메뉴 건너뛰기




Volumn 179, Issue 5, 2010, Pages 527-535

Cloning, expression, purification and physical and kinetic characterization of the phosphoenolpyruvate carboxylase from orange (Citrus sinensis osbeck var. Valencia) fruit juice sacs

Author keywords

Carbon metabolism; Citrus sinensis; Orange fruit; Phosphoenolpyruvate carboxylase

Indexed keywords

CITRUS SINENSIS; MAMMALIA;

EID: 77956759892     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2010.08.003     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0038122942 scopus 로고
    • Higher plant phosphoenolpyruvate carboxylase. Structure and regulation
    • Andreo C.S., González D.H., Iglesias A.A. Higher plant phosphoenolpyruvate carboxylase. Structure and regulation. FEBS Lett. 1987, 213:1-8.
    • (1987) FEBS Lett. , vol.213 , pp. 1-8
    • Andreo, C.S.1    González, D.H.2    Iglesias, A.A.3
  • 2
    • 3242719687 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: a new era of structural biology
    • Izui K., Matsumura H., Furumoto T., Kai Y. Phosphoenolpyruvate carboxylase: a new era of structural biology. Annu. Rev. Plant Biol. 2004, 55:69-84.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 69-84
    • Izui, K.1    Matsumura, H.2    Furumoto, T.3    Kai, Y.4
  • 3
    • 0037763823 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms
    • Kai Y., Matsumura H., Izui K. Phosphoenolpyruvate carboxylase: three-dimensional structure and molecular mechanisms. Arch. Biochem. Biophys. 2003, 414:170-179.
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 170-179
    • Kai, Y.1    Matsumura, H.2    Izui, K.3
  • 4
    • 33645536135 scopus 로고    scopus 로고
    • The functional organization and control of plant respiration
    • Plaxton W.C., Podestá F.E. The functional organization and control of plant respiration. Crit. Rev. Plant Sci. 2006, 25:159-198.
    • (2006) Crit. Rev. Plant Sci. , vol.25 , pp. 159-198
    • Plaxton, W.C.1    Podestá, F.E.2
  • 5
  • 8
    • 0032055053 scopus 로고    scopus 로고
    • Purification and characterization of high- and low-molecular-mass isoforms of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtii. Kinetic, structural and immunological evidence that the green algal enzyme is distinct from the prokaryotic and higher plant enzymes
    • Rivoal J., Plaxton W.C., Turpin D.H. Purification and characterization of high- and low-molecular-mass isoforms of phosphoenolpyruvate carboxylase from Chlamydomonas reinhardtii. Kinetic, structural and immunological evidence that the green algal enzyme is distinct from the prokaryotic and higher plant enzymes. Biochem. J. 1998, 331:201-209.
    • (1998) Biochem. J. , vol.331 , pp. 201-209
    • Rivoal, J.1    Plaxton, W.C.2    Turpin, D.H.3
  • 9
    • 0030220313 scopus 로고    scopus 로고
    • Purification and properties of four phosphoenolpyruvate carboxylase isoforms from the green alga Selenastrum minutum: evidence that association of the 102-kDa catalytic subunit with unrelated polypeptides may modify the physical and kinetic properties of the enzyme
    • Rivoal J., Dunford R., Plaxton W.C., Turpin D.H. Purification and properties of four phosphoenolpyruvate carboxylase isoforms from the green alga Selenastrum minutum: evidence that association of the 102-kDa catalytic subunit with unrelated polypeptides may modify the physical and kinetic properties of the enzyme. Arch. Biochem. Biophys. 1996, 332:47-57.
    • (1996) Arch. Biochem. Biophys. , vol.332 , pp. 47-57
    • Rivoal, J.1    Dunford, R.2    Plaxton, W.C.3    Turpin, D.H.4
  • 10
    • 0038485638 scopus 로고    scopus 로고
    • Structural and kinetic properties of high and low molecular mass phosphoenolpyruvate carboxylase isoforms from the endosperm of developing castor oilseeds
