메뉴 건너뛰기




Volumn 102, Issue 3, 2007, Pages 674-679

Construction of Lactobacillus plantarum strain with enhanced L-lysine yield

Author keywords

Aspartokinase; Dihydrodipicolinate synthase; Gene overexpression; L lysine overproduction; Lactobacillus plantarum; S 2 aminoethyl L cystein resistant mutant; Strain improvement

Indexed keywords

AMINO ACIDS; BACILLI; CLONING; PHYSIOLOGY;

EID: 33847047181     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2006.03174.x     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 0001782583 scopus 로고
    • β-Aspartokinase and β-aspartyl phosphate
    • Black, S. and Wright, N.G. (1955) β-Aspartokinase and β-aspartyl phosphate. J Biol Chem 213, 27-38.
    • (1955) J Biol Chem , vol.213 , pp. 27-38
    • Black, S.1    Wright, N.G.2
  • 2
    • 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
  • 3
    • 33646455178 scopus 로고    scopus 로고
    • Cloning of Lactobacillus plantarum IAM 12477 lysine biosynthetic genes encoding functional aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase
    • Cahyanto, M.N., Kawasaki, H., Fujiyama, K. and Seki, T. (2006a) Cloning of Lactobacillus plantarum IAM 12477 lysine biosynthetic genes encoding functional aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase. World J Microbiol Biotechnol 22, 409-416.
    • (2006) World J Microbiol Biotechnol , vol.22 , pp. 409-416
    • Cahyanto, M.N.1    Kawasaki, H.2    Fujiyama, K.3    Seki, T.4
  • 4
    • 30744458839 scopus 로고    scopus 로고
    • Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase in Lactobacillus plantarum
    • Cahyanto, M.N., Kawasaki, H., Nagashio, M., Fujiyama, K. and Seki, T. (2006b) Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase in Lactobacillus plantarum. Microbiology 152, 105-112.
    • (2006) Microbiology , vol.152 , pp. 105-112
    • Cahyanto, M.N.1    Kawasaki, H.2    Nagashio, M.3    Fujiyama, K.4    Seki, T.5
  • 5
    • 0025755467 scopus 로고
    • Control of the lysine biosynthesis sequence in Corynebacterium glutamicum as analyzed by overexpression of the individual corresponding genes
    • Cremer, J., Eggeling, L. and Sahm, H. (1991) Control of the lysine biosynthesis sequence in Corynebacterium glutamicum as analyzed by overexpression of the individual corresponding genes. Appl Environ Microbiol 57, 1746-1752.
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1746-1752
    • Cremer, J.1    Eggeling, L.2    Sahm, H.3
  • 6
    • 0024145176 scopus 로고
    • Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum
    • Cremer, J., Treptow, C., Eggeling, L. and Sahm, H. (1988) Regulation of enzymes of lysine biosynthesis in Corynebacterium glutamicum. J Gen Microbiol 134, 3221-3229.
    • (1988) J Gen Microbiol , vol.134 , pp. 3221-3229
    • Cremer, J.1    Treptow, C.2    Eggeling, L.3    Sahm, H.4
  • 7
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, W.J., Miller, J.F. and Ragsdale, C.W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res 16, 6127-6145.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 8
    • 0031963010 scopus 로고    scopus 로고
    • Improved L-lysine yield with Corynebacterium glutamicum: Use of dapA resulting in increased flux combined with growth limitation
    • Eggeling, L., Oberle, S. and Sahm, H. (1998) Improved L-lysine yield with Corynebacterium glutamicum: use of dapA resulting in increased flux combined with growth limitation. Appl Microbiol Biotechnol 49, 24-30.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 24-30
    • Eggeling, L.1    Oberle, S.2    Sahm, H.3
  • 10
    • 0004766628 scopus 로고
    • Aspartic semialdehyde dehydrogenase
    • Hegeman, G.D., Cohen, G.N. and Morgan, R. (1970) Aspartic semialdehyde dehydrogenase. Meth Enzymol 17A, 708-713.
    • (1970) Meth Enzymol , vol.17 A , pp. 708-713
    • Hegeman, G.D.1    Cohen, G.N.2    Morgan, R.3
  • 11
    • 0025802142 scopus 로고
    • Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum
    • Kalinowski, J., Cremer, J., Bachmann, B., Eggeling, L., Sahm, H. and Puehler, A. (1991) Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum. Mol Microbiol 5, 1197-1204.
    • (1991) Mol Microbiol , vol.5 , pp. 1197-1204
    • Kalinowski, J.1    Cremer, J.2    Bachmann, B.3    Eggeling, L.4    Sahm, H.5    Puehler, A.6
  • 12
    • 0033969932 scopus 로고    scopus 로고
    • Development of a host-vector system for Lactobacillus plantarum L137 isolated from a traditional fermented food produced in the Philippines
    • Kaneko, Y., Kobayashi, H., Kiatpapan, P., Nishimoto, T., Napitupulu, R., Ono, H. and Murooka, Y. (2000) Development of a host-vector system for Lactobacillus plantarum L137 isolated from a traditional fermented food produced in the Philippines. J Biosci Bioeng 89, 62-67.
