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Volumn 59, Issue 7, 2008, Pages 1811-1818

Maize C4-form phosphoenolpyruvate carboxylase engineered to be functional in C3 plants: Mutations for diminished sensitivity to feedback inhibitors and for increased substrate affinity

Author keywords

C4 photosynthesis; Genetic engineering; PEP carboxylase; Site directed mutagenesis; Zea mays

Indexed keywords

ESCHERICHIA COLI; ZEA MAYS;

EID: 44649128674     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/ern018     Document Type: Conference Paper
Times cited : (20)

References (37)
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 3543103283 scopus 로고    scopus 로고
    • Overexpression of a cyanobacterial phosphoenolpyruvate carboxylase with diminished sensitivity to feedback inhibition in Arabidopsis changes amino acid metabolism
    • Chen LM, Li KZ, Miwa T, Izui K. 2004. Overexpression of a cyanobacterial phosphoenolpyruvate carboxylase with diminished sensitivity to feedback inhibition in Arabidopsis changes amino acid metabolism. Planta 219, 440-449.
    • (2004) Planta , vol.219 , pp. 440-449
    • Chen, L.M.1    Li, K.Z.2    Miwa, T.3    Izui, K.4
  • 5
    • 0031105045 scopus 로고    scopus 로고
    • 4-type phosphoenolpyruvate carboxylase in Escherichia coli and its rapid purification
    • 4-type phosphoenolpyruvate carboxylase in Escherichia coli and its rapid purification. Bioscience, Biotechnology and Biochemistry 61, 545-546.
    • (1997) Bioscience, Biotechnology and Biochemistry , vol.61 , pp. 545-546
    • Dong, L.1    Hata, S.2    Izui, K.3
  • 8
    • 0031397428 scopus 로고    scopus 로고
    • Evidence that a malate/inorganic phosphate exchange translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm
    • Eastmond PJ, Dennis DT, Rawsthorne S. 1997. Evidence that a malate/inorganic phosphate exchange translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm. Plant Physiology 114, 851-856.
    • (1997) Plant Physiology , vol.114 , pp. 851-856
    • Eastmond, P.J.1    Dennis, D.T.2    Rawsthorne, S.3
  • 10
    • 33745678052 scopus 로고    scopus 로고
    • Characterization and functional analysis of phosphoenolpyruvate carboxylase kinase genes in rice
    • Fukayama H, Tamai T, Taniguchi Y, Sullivan S, Miyao M, Nimmo H. 2006. Characterization and functional analysis of phosphoenolpyruvate carboxylase kinase genes in rice. The Plant Journal 47, 258-268.
    • (2006) The Plant Journal , vol.47 , pp. 258-268
    • Fukayama, H.1    Tamai, T.2    Taniguchi, Y.3    Sullivan, S.4    Miyao, M.5    Nimmo, H.6
  • 11
    • 0033213556 scopus 로고    scopus 로고
    • cDNA cloning and characterization of maize phosphoenolpyruvate carboxykinase, a bundle sheath cell-specific enzyme
    • Furumoto T, Hata S, Izui K. 1999. cDNA cloning and characterization of maize phosphoenolpyruvate carboxykinase, a bundle sheath cell-specific enzyme. Plant Molecular Biology 41, 301-311.
    • (1999) Plant Molecular Biology , vol.41 , pp. 301-311
    • Furumoto, T.1    Hata, S.2    Izui, K.3
  • 14
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 18
    • 0037763823 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: Three-dimensional structure and molecular mechanisms
    • Kai Y, Matsumura H, Izui K. 2003. Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms. Archives of Biochemistry and Biophysics 414, 170-179.
    • (2003) Archives of Biochemistry and Biophysics , vol.414 , pp. 170-179
    • Kai, Y.1    Matsumura, H.2    Izui, K.3
  • 19
    • 0345495698 scopus 로고    scopus 로고
    • Characterization of two functional phosphoenolpyruvate/phosphate translocator (PPT) genes in Arabidopsis-AtPPT1 may be involved in the provision of signals for correct mesophyll development
    • Knappe S, Lottgert T, Schneider A, Voll L, Flugge UI, Fischer K. 2003. Characterization of two functional phosphoenolpyruvate/phosphate translocator (PPT) genes in Arabidopsis-AtPPT1 may be involved in the provision of signals for correct mesophyll development. The Plant Journal 36, 411-420.
