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Volumn 145, Issue 6, 1999, Pages 1375-1380

Lactococcus lactis contains only one glutamate decarboxylase gene

Author keywords

Acid resistance; gadB; Glutamate decarboxylase; Lactococcus lactis

Indexed keywords

BACTERIAL ENZYME; GLUTAMATE DECARBOXYLASE;

EID: 0032981370     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-145-6-1375     Document Type: Article
Times cited : (124)

References (29)
  • 1
    • 0020593886 scopus 로고
    • Simple and rapid method for isolating large plasmid DNA from lactic streptococci
    • Anderson, D. G. & McKay, L. L. (1983). Simple and rapid method for isolating large plasmid DNA from lactic streptococci. Appl Environ Microbiol 46, 549-552.
    • (1983) Appl Environ Microbiol , vol.46 , pp. 549-552
    • Anderson, D.G.1    McKay, L.L.2
  • 2
    • 0027203970 scopus 로고
    • A plant glutamate decarboxylase containing a calmodulin binding domain
    • Baum, G., Chen, Y., Arazi, T., Takatsuji, H. & Fromm, H. (1993). A plant glutamate decarboxylase containing a calmodulin binding domain. J Biol Chem 268, 19610-19617.
    • (1993) J Biol Chem , vol.268 , pp. 19610-19617
    • Baum, G.1    Chen, Y.2    Arazi, T.3    Takatsuji, H.4    Fromm, H.5
  • 4
    • 0014429449 scopus 로고
    • Arginine decarboxylase from Escherichia coli
    • Blethen, S. L., Boeker, E. A. & Snell, E. E. (1968). Arginine decarboxylase from Escherichia coli. J Biol Chem 243, 1671-1677.
    • (1968) J Biol Chem , vol.243 , pp. 1671-1677
    • Blethen, S.L.1    Boeker, E.A.2    Snell, E.E.3
  • 5
    • 0030470440 scopus 로고    scopus 로고
    • Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli
    • De Biase, D., Tramonti, A., John, R. A. & Bossa, F. (1996). Isolation, overexpression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expr Purif 8, 430-438.
    • (1996) Protein Expr Purif , vol.8 , pp. 430-438
    • De Biase, D.1    Tramonti, A.2    John, R.A.3    Bossa, F.4
  • 6
    • 0022272437 scopus 로고
    • L-glutamate decarboxylase from bacteria
    • Fonda, M. L. (1985). L-Glutamate decarboxylase from bacteria. Methods Enzymol 113, 11-16.
    • (1985) Methods Enzymol , vol.113 , pp. 11-16
    • Fonda, M.L.1
  • 7
    • 77957002734 scopus 로고
    • Analytical disc gel electrophoresis
    • Gabriel, O. (1971). Analytical disc gel electrophoresis. Methods Enzymol 22, 565-578.
    • (1971) Methods Enzymol , vol.22 , pp. 565-578
    • Gabriel, O.1
  • 8
    • 0002116418 scopus 로고
    • The bacterial amino acid decarboxylases
    • Gale, E. F. (1946). The bacterial amino acid decarboxylases. Adv Enzymol 6, 1-32.
    • (1946) Adv Enzymol , vol.6 , pp. 1-32
    • Gale, E.F.1
  • 11
    • 0025048267 scopus 로고
    • Prokaryotic and eukaryotic pyridoxaldependent decarboxylases are homologous
    • Jackson, F. R. (1990). Prokaryotic and eukaryotic pyridoxaldependent decarboxylases are homologous. J Mol Evol 31, 325-329.
    • (1990) J Mol Evol , vol.31 , pp. 325-329
    • Jackson, F.R.1
  • 12
    • 0001763944 scopus 로고
    • Bioenergetics of lactic acid bacteria: Cytoplasmic pH and osmotolerance
    • Kashket E. R. (1987). Bioenergetics of lactic acid bacteria: cytoplasmic pH and osmotolerance. FEMS Microbiol Rev 46, 233-244.
    • (1987) FEMS Microbiol Rev , vol.46 , pp. 233-244
    • Kashket, E.R.1
  • 13
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0006396605 scopus 로고    scopus 로고
    • Stability of lactic acid bacteria in fermented milk
    • Edited by S. Salminen & A. von Wright. New York: Marcel Dekker
    • Lee, Y.-K. & Wong, S.-F. (1998). Stability of lactic acid bacteria in fermented milk. In Lactic Acid Bacteria: Microbiology and Functional Aspects, 2nd edn, pp. 103-114. Edited by S. Salminen & A. von Wright. New York: Marcel Dekker.
    • (1998) Lactic Acid Bacteria: Microbiology and Functional Aspects, 2nd Edn , pp. 103-114
    • Lee, Y.-K.1    Wong, S.-F.2
  • 16
    • 0025287371 scopus 로고
    • Acid tolerance of Leuconostoc mesenteroides and Lactobacillus plantarum
    • McDonald, L. C., Fleming, H. P. & Hassan, H. M. (1990). Acid tolerance of Leuconostoc mesenteroides and Lactobacillus plantarum. Appl Environ Microbiol 56, 2120-2124.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 2120-2124
    • McDonald, L.C.1    Fleming, H.P.2    Hassan, H.M.3
  • 17
    • 0026540827 scopus 로고
