메뉴 건너뛰기




Volumn 121, Issue 2, 2016, Pages 172-177

Effects of phosphoenolpyruvate carboxylase desensitization on glutamic acid production in Corynebacterium glutamicum ATCC 13032

Author keywords

Anaplerotic pathway; Aspartic acid; Corynebacterium glutamicum; Feed back inhibition; Glutamic acid; Phosphoenolpyruvate carboxylase; Pyruvate kinase

Indexed keywords

FEEDBACK; GENES;

EID: 84953364145     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2015.06.008     Document Type: Article
Times cited : (22)

References (19)
  • 1
    • 84991906038 scopus 로고    scopus 로고
    • L-Glutamate production, pp. 439-463
    • CRC Press, Boca Raton, L. Eggeling, M. Bott (Eds.)
    • Kimura E. L-Glutamate production, pp. 439-463. Handbook of Corynebacterium glutamicum 2005, CRC Press, Boca Raton. L. Eggeling, M. Bott (Eds.).
    • (2005) Handbook of Corynebacterium glutamicum
    • Kimura, E.1
  • 4
    • 0033205652 scopus 로고    scopus 로고
    • Importance of phosphoenolpyruvate carboxylase of Corynebacterium glutamicum during the temperature triggered glutamic acid fermentation
    • Delaunay S., Uy D., Baucher M.F., Engasser J.M., Guyonvarch A., Goergen J.L. Importance of phosphoenolpyruvate carboxylase of Corynebacterium glutamicum during the temperature triggered glutamic acid fermentation. Metab. Eng. 1999, 1:334-343.
    • (1999) Metab. Eng. , vol.1 , pp. 334-343
    • Delaunay, S.1    Uy, D.2    Baucher, M.F.3    Engasser, J.M.4    Guyonvarch, A.5    Goergen, J.L.6
  • 5
    • 48449096521 scopus 로고    scopus 로고
    • Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum
    • Sato H., Orishimo K., Shirai T., Hirasawa T., Nagahisa K., Shimizu H., Wachi M. Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum. J. Biosci. Bioeng. 2008, 106:51-58.
    • (2008) J. Biosci. Bioeng. , vol.106 , pp. 51-58
    • Sato, H.1    Orishimo, K.2    Shirai, T.3    Hirasawa, T.4    Nagahisa, K.5    Shimizu, H.6    Wachi, M.7
  • 6
    • 39449104902 scopus 로고    scopus 로고
    • Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum
    • Hasegawa T., Hashimoto K., Kawasaki H., Nakamatsu T. Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum. J. Biosci. Bioeng. 2008, 105:12-19.
    • (2008) J. Biosci. Bioeng. , vol.105 , pp. 12-19
    • Hasegawa, T.1    Hashimoto, K.2    Kawasaki, H.3    Nakamatsu, T.4
  • 7
    • 34447620670 scopus 로고    scopus 로고
    • Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis
    • Shirai T., Fujimura K., Furusawa C., Nagahisa K., Shioya S., Shimizu H. Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolic flux analysis. Microb. Cell Fact. 2007, 6:19.
    • (2007) Microb. Cell Fact. , vol.6 , pp. 19
    • Shirai, T.1    Fujimura, K.2    Furusawa, C.3    Nagahisa, K.4    Shioya, S.5    Shimizu, H.6
  • 9
    • 0028329083 scopus 로고
    • Effects of phosphoenol pyruvate carboxylase deficiency on metabolism and lysine production in Corynebacterium glutamicum
    • Gubler M., Park S.M., Jetten M., Stephanopoulos G., Sinskey A.J. Effects of phosphoenol pyruvate carboxylase deficiency on metabolism and lysine production in Corynebacterium glutamicum. Appl. Microbiol. Biotechnol. 1994, 40:857-863.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 857-863
    • Gubler, M.1    Park, S.M.2    Jetten, M.3    Stephanopoulos, G.4    Sinskey, A.J.5
  • 10
    • 0021939874 scopus 로고
    • Purification and some properties of phosphoenolpyruvate carboxylase from Brevibacterium flavum and its aspartate-overproducing mutant
    • Mori M., Shiio I. Purification and some properties of phosphoenolpyruvate carboxylase from Brevibacterium flavum and its aspartate-overproducing mutant. J. Biochem. 1985, 97:1119-1128.
    • (1985) J. Biochem. , vol.97 , pp. 1119-1128
    • Mori, M.1    Shiio, I.2
  • 11
    • 0022399869 scopus 로고
    • Synergistic inhibition of phosphoenolpyruvate carboxylase by aspartate and 2-oxoglutarate in Brevibacterium flavum
    • Mori M., Shiio I. Synergistic inhibition of phosphoenolpyruvate carboxylase by aspartate and 2-oxoglutarate in Brevibacterium flavum. J. Biochem. 1985, 98:1621-1630.
    • (1985) J. Biochem. , vol.98 , pp. 1621-1630
    • Mori, M.1    Shiio, I.2
  • 12
    • 84954958956 scopus 로고
    • Production of aspartic acid and enzymatic alteration in pyruvate kinase mutants of Brevibacterium flavum
    • Mori M., Shiio I. Production of aspartic acid and enzymatic alteration in pyruvate kinase mutants of Brevibacterium flavum. Agric. Biol. Chem. 1984, 48:1189-1197.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1189-1197
    • Mori, M.1    Shiio, I.2
  • 13
    • 84893405383 scopus 로고    scopus 로고
    • Deregulation of feedback inhibition of phosphoenolpyruvate carboxylase for improved lysine production in Corynebacterium glutamicum
    • Chen Z., Bommareddy R.R., Frank D., Rappert S., Zeng A.-P. Deregulation of feedback inhibition of phosphoenolpyruvate carboxylase for improved lysine production in Corynebacterium glutamicum. Appl. Environ. Microbiol. 2014, 80:1388-1393.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 1388-1393
    • Chen, Z.1    Bommareddy, R.R.2    Frank, D.3    Rappert, S.4    Zeng, A.-P.5
  • 14
    • 77953025992 scopus 로고    scopus 로고
    • Metabolic changes in a pyruvate kinase gene deletion mutant of Corynebacterium glutamicum ATCC 13032
    • Sawada K., Zen-in S., Wada M., Yokota A. Metabolic changes in a pyruvate kinase gene deletion mutant of Corynebacterium glutamicum ATCC 13032. Metab. Eng. 2010, 12:401-407.
    • (2010) Metab. Eng. , vol.12 , pp. 401-407
    • Sawada, K.1    Zen-in, S.2    Wada, M.3    Yokota, A.4
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 18
    • 0026571809 scopus 로고
    • Application of an allele-specific polymerase chain reaction to the direct determination of ABO blood group genotypes
    • Ugozzoli L., Wallace R.B. Application of an allele-specific polymerase chain reaction to the direct determination of ABO blood group genotypes. Genomics 1992, 12:670-674.
    • (1992) Genomics , vol.12 , pp. 670-674
    • Ugozzoli, L.1    Wallace, R.B.2
  • 19
    • 0024512267 scopus 로고
    • Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC13032
    • O'Regan M., Thierbach G., Bachmann B., Villeval D., Lepage P., Viret J.-F., Lemoine Y. Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC13032. Gene 1989, 77:237-251.
    • (1989) Gene , vol.77 , pp. 237-251
    • O'Regan, M.1    Thierbach, G.2    Bachmann, B.3    Villeval, D.4    Lepage, P.5    Viret, J.-F.6    Lemoine, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.