    • Blonde J.D., Plaxton W.C. Structural and kinetic properties of high and low molecular mass phosphoenolpyruvate carboxylase isoforms from the endosperm of developing castor oilseeds. J. Biol. Chem. 2003, 278:11867-11873.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11867-11873
    • Blonde, J.D.1    Plaxton, W.C.2
  • 11
    • 28544435430 scopus 로고    scopus 로고
    • In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase Isoforms in endosperm of developing castor oil seeds
    • Trípodi K.E.J., Turner W.L., Gennidakis S., Plaxton W.C. In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase Isoforms in endosperm of developing castor oil seeds. Plant Physiol. 2005, 139:969-978.
    • (2005) Plant Physiol. , vol.139 , pp. 969-978
    • Trípodi, K.E.J.1    Turner, W.L.2    Gennidakis, S.3    Plaxton, W.C.4
  • 12
    • 36348985146 scopus 로고    scopus 로고
    • Bacterial- and plant-type phosphoenolpyruvate carboxylase polypeptides interact in the hetero-oligomeric Class-2 PEPC complex of developing castor oil seeds
    • Gennidakis S., Rao S.K., Greenham K., Uhrig R.G., O'Leary B., Snedden W.A., Lu C., Plaxton W.C. Bacterial- and plant-type phosphoenolpyruvate carboxylase polypeptides interact in the hetero-oligomeric Class-2 PEPC complex of developing castor oil seeds. Plant J. 2007, 52:839-849.
    • (2007) Plant J. , vol.52 , pp. 839-849
    • Gennidakis, S.1    Rao, S.K.2    Greenham, K.3    Uhrig, R.G.4    O'Leary, B.5    Snedden, W.A.6    Lu, C.7    Plaxton, W.C.8
  • 15
    • 33845664519 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy-based metabolite profiling of transgenic tomato fruit engineered to accumulate spermidine and spermine reveals enhanced anabolic and nitrogen-carbon interactions
    • Mattoo A.K., Sobolev A.P., Neelam A., Goyal R.K., Handa A.K., Segre A.L. Nuclear magnetic resonance spectroscopy-based metabolite profiling of transgenic tomato fruit engineered to accumulate spermidine and spermine reveals enhanced anabolic and nitrogen-carbon interactions. Plant Physiol. 2006, 142:1759-1770.
    • (2006) Plant Physiol. , vol.142 , pp. 1759-1770
    • Mattoo, A.K.1    Sobolev, A.P.2    Neelam, A.3    Goyal, R.K.4    Handa, A.K.5    Segre, A.L.6
  • 17
    • 0001495653 scopus 로고
    • Phosphoenolpyruvate carboxylase in avocado fruit: purification and properties
    • Notton B.A., Blanke M.M. Phosphoenolpyruvate carboxylase in avocado fruit: purification and properties. Phytochemistry 1993, 33:1333-1337.
    • (1993) Phytochemistry , vol.33 , pp. 1333-1337
    • Notton, B.A.1    Blanke, M.M.2
  • 18
    • 0029029080 scopus 로고
    • Purification and characterization of a novel phosphoenolpyruvate carboxylase from banana fruit
    • Law R.D., Plaxton W.C. Purification and characterization of a novel phosphoenolpyruvate carboxylase from banana fruit. Biochem. J. 1995, 307:807-816.
    • (1995) Biochem. J. , vol.307 , pp. 807-816
    • Law, R.D.1    Plaxton, W.C.2
  • 20
    • 0017808011 scopus 로고
    • Messenger RNA for G1 protein of French bean seeds: cell-free translation and product characterization
    • Hall T.C, Ma Y., Buchbinder B.U., Pyne J.W., Sun S.M., Bliss F.A. Messenger RNA for G1 protein of French bean seeds: cell-free translation and product characterization. Proc. Natl. Acad. Sci. U.S.A. 1978, 75:3196-3200.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3196-3200
    • Hall, T.C.1    Ma, Y.2    Buchbinder, B.U.3    Pyne, J.W.4    Sun, S.M.5    Bliss, F.A.6
  • 21
    • 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. Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation. J. Biol. Chem. 2005, 280:11798-11806.
    • (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
  • 22
    • 0031423783 scopus 로고    scopus 로고
    • Carbon metabolism in germinating Ricinus communis cotyledons. Purification, characterization and developmental profile of NADP-dependent malic enzyme
