bacteriol. 174:3212-3219.
    • (1992) J. Bacteriol. , vol.174 , pp. 3212-3219
    • Grandoni, J.A.1    Zahler, S.A.2    Calvo, J.M.3
  • 21
    • 0009387474 scopus 로고
    • Evidence for two distinct enzyme systems forming acetolactate in Aerobacter aerogenes
    • Halpern, Y. S., and H. E. Umbarger. 1959. Evidence for two distinct enzyme systems forming acetolactate in Aerobacter aerogenes. J. Biol. Chem. 234:3067-3071.
    • (1959) J. Biol. Chem. , vol.234 , pp. 3067-3071
    • Halpern, Y.S.1    Umbarger, H.E.2
  • 22
    • 0001441484 scopus 로고
    • Roles of citrate and acetoin in the metabolism of Streptococcus diacetilactis
    • Harvey, R. J., and E. B. Collins. 1963. Roles of citrate and acetoin in the metabolism of Streptococcus diacetilactis. J. Bacteriol. 86:1301-1307.
    • (1963) J. Bacteriol. , vol.86 , pp. 1301-1307
    • Harvey, R.J.1    Collins, E.B.2
  • 23
    • 0014939369 scopus 로고
    • Threonine deaminase from Bacillus subtilis. II. The steady state kinetic properties
    • Hatfield, G. W., and H. E. Umbarger. 1970. Threonine deaminase from Bacillus subtilis. II. The steady state kinetic properties. J. Biol. Chem 245:1742-1747.
    • (1970) J. Biol. Chem , vol.245 , pp. 1742-1747
    • Hatfield, G.W.1    Umbarger, H.E.2
  • 24
    • 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
  • 25
    • 0016481558 scopus 로고
    • Degradative acetolactate synthase of Bacillus subtilis: Purification and properties
    • Holtzclaw, W. D., and L. F. Chapman. 1975. Degradative acetolactate synthase of Bacillus subtilis: purification and properties. J. Bacteriol. 121:917-922.
    • (1975) J. Bacteriol. , vol.121 , pp. 917-922
    • Holtzclaw, W.D.1    Chapman, L.F.2
  • 26
    • 0027197407 scopus 로고
    • Citrate metabolism in lactic acid bacteria
    • Hugenholz, J. 1993. Citrate metabolism in lactic acid bacteria. FEMS Microbiol. Rev. 12:165-178.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 165-178
    • Hugenholz, J.1
  • 27
    • 0019890817 scopus 로고
    • Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization
    • Imbault, P., B. Colas, V. Sarantoglou, Y. Boulanger, and J. H. Weil. 1981. Chloroplast leucyl-tRNA synthetase from Euglena gracilis. Purification, kinetic analysis, and structural characterization. Biochemistry 20:5855-5859.
    • (1981) Biochemistry , vol.20 , pp. 5855-5859
    • Imbault, P.1    Colas, B.2    Sarantoglou, V.3    Boulanger, Y.4    Weil, J.H.5
  • 28
    • 0020318543 scopus 로고
    • Antimicrobial properties of diacetyl
    • Jay, J. M. 1982. Antimicrobial properties of diacetyl. Appl. Environ. Microbiol. 44:525-532.
    • (1982) Appl. Environ. Microbiol. , vol.44 , pp. 525-532
    • Jay, J.M.1
  • 29
    • 0016818029 scopus 로고
    • Physiological and biochemical role of the butanediol pathway in Aerobacter (Enterobacter) aerogenes
    • Johansen, L., K. Bryn, and F. C. Stormer. 1975. Physiological and biochemical role of the butanediol pathway in Aerobacter (Enterobacter) aerogenes. J. Bacteriol. 123:1124-1130.
    • (1975) J. Bacteriol. , vol.123 , pp. 1124-1130
    • Johansen, L.1    Bryn, K.2    Stormer, F.C.3
  • 30
    • 0040321443 scopus 로고
    • Enhancement of diacetyl production by a diacetyl-resistant mutant of citrate-positive Lactobacillus lactis ssp. lactis 3022 and by aerobic conditions of growth
    • Kaneto, T., Y. Watanabe, and H. Suzuki. 1990. Enhancement of diacetyl production by a diacetyl-resistant mutant of citrate-positive Lactobacillus lactis ssp. lactis 3022 and by aerobic conditions of growth. J. Dairy Sci. 73:291-298.