    • (2000) J Biosci Bioeng , vol.89 , pp. 62-67
    • Kaneko, Y.1    Kobayashi, H.2    Kiatpapan, P.3    Nishimoto, T.4    Napitupulu, R.5    Ono, H.6    Murooka, Y.7
  • 13
    • 0033039869 scopus 로고    scopus 로고
    • Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli
    • Kikuchi, Y., Kojima, H. and Tanaka, T. (1999) Mutational analysis of the feedback sites of lysine-sensitive aspartokinase of Escherichia coli. FEMS Microbiol Lett 173, 211-215.
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 211-215
    • Kikuchi, Y.1    Kojima, H.2    Tanaka, T.3
  • 15
    • 0019856610 scopus 로고
    • Multiple nutritional requirements of lactobacilli: Genetic lesions affecting amino acid biosynthetic pathways
    • Morishita, T., Deguchi, Y., Yajima, M., Sakurai, T. and Yura, T. (1981) Multiple nutritional requirements of lactobacilli: Genetic lesions affecting amino acid biosynthetic pathways. J Bacteriol 148, 64-71.
    • (1981) J Bacteriol , vol.148 , pp. 64-71
    • Morishita, T.1    Deguchi, Y.2    Yajima, M.3    Sakurai, T.4    Yura, T.5
  • 16
    • 0027513393 scopus 로고
    • Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I
    • Omori, K., Imai, Y., Suzuki, S. and Komatsubara, S. (1993) Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I. J Bacteriol 175, 785-794.
    • (1993) J Bacteriol , vol.175 , pp. 785-794
    • Omori, K.1    Imai, Y.2    Suzuki, S.3    Komatsubara, S.4
  • 17
    • 0014213654 scopus 로고
    • Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K12
    • Patte, J.C., Le Bras, G. and Cohen, G.N. (1967) Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K12. Biochim Biophys Acta 136, 245-257.
    • (1967) Biochim Biophys Acta , vol.136 , pp. 245-257
    • Patte, J.C.1    Le Bras, G.2    Cohen, G.N.3
  • 19
    • 0026761151 scopus 로고
    • Isolation and prominent characteristics of an L-lysine hyperproducing strain of Corynebacterium glutamicum
    • Schrumpf, B., Eggeling, L. and Sahm, H. (1992) Isolation and prominent characteristics of an L-lysine hyperproducing strain of Corynebacterium glutamicum. Appl Microbiol Biotechnol 37, 566-571.
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 566-571
    • Schrumpf, B.1    Eggeling, L.2    Sahm, H.3
  • 20
    • 0014870726 scopus 로고
    • Genetically desensitized aspartate kinase to the concerted feedbeck inhibition in Brevibacterium flavum
    • Shiio, I., Miyajima, R. and Sano, K. (1970) Genetically desensitized aspartate kinase to the concerted feedbeck inhibition in Brevibacterium flavum. J Biochem 68, 701-710.
    • (1970) J Biochem , vol.68 , pp. 701-710
    • Shiio, I.1    Miyajima, R.2    Sano, K.3
  • 21
    • 0017842716 scopus 로고
    • L-Lysine production by S-(2-aminoethyl) L-cysteine and α-amino-β-hydroxyvaleric acid resistant mutants of Brevibacterium lactofermentum
    • Tosaka, O., Takinami, K. and Hirose, Y. (1978) L-Lysine production by S-(2-aminoethyl) L-cysteine and α-amino-β-hydroxyvaleric acid resistant mutants of Brevibacterium lactofermentum. Agric Biol Chem 42, 745-752.
    • (1978) Agric Biol Chem , vol.42 , pp. 745-752
    • Tosaka, O.1    Takinami, K.2    Hirose, Y.3
  • 22
    • 33847039928 scopus 로고
    • Spectrophotometric determination of lysine
    • Vogel, H.J. and Shimura, Y. (1971) Spectrophotometric determination of lysine. Methods Enzymol 17B, 228-229.
    • (1971) Methods Enzymol , vol.17 B , pp. 228-229
    • Vogel, H.J.1    Shimura, Y.2
  • 23
    • 0017105729 scopus 로고
    • The regulation of diaminopimelate decarboxylase activity in Escherichia coli strain w
    • White, P.J. (1976) The regulation of diaminopimelate decarboxylase activity in Escherichia coli strain w. J Gen Microbiol 96, 51-62.
    • (1976) J Gen Microbiol , vol.96 , pp. 51-62
    • White, P.J.1
  • 24
    • 0016271651 scopus 로고
    • Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis
    • Yamakura, F., Ikeda, Y., Kimura, K. and Sasakawa, T. (1974) Partial purification and some properties of pyruvate-aspartic semialdehyde condensing enzyme from sporulating Bacillus subtilis. J Biochem 76, 611-621.
    • (1974) J Biochem , vol.76 , pp. 611-621
    • Yamakura, F.1    Ikeda, Y.2    Kimura, K.3    Sasakawa, T.4
  • 25
    • 0002998214 scopus 로고
    • Coordinated end-product inhibition in lysine synthesis in Escherichia coli
    • Yugari, Y. and Gilvarg, C. (1962) Coordinated end-product inhibition in lysine synthesis in Escherichia coli. Biochim Biophys Acta 62, 610-612.
    • (1962) Biochim Biophys Acta , vol.62 , pp. 610-612
    • Yugari, Y.1    Gilvarg, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.