    • (2003) The Plant Journal , vol.36 , pp. 411-420
    • Knappe, S.1    Lottgert, T.2    Schneider, A.3    Voll, L.4    Flugge, U.I.5    Fischer, K.6
  • 20
    • 0028042263 scopus 로고
    • Molecular and physiological evaluation of transgenic tobacco plants expressing a maize phosphoenolpyruvate carboxylase gene under the control of the cauliflower mosaic virus 35S promoter
    • Kogami H, Syono M, Koike T, Yanagisawa S, Izui K, Sentoku N, Tanifuji S, Uchimiya H, Toki S. 1994. Molecular and physiological evaluation of transgenic tobacco plants expressing a maize phosphoenolpyruvate carboxylase gene under the control of the cauliflower mosaic virus 35S promoter. Transgenic Research 3, 287-296.
    • (1994) Transgenic Research , vol.3 , pp. 287-296
    • Kogami, H.1    Syono, M.2    Koike, T.3    Yanagisawa, S.4    Izui, K.5    Sentoku, N.6    Tanifuji, S.7    Uchimiya, H.8    Toki, S.9
  • 23
    • 33746843948 scopus 로고    scopus 로고
    • Surcharging rice photosynthesis to increase yield
    • Mitchell PL, Sheehy LE. 2006. Surcharging rice photosynthesis to increase yield. New Phytologist 171, 688-693.
    • (2006) New Phytologist , vol.171 , pp. 688-693
    • Mitchell, P.L.1    Sheehy, L.E.2
  • 25
    • 0037763816 scopus 로고    scopus 로고
    • Control of the phosphorylation of phosphoenolpyruvate carboxylase in higher plants
    • Nimmo HG. 2003. Control of the phosphorylation of phosphoenolpyruvate carboxylase in higher plants. Archives of Biochemistry and Biophysics 414, 189-196.
    • (2003) Archives of Biochemistry and Biophysics , vol.414 , pp. 189-196
    • Nimmo, H.G.1
  • 26
    • 0000658761 scopus 로고
    • Phosphoenolpyruvate carboxylase: An enzymologist's view
    • O'Leary MH. 1982. Phosphoenolpyruvate carboxylase: an enzymologist's view. Annual Review of Plant Physiology 33, 297-231.
    • (1982) Annual Review of Plant Physiology , vol.33 , pp. 297-231
    • O'Leary, M.H.1
  • 29
    • 0037061420 scopus 로고    scopus 로고
    • Agricultural biotech: The rice squad
    • Surridge C. 2002. Agricultural biotech: the rice squad. Nature 416, 576-578.
    • (2002) Nature , vol.416 , pp. 576-578
    • Surridge, C.1
  • 31
    • 15744386874 scopus 로고    scopus 로고
    • Maize phosphoenolpyruvate carboxylase: Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation
    • Takahashi-Terada A, Kotera M, Ohshima K, Furumoto T, Matsumura H, Kai Y, Izui K. 2005. Maize phosphoenolpyruvate carboxylase: mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. Journal of Biological Chemistry 12, 11798-11806.
    • (2005) Journal of Biological Chemistry , vol.12 , pp. 11798-11806
    • Takahashi-Terada, A.1    Kotera, M.2    Ohshima, K.3    Furumoto, T.4    Matsumura, H.5    Kai, Y.6    Izui, K.7
  • 32
    • 0029284996 scopus 로고
    • Construction of a plasmid for high level expression of Escherichia coli phosphoenolpyruvate carboxylase
    • Terada K, Fujita N, Katsuki H, Izui K. 1995. Construction of a plasmid for high level expression of Escherichia coli phosphoenolpyruvate carboxylase. Bioscience, Biotechnology and Biochemistry 59, 735-737.
    • (1995) Bioscience, Biotechnology and Biochemistry , vol.59 , pp. 735-737
    • Terada, K.1    Fujita, N.2    Katsuki, H.3    Izui, K.4
  • 33
    • 0026343112 scopus 로고
    • Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase: His 138 is essential for the second partial reaction
    • Terada K, Izui K. 1991. Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase: His 138 is essential for the second partial reaction. European Journal of Biochemistry 202, 797-803.
    • (1991) European Journal of Biochemistry , vol.202 , pp. 797-803
    • Terada, K.1    Izui, K.2
  • 37
    • 0028999716 scopus 로고
    • Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase
    • Yano M, Terada K, Umiji K, Izui K. 1995. Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase. Journal of Biochemistry 11, 1196-1200.
    • (1995) Journal of Biochemistry , vol.11 , pp. 1196-1200
    • Yano, M.1    Terada, K.2    Umiji, K.3    Izui, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.