    • (1990) J. Dairy Sci. , vol.73 , pp. 291-298
    • Kaneto, T.1    Watanabe, Y.2    Suzuki, H.3
  • 31
    • 0027164654 scopus 로고
    • Isoleucine synthesis in Corynebacterium glutamicum: Molecular analysis of the ilvB-ilvN-ilvC operon
    • Keilhauer, C., L. Eggeling, and H. Sahm. 1993. Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon. J. Bacteriol. 175:5595-5603.
    • (1993) J. Bacteriol. , vol.175 , pp. 5595-5603
    • Keilhauer, C.1    Eggeling, L.2    Sahm, H.3
  • 32
    • 1842380608 scopus 로고
    • Regulation of leucine biosynthesis in lower eukaryotes
    • K. M. Herrman and R. L. Somerville (ed.), Addison-Wesley, Reading, Mass.
    • Kohlhaw, G. B. 1983. Regulation of leucine biosynthesis in lower eukaryotes, p. 285-299. In K. M. Herrman and R. L. Somerville (ed.), Amino-acid biosynthesis and genetic regulation. Addison-Wesley, Reading, Mass.
    • (1983) Amino-acid Biosynthesis and Genetic Regulation , pp. 285-299
    • Kohlhaw, G.B.1
  • 33
    • 0017653033 scopus 로고
    • Transcription termination at the trp operon attenuators of Escherichia coli and Salmonella typhimurium: RNA secondary structure and regulation of termination
    • Lee, F., and C. Yanofsky. 1977. Transcription termination at the trp operon attenuators of Escherichia coli and Salmonella typhimurium: RNA secondary structure and regulation of termination. Proc. Natl. Acad. Sci. USA 74:4365-4369.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4365-4369
    • Lee, F.1    Yanofsky, C.2
  • 35
    • 0026801262 scopus 로고
    • New thermosensitive plasmid for gram-positive bacteria
    • Maguin, E., P. Duwat, T. Hege, S. D. Ehrlich, and A. Gruss. 1992. New thermosensitive plasmid for gram-positive bacteria. J. Bacteriol. 174:5633-5638.
    • (1992) J. Bacteriol. , vol.174 , pp. 5633-5638
    • Maguin, E.1    Duwat, P.2    Hege, T.3    Ehrlich, S.D.4    Gruss, A.5
  • 36
    • 0028179066 scopus 로고
    • Identification and characterization of the α-acetolactate synthase gene from Lactococcus lactis subsp. lactis biovar diacetylactis
    • Marugg, J. D., D. Goelling, U. Stahl, A. M. Ledeboer, M. Y. Toonen, W. M. Verhue, and C. T. Verrips. 1994. Identification and characterization of the α-acetolactate synthase gene from Lactococcus lactis subsp. lactis biovar diacetylactis. Appl. Environ. Microbiol. 60:1390-1394.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1390-1394
    • Marugg, J.D.1    Goelling, D.2    Stahl, U.3    Ledeboer, A.M.4    Toonen, M.Y.5    Verhue, W.M.6    Verrips, C.T.7
  • 37
    • 0029084565 scopus 로고
    • Identification of the transcriptional activator controlling the butanediol fermentation pathway in Klebsiella terrigena
    • Mayer, D., V. Schlensog, and A. Bock. 1995. Identification of the transcriptional activator controlling the butanediol fermentation pathway in Klebsiella terrigena. J. Bacteriol. 177:5261-5269.
    • (1995) J. Bacteriol. , vol.177 , pp. 5261-5269
    • Mayer, D.1    Schlensog, V.2    Bock, A.3
  • 38
    • 0026621920 scopus 로고
    • Functional and structural analyses of threonine dehydratase from Corynebacterium glutamicum
    • Mockel, B., L. Eggeling, and H. Sahm. 1992. Functional and structural analyses of threonine dehydratase from Corynebacterium glutamicum. J. Bacteriol. 174:8065-8072.