    • The amino acid sequence of glutamate decarboxylase from Escherichia coli
    • Maras, B., Sweeney, G., Barra, D., Bossa, F. & John, R. A. (1992). The amino acid sequence of glutamate decarboxylase from Escherichia coli. Eur J Biochem 204, 93-98.
    • (1992) Eur J Biochem , vol.204 , pp. 93-98
    • Maras, B.1    Sweeney, G.2    Barra, D.3    Bossa, F.4    John, R.A.5
  • 18
    • 0031570297 scopus 로고    scopus 로고
    • The N-terminal sequence of Lactococcus lactis phosphoglucose isomerase purified by affinity chromatography differs from the other species
    • Nomura, M., Nakajima, I., Matsuzaki, M., Kimoto, H., Suzuki, I. & Aso, H. (1997). The N-terminal sequence of Lactococcus lactis phosphoglucose isomerase purified by affinity chromatography differs from the other species. Arch Biochem Biophys 341, 315-320.
    • (1997) Arch Biochem Biophys , vol.341 , pp. 315-320
    • Nomura, M.1    Nakajima, I.2    Matsuzaki, M.3    Kimoto, H.4    Suzuki, I.5    Aso, H.6
  • 19
    • 0032087827 scopus 로고    scopus 로고
    • Production of γ-aminobutyric acid by cheese starters during cheese ripening
    • Nomura, M., Kimoto, H., Someya, Y., Furukawa, S. & Suzuki, I. (1998). Production of γ-aminobutyric acid by cheese starters during cheese ripening. J Dairy Sci 81, 1486-1491.
    • (1998) J Dairy Sci , vol.81 , pp. 1486-1491
    • Nomura, M.1    Kimoto, H.2    Someya, Y.3    Furukawa, S.4    Suzuki, I.5
  • 20
    • 0015957627 scopus 로고
    • Purification and physical properties of inducible Escherichia coli lysine decarboxylase
    • Sabo, D. L., Boeker, E. A., Byers, B., Waron, H. & Fisher, E. H. (1974). Purification and physical properties of inducible Escherichia coli lysine decarboxylase. Biochemistry 13, 662-670.
    • (1974) Biochemistry , vol.13 , pp. 662-670
    • Sabo, D.L.1    Boeker, E.A.2    Byers, B.3    Waron, H.4    Fisher, E.H.5
  • 21
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, H. & Miura, K. (1963). Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72, 619-629.
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.2
  • 23
    • 0031984335 scopus 로고    scopus 로고
    • A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation
    • Sanders, J. W., Leenhouts, K., Burghoorn, J., Brands, J. R., Venema, G. & Kok, J. (1998). A chloride-inducible acid resistance mechanism in Lactococcus lactis and its regulation. Mol Microbiol 27, 299-310.
    • (1998) Mol Microbiol , vol.27 , pp. 299-310
    • Sanders, J.W.1    Leenhouts, K.2    Burghoorn, J.3    Brands, J.R.4    Venema, G.5    Kok, J.6
  • 24
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger, F., Nicklen, S. & Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74, 5463-5467.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 25
    • 0031806146 scopus 로고    scopus 로고
    • Acid stress, anaerobiosis and gadCB: Lessons from Lactococcus lactis and Escherichia coli
    • Small, P. L. C. & Waterman, S. R. (1998). Acid stress, anaerobiosis and gadCB: lessons from Lactococcus lactis and Escherichia coli. Trends Microbiol 6, 214-216.
    • (1998) Trends Microbiol , vol.6 , pp. 214-216
    • Small, P.L.C.1    Waterman, S.R.2
  • 26
    • 0026641173 scopus 로고
    • Escberichia coli has two homologous glutamate decarboxylase genes that map to distinct loci
    • Smith, D. K., Kassam, T., Singh, B. & Elliott, J. F. (1992). Escberichia coli has two homologous glutamate decarboxylase genes that map to distinct loci. J Bacteriol 174, 5820-5826.
    • (1992) J Bacteriol , vol.174 , pp. 5820-5826
    • Smith, D.K.1    Kassam, T.2    Singh, B.3    Elliott, J.F.4
  • 28
    • 0029839533 scopus 로고    scopus 로고
    • S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneri
    • S-dependent genes associated with the stationary-phase acid-resistance phenotype of Shigella flexneri. Mol Microbiol 21, 925-940.
    • (1996) Mol Microbiol , vol.21 , pp. 925-940
    • Waterman, S.R.1    Small, P.L.C.2
  • 29
    • 0001242796 scopus 로고    scopus 로고
    • Eye and crack formation in cheese by carbon dioxide from decarboxylation of glutamic acid
    • Zoon, P. & Allersma, D. (1996). Eye and crack formation in cheese by carbon dioxide from decarboxylation of glutamic acid. Neth Milk Dairy J 50, 309-318.
    • (1996) Neth Milk Dairy J , vol.50 , pp. 309-318
    • Zoon, P.1    Allersma, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.