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Volumn 174, Issue 4, 2008, Pages 475-483

Kinetic analyses of recombinant isoforms of phosphoenolpyruvate carboxylase from Hydrilla verticillata leaves and the impact of substituting a C4-signature serine

Author keywords

Aquatic monocot; C3, C4 photosynthesis; Kinetic analyses; Phosphoenolpyruvate carboxylase (PEPC); Recombinant protein; Site directed mutagenesis

Indexed keywords

HYDRILLA VERTICILLATA;

EID: 39749100481     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2008.01.010     Document Type: Article
Times cited : (15)

References (38)
  • 1
    • 0027549404 scopus 로고
    • Sorghum phosphoenolpyruvate carboxylase gene family: structure, function and molecular evolution
    • Lepiniec L., Keryer E., Philippe H., Gadal P., and Cretin C. Sorghum phosphoenolpyruvate carboxylase gene family: structure, function and molecular evolution. Plant Mol. Biol. 21 (1993) 487-502
    • (1993) Plant Mol. Biol. , vol.21 , pp. 487-502
    • Lepiniec, L.1    Keryer, E.2    Philippe, H.3    Gadal, P.4    Cretin, C.5
  • 2
    • 0028121329 scopus 로고
    • Phosphoenolpyruvate carboxylase: structure, regulation and evolution
    • Lepiniec L., Vidal J., Chollet R., Gadal P., and Cretin C. Phosphoenolpyruvate carboxylase: structure, regulation and evolution. Plant Sci. 99 (1994) 111-124
    • (1994) Plant Sci. , vol.99 , pp. 111-124
    • Lepiniec, L.1    Vidal, J.2    Chollet, R.3    Gadal, P.4    Cretin, C.5
  • 3
    • 0000756509 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: a ubiquitous highly regulated enzyme in plants.
    • Chollet R., Vidal J., and O'Leary M.H. Phosphoenolpyruvate carboxylase: a ubiquitous highly regulated enzyme in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47 (1996) 273-298
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 273-298
    • Chollet, R.1    Vidal, J.2    O'Leary, M.H.3
  • 4
    • 0031171689 scopus 로고    scopus 로고
    • 3): molecular characterization and expression analysis of the ppcB and ppcC genes
    • 3): molecular characterization and expression analysis of the ppcB and ppcC genes. Plant Mol. Biol. 34 (1997) 427-443
    • (1997) Plant Mol. Biol. , vol.34 , pp. 427-443
    • Ernst, K.1    Westhoff, P.2
  • 6
    • 0000158343 scopus 로고
    • Two photosynthetic mechanisms mediating the low photorespiratory state in submersed aquatic angiosperms
    • Salvucci M.E., and Bowes G. Two photosynthetic mechanisms mediating the low photorespiratory state in submersed aquatic angiosperms. Plant Physiol. 73 (1983) 488-496
    • (1983) Plant Physiol. , vol.73 , pp. 488-496
    • Salvucci, M.E.1    Bowes, G.2
  • 8
    • 0033845345 scopus 로고    scopus 로고
    • 2 fixation in Egeria densa, a submersed aquatic species
    • 2 fixation in Egeria densa, a submersed aquatic species. Plant Physiol. 123 (2000) 1611-1621
    • (2000) Plant Physiol. , vol.123 , pp. 1611-1621
    • Casati, P.1    Lara, M.V.2    Andreo, C.S.3
  • 11
    • 45149145135 scopus 로고
    • Plasticity in the photosynthetic carbon metabolism of submersed aquatic macrophytes
    • Bowes G., and Salvucci M.E. Plasticity in the photosynthetic carbon metabolism of submersed aquatic macrophytes. Aquat. Bot. 34 (1989) 233-266
    • (1989) Aquat. Bot. , vol.34 , pp. 233-266
    • Bowes, G.1    Salvucci, M.E.2
  • 14
    • 84878939580 scopus 로고    scopus 로고
    • Light regulation of the photosynthetic phosphoenolpyruvate carboxylase (PEPC) in Hydrilla verticillata
    • Rao S.K., Reiskind J.B., and Bowes G. Light regulation of the photosynthetic phosphoenolpyruvate carboxylase (PEPC) in Hydrilla verticillata. Plant Cell Physiol. 47 (2006) 1206-1216
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1206-1216
    • Rao, S.K.1    Reiskind, J.B.2    Bowes, G.3
  • 24
    • 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. Biosci. Biotech. Biochem. 61 (1997) 545-546
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 545-546
    • Dong, L.-Y.1    Hata, S.2    Izui, K.3
  • 25
    • 0001432678 scopus 로고
    • Light activation of maize phosphoenolpyruvate carboxylase protein-serine kinase activity is inhibited by mesophyll and bundle sheath-directed photosynthesis inhibitors
    • Jiao J.A., and Chollet R. Light activation of maize phosphoenolpyruvate carboxylase protein-serine kinase activity is inhibited by mesophyll and bundle sheath-directed photosynthesis inhibitors. Plant Physiol. 98 (1992) 152-156
    • (1992) Plant Physiol. , vol.98 , pp. 152-156
    • Jiao, J.A.1    Chollet, R.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of dye-binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of dye-binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 3242719687 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: a new era of structural biology
    • Izui K., Matsumura H., Furumoto T., and Kai Y. Phosphoenolpyruvate carboxylase: a new era of structural biology. Ann. Rev. Plant Biol. 55 (2004) 69-84
    • (2004) Ann. Rev. Plant Biol. , vol.55 , pp. 69-84
    • Izui, K.1    Matsumura, H.2    Furumoto, T.3    Kai, Y.4
  • 34
    • 0344002713 scopus 로고    scopus 로고
    • Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase
    • Tovar-Mendez A., Mujica-Jimenez C., and Munoz-Clares R.A. Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. Plant Physiol. 123 (2000) 149-160
    • (2000) Plant Physiol. , vol.123 , pp. 149-160
    • Tovar-Mendez, A.1    Mujica-Jimenez, C.2    Munoz-Clares, R.A.3
  • 35
    • 0037763823 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms
    • Kai Y., Matsumura H., and Izui K. Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms. Arch. Biochem. Biophys. 414 (2003) 170-179
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 170-179
    • Kai, Y.1    Matsumura, H.2    Izui, K.3
  • 36
    • 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., and Izui K. Maize phosphoenolpyruvate carboxylase: mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. J. Biol. Chem. 280 (2005) 11798-11806
    • (2005) J. Biol. Chem. , vol.280 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.