    • (1992) J. Bacteriol. , vol.174 , pp. 8065-8072
    • Mockel, B.1    Eggeling, L.2    Sahm, H.3
  • 39
    • 0028176688 scopus 로고
    • Comparison of α-acetolactate synthase and α-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp
    • Monnet, C., V. Phalip, P. Schmitt, and C. Diviès. 1994. Comparison of α-acetolactate synthase and α-acetolactate decarboxylase in Lactococcus spp. and Leuconostoc spp. Biotechnol. Lett. 16:257-262.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 257-262
    • Monnet, C.1    Phalip, V.2    Schmitt, P.3    Diviès, C.4
  • 40
    • 0002272647 scopus 로고
    • Chemical composition of Escherichia coli
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Neidhardt, F. C. 1987. Chemical composition of Escherichia coli, p. 3-6. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol. 1. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.1 , pp. 3-6
    • Neidhardt, F.C.1
  • 41
    • 0028052909 scopus 로고
    • Leucine synthesis in Corynebacterium glutamicum: Enzyme activities, structure of LeuA, and effect of LeuA inactivation on lysine synthesis
    • Patek, M., K. Krumbach, L. Eggeling, and H. Sahm. 1994. Leucine synthesis in Corynebacterium glutamicum: enzyme activities, structure of LeuA, and effect of LeuA inactivation on lysine synthesis. Appl. Environ. Microbiol. 60:133-140.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 133-140
    • Patek, M.1    Krumbach, K.2    Eggeling, L.3    Sahm, H.4
  • 42
    • 0028169895 scopus 로고
    • Purification and properties of the alpha-acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118
    • Phalip, V., C. Monnet, P. Schmitt, P. Renault, J. J. Godon, and C. Divies. 1994. Purification and properties of the alpha-acetolactate decarboxylase from Lactococcus lactis subsp. lactis NCDO 2118. FEBS Lett. 351:95-99.
    • (1994) FEBS Lett. , vol.351 , pp. 95-99
    • Phalip, V.1    Monnet, C.2    Schmitt, P.3    Renault, P.4    Godon, J.J.5    Divies, C.6
  • 43
    • 0023955260 scopus 로고
    • Relation of growth of Streptococcus lactis and Streptococcus cremoris to amino acid transport
    • Poolman, B., and W. N. Konings. 1988. Relation of growth of Streptococcus lactis and Streptococcus cremoris to amino acid transport. J. Bacteriol. 170:700-707.
    • (1988) J. Bacteriol. , vol.170 , pp. 700-707
    • Poolman, B.1    Konings, W.N.2
  • 44
    • 0028177315 scopus 로고
    • 13C nuclear magnetic resonance studies of citrate and glucose cometabolism by Lactococcus lactis
    • 13C nuclear magnetic resonance studies of citrate and glucose cometabolism by Lactococcus lactis. Appl. Environ. Microbiol. 60:1739-1748.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1739-1748
    • Ramos, A.1    Jordan, K.N.2    Cogan, T.M.3    Santos, H.4
  • 46
    • 0027167447 scopus 로고
    • Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin
    • Renna, M. C., N. Najimudin, L. R. Winik, and S. A. Zahler. 1993. Regulation of the Bacillus subtilis alsS, alsD, and alsR genes involved in post-exponential-phase production of acetoin. J. Bacteriol. 175:3863-3875.
    • (1993) J. Bacteriol. , vol.175 , pp. 3863-3875
    • Renna, M.C.1    Najimudin, N.2    Winik, L.R.3    Zahler, S.A.4
  • 47
    • 0014273680 scopus 로고
    • Reaction sequence of leucine activation catalysed by leucyl-RNA synthetase. 1. Kinetic studies
    • Rouget, P., and F. Chapeville. 1968. Reaction sequence of leucine activation catalysed by leucyl-RNA synthetase. 1. Kinetic studies. Eur. J. Biochem. 4:305-309.
    • (1968) Eur. J. Biochem. , vol.4 , pp. 305-309
    • Rouget, P.1    Chapeville, F.2
  • 48
    • 0028979280 scopus 로고
    • An extended -10 promoter alone directs transcription of the DpnII operon of Streptococcus pneumoniae
    • Sabelnikov, A. G., B. Greenberg, and S. A. Lacks. 1995. An extended -10 promoter alone directs transcription of the DpnII operon of Streptococcus pneumoniae. J. Mol. Biol. 250:144-155.
    • (1995) J. Mol. Biol. , vol.250 , pp. 144-155
    • Sabelnikov, A.G.1    Greenberg, B.2    Lacks, S.A.3
  • 50
    • 0023992075 scopus 로고
    • Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon, D., and A. Chopin. 1988. Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70:559-566.