    • Colombo S.L., Andreo C.S., Podestá F.E. Carbon metabolism in germinating Ricinus communis cotyledons. Purification, characterization and developmental profile of NADP-dependent malic enzyme. Physiol. Plant. 1997, 101:821-826.
    • (1997) Physiol. Plant. , vol.101 , pp. 821-826
    • Colombo, S.L.1    Andreo, C.S.2    Podestá, F.E.3
  • 24
    • 0027092553 scopus 로고
    • A simple computer program with statistical tests for analysis of enzyme kinetics
    • Brooks S.P.J. A simple computer program with statistical tests for analysis of enzyme kinetics. Biotechniques 1992, 13:906-911.
    • (1992) Biotechniques , vol.13 , pp. 906-911
    • Brooks, S.P.J.1
  • 26
    • 0024669157 scopus 로고
    • Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor-oil-plant endosperm and leaf
    • Plaxton W.C. Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor-oil-plant endosperm and leaf. Eur. J. Biochem. 1989, 181:443-451.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 443-451
    • Plaxton, W.C.1
  • 27
    • 33745218323 scopus 로고    scopus 로고
    • The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall Catalysis
    • Xu W., Ahmed S., Moriyama H., Chollet R. The importance of the strictly conserved, C-terminal glycine residue in phosphoenolpyruvate carboxylase for overall Catalysis. J. Biol. Chem. 2006, 281:17238-17245.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17238-17245
    • Xu, W.1    Ahmed, S.2    Moriyama, H.3    Chollet, R.4
  • 28
    • 44649128674 scopus 로고    scopus 로고
    • 3 plants: mutations for diminished sensitivity to feedback inhibitors and for increased substrate affinity
    • 3 plants: mutations for diminished sensitivity to feedback inhibitors and for increased substrate affinity. J. Exp. Bot. 2008, 59:1811-1818.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1811-1818
    • Endo, T.1    Mihara, Y.2    Furumoto, T.3    Matsumura, H.4    Kai, Y.5    Izui, K.6
  • 30
    • 28544435430 scopus 로고    scopus 로고
    • In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase Isoforms in endosperm of developing castor oil seeds
    • Trípodi K.E.J., Plaxton W.C. In vivo regulatory phosphorylation of novel phosphoenolpyruvate carboxylase Isoforms in endosperm of developing castor oil seeds. Plant Physiol. 2005, 139:969-978.
    • (2005) Plant Physiol. , vol.139 , pp. 969-978
    • Trípodi, K.E.J.1    Plaxton, W.C.2
  • 31
    • 0031882683 scopus 로고    scopus 로고
    • Expression of a soybean nodule-enhanced phosphoenolpyruvate carboxylase gene that shows striking similarity to another gene for a house-keeping isoform
    • Hata S., Izui K., Kouchi H. Expression of a soybean nodule-enhanced phosphoenolpyruvate carboxylase gene that shows striking similarity to another gene for a house-keeping isoform. Plant J. 1998, 13:267-273.
    • (1998) Plant J. , vol.13 , pp. 267-273
    • Hata, S.1    Izui, K.2    Kouchi, H.3
  • 32
    • 0001808607 scopus 로고
    • Carbohydrate and enzyme distribution in protoplasts from valencia orange juice sacs
    • Echeverria E., Valich J. Carbohydrate and enzyme distribution in protoplasts from valencia orange juice sacs. Phytochemistry 1988, 27:73-76.
    • (1988) Phytochemistry , vol.27 , pp. 73-76
    • Echeverria, E.1    Valich, J.2
  • 35
    • 0002255208 scopus 로고
    • Physical properties of phosphoenolpyruvate carboxylase and malic enzyme in grape berries
    • Lakso A.N., Kliewer W.M. Physical properties of phosphoenolpyruvate carboxylase and malic enzyme in grape berries. Am. J. Enol. Viticult. 1975, 26:75-78.
    • (1975) Am. J. Enol. Viticult. , vol.26 , pp. 75-78
    • Lakso, A.N.1    Kliewer, W.M.2
  • 36
    • 0030752239 scopus 로고    scopus 로고
    • Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase
    • Law R.D., Plaxton W.C. Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase. Eur. J. Biochem. 1997, 247:642-651.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 642-651
    • Law, R.D.1    Plaxton, W.C.2
  • 37
    • 0001730789 scopus 로고
    • Maize leaf phosphoenolpyruvate carboxylase: oligomeric state and activity in the presence of glycerol
    • Podestá F.E., Andreo C.S. Maize leaf phosphoenolpyruvate carboxylase: oligomeric state and activity in the presence of glycerol. Plant Physiol. 1989, 90:427-433.
    • (1989) Plant Physiol. , vol.90 , pp. 427-433
    • Podestá, F.E.1    Andreo, C.S.2
  • 38
    • 0027974775 scopus 로고
    • Regulation of carbon metabolism in germinating Ricinus communis cotyledons. II. Properties of phosphoenolpyruvate carboxylase and cytosolic pyruvate kinase associated with the regulation of glycolysis and nitrogen assimilation
    • Podestá F.E., Plaxton W.C. Regulation of carbon metabolism in germinating Ricinus communis cotyledons. II. Properties of phosphoenolpyruvate carboxylase and cytosolic pyruvate kinase associated with the regulation of glycolysis and nitrogen assimilation. Planta 1994, 194:406-417.
    • (1994) Planta , vol.194 , pp. 406-417
    • Podestá, F.E.1    Plaxton, W.C.2
  • 39
    • 0033942050 scopus 로고    scopus 로고
    • Purification and characterization of phosphoenolpyruvate carboxylase from Brassica napus (rapeseed) suspension cell cultures: implications for phosphoenolpyruvate carboxylase regulation during phosphate starvation, and the integration of glycolysis with nitrogen assimilation
    • Moraes T.F., Plaxton W.C. Purification and characterization of phosphoenolpyruvate carboxylase from Brassica napus (rapeseed) suspension cell cultures: implications for phosphoenolpyruvate carboxylase regulation during phosphate starvation, and the integration of glycolysis with nitrogen assimilation. Eur. J. Biochem. 2000, 267:4465-4476.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4465-4476
    • Moraes, T.F.1    Plaxton, W.C.2
  • 40
    • 34548018541 scopus 로고    scopus 로고
    • The citrus fruit proteome: insights into citrus fruit metabolism
    • Katz E., Fon M., Lee Y., Phinney B., Sadka A., Blumwald E. The citrus fruit proteome: insights into citrus fruit metabolism. Planta 2007, 226:989-1005.
    • (2007) Planta , vol.226 , pp. 989-1005
    • Katz, E.1    Fon, M.2    Lee, Y.3    Phinney, B.4    Sadka, A.5    Blumwald, E.6
  • 41
    • 0004797546 scopus 로고
    • Pyruvate metabolism during maturation of hamlin oranges
    • Roe B., Davis P.L., Bruemmer J.H. Pyruvate metabolism during maturation of hamlin oranges. Phytochemistry 1984, 23:713-717.
    • (1984) Phytochemistry , vol.23 , pp. 713-717
    • Roe, B.1    Davis, P.L.2    Bruemmer, J.H.3
  • 42
    • 0344002713 scopus 로고    scopus 로고
    • Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase
    • Tovar-Méndez A., Mujica-Jiménez C., Muñoz-Clares R.A. Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. Plant Physiol. 2000, 123:149-160.
    • (2000) Plant Physiol. , vol.123 , pp. 149-160
    • Tovar-Méndez, A.1    Mujica-Jiménez, C.2    Muñoz-Clares, R.A.3
  • 43
    • 0025322611 scopus 로고
    • The role of oligomerization in regulation of maize phosphoenolpyruvate carboxylase activity: influence of Mg-PEP and malate on the oligomeric equilibrium of PEP carboxylase
    • Willeford K.O., Wu M.-X., Meyer C.R., Wedding R.T. The role of oligomerization in regulation of maize phosphoenolpyruvate carboxylase activity: influence of Mg-PEP and malate on the oligomeric equilibrium of PEP carboxylase. Biochem. Biophys. Res. Commun. 1990, 168:778-785.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 778-785
    • Willeford, K.O.1    Wu, M.-X.2    Meyer, C.R.3    Wedding, R.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.