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 51
    • 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. J. C. 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.J.C.3    Hugenholtz, J.4
  • 52
    • 0025790130 scopus 로고
    • Citrate fermentation by Lactococcus and Leuconostoc spp
    • Starrenburg, M. J. C., and J. Hugenholtz. 1991. Citrate fermentation by Lactococcus and Leuconostoc spp. Appl. Environ. Microbiol. 57:3535-3540.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3535-3540
    • Starrenburg, M.J.C.1    Hugenholtz, J.2
  • 53
    • 0015853966 scopus 로고
    • Mechanism of feedback inhibition by leucine. Binding of leucine to wild-type and feedback-resistant α-isopropylmalate synthases and its structural consequences
    • Teng-Leary, E., and G. B. Kohlhaw. 1973. Mechanism of feedback inhibition by leucine. Binding of leucine to wild-type and feedback-resistant α-isopropylmalate synthases and its structural consequences. Biochemistry 12:2980-2986.
    • (1973) Biochemistry , vol.12 , pp. 2980-2986
    • Teng-Leary, E.1    Kohlhaw, G.B.2
  • 54
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi, B., and W. E. Sandine. 1975. Improved medium for lactic streptococci and their bacteriophages. Appl. Microbiol. 29:807-813.
    • (1975) Appl. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.1    Sandine, W.E.2
  • 55
    • 0000110242 scopus 로고
    • Regulation of sugar transport and metabolism in lactic acid bacteria
    • Thompson, J. 1987. Regulation of sugar transport and metabolism in lactic acid bacteria. FEMS Microbiol. Rev. 46:221-231.
    • (1987) FEMS Microbiol. Rev. , vol.46 , pp. 221-231
    • Thompson, J.1
  • 56
    • 0025254808 scopus 로고
    • Relationship between pyruvate utilization and acetoin production by Lactobacillus plantarum: Influence of carbon source, pyruvate concentration, and metabolic inhibitors
    • Tsau, J. L., and T. J. Montville. 1990. Relationship between pyruvate utilization and acetoin production by Lactobacillus plantarum: influence of carbon source, pyruvate concentration, and metabolic inhibitors. Food Biotechnol. 4:727-738.
    • (1990) Food Biotechnol. , vol.4 , pp. 727-738
    • Tsau, J.L.1    Montville, T.J.2
  • 57
    • 0006339667 scopus 로고
    • The biosynthesis of isoleucine and valine and its regulation
    • K. M. Herrman and R. L. Somerville (ed.), Addison-Wesley, Reading, Mass.
    • Umbarger, H. E. 1983. The biosynthesis of isoleucine and valine and its regulation, p. 245-266. In K. M. Herrman and R. L. Somerville (ed.), Amino-acid biosynthesis and genetic regulation. Addison-Wesley, Reading, Mass.
    • (1983) Amino-acid Biosynthesis and Genetic Regulation , pp. 245-266
    • Umbarger, H.E.1
  • 58
    • 0001348712 scopus 로고
    • Biosynthesis of the branched-chain amino acids
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Umbarger, H. E. 1987. Biosynthesis of the branched-chain amino acids, p. 353-367. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 353-367
    • Umbarger, H.E.1
  • 59
    • 0001271774 scopus 로고
    • Determination of diacetyl in dairy products containing α-acetolactic acid
    • Veringa, H. A., E. H. Verburg, and J. Stadhouders. 1984. Determination of diacetyl in dairy products containing α-acetolactic acid. Neth. Milk Dairy J. 38:251-263.
    • (1984) Neth. Milk Dairy J. , vol.38 , pp. 251-263
    • Veringa, H.A.1    Verburg, E.H.2    Stadhouders, J.3
  • 60
    • 0015846173 scopus 로고
    • Regulation of leucine biosynthesis in Bacillus subtilis
    • Ward, J. B., and S. A. Zahler. 1973. Regulation of leucine biosynthesis in Bacillus subtilis. J. Bacteriol. 116:727-735.
    • (1973) J. Bacteriol. , vol.116 , pp. 727-735
    • Ward, J.B.1    Zahler, S.A.2
  • 61
    • 84864301531 scopus 로고
    • A colorimetric determination of blood acetoin
    • Westerfeld, W. W. 1945. A colorimetric determination of blood acetoin. J. Biol. Chem. 16:495-502.
    • (1945) J. Biol. Chem. , vol.16 , pp. 495-502
    • Westerfeld, W.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.