메뉴 건너뛰기




Volumn 19, Issue PB, 2014, Pages 184-190

Activity of the mitochondrial pyruvate dehydrogenase complex in plants is stimulated in the presence of malate

Author keywords

Glycine; Malate dehydrogenase; Photorespiration; Plant mitochondria; Pyruvate dehydrogenase complex

Indexed keywords

GLYCINE; MALIC ACID; MALIC ACID DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PYRUVATE DEHYDROGENASE COMPLEX;

EID: 84914163912     PISSN: 15677249     EISSN: 18728278     Source Type: Journal    
DOI: 10.1016/j.mito.2014.04.006     Document Type: Article
Times cited : (26)

References (59)
  • 1
    • 0032561470 scopus 로고    scopus 로고
    • A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L
    • Berkemeyer M., Scheibe R., Ocheretina O. A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L. J. Biol. Chem. 1998, 273:27927-27933.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27927-27933
    • Berkemeyer, M.1    Scheibe, R.2    Ocheretina, O.3
  • 2
    • 0024098058 scopus 로고
    • Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase
    • Bourguignon J., Neuburger M., Douce R. Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase. Biochem. J. 1988, 255:169-178.
    • (1988) Biochem. J. , vol.255 , pp. 169-178
    • Bourguignon, J.1    Neuburger, M.2    Douce, R.3
  • 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 M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 4
    • 0025139727 scopus 로고
    • Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner
    • Budde R.J., Randall D.D. Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 1990, 87:673-676.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 673-676
    • Budde, R.J.1    Randall, D.D.2
  • 5
    • 0000361321 scopus 로고
    • Regulation of the phosphorylation of mitochondrial pyruvate dehydrogenase complex in situ: effects of respiratory substrates and calcium
    • Budde R.J., Fang T.K., Randall D.D. Regulation of the phosphorylation of mitochondrial pyruvate dehydrogenase complex in situ: effects of respiratory substrates and calcium. Plant Physiol. 1988, 88:1031-1036.
    • (1988) Plant Physiol. , vol.88 , pp. 1031-1036
    • Budde, R.J.1    Fang, T.K.2    Randall, D.D.3
  • 6
    • 0001186926 scopus 로고
    • Acetyl-coenzyme a can regulate activity of the mitochondrial pyruvate dehydrogenase complex in situ
    • Budde R.J., Fang T.K., Randall D.D., Miernyk J.A. Acetyl-coenzyme a can regulate activity of the mitochondrial pyruvate dehydrogenase complex in situ. Plant Physiol. 1991, 95:131-136.
    • (1991) Plant Physiol. , vol.95 , pp. 131-136
    • Budde, R.J.1    Fang, T.K.2    Randall, D.D.3    Miernyk, J.A.4
  • 7
    • 84914106488 scopus 로고    scopus 로고
    • The function of glycine decarboxylase complex is optimized to maintain high photorespiratory flux via buffering of its reaction products
    • Bykova N.V., Møller I.M., Gardeström P., Igamberdiev A.U. The function of glycine decarboxylase complex is optimized to maintain high photorespiratory flux via buffering of its reaction products. Mitochondrion 2014, 10.1016/j.mito.2014.01.001.
    • (2014) Mitochondrion
    • Bykova, N.V.1    Møller, I.M.2    Gardeström, P.3    Igamberdiev, A.U.4
  • 8
    • 0001028416 scopus 로고
    • Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex: a source of acetyl-CoA and NADH for fatty acid biosynthesis
    • Camp P.J., Randall D.D. Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex: a source of acetyl-CoA and NADH for fatty acid biosynthesis. Plant Physiol. 1985, 77:571-577.
    • (1985) Plant Physiol. , vol.77 , pp. 571-577
    • Camp, P.J.1    Randall, D.D.2
  • 9
    • 0024578338 scopus 로고
    • Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector
    • Cárdenas M.L., Cornish-Bowden A. Characteristics necessary for an interconvertible enzyme cascade to generate a highly sensitive response to an effector. Biochem. J. 1989, 257:339-345.
    • (1989) Biochem. J. , vol.257 , pp. 339-345
    • Cárdenas, M.L.1    Cornish-Bowden, A.2
  • 10
    • 0022470755 scopus 로고
    • Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides
    • Cornish-Bowden A. Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides. FEBS Lett. 1986, 203:3-6.
    • (1986) FEBS Lett. , vol.203 , pp. 3-6
    • Cornish-Bowden, A.1
  • 11
    • 0034075517 scopus 로고    scopus 로고
    • +-dependent malate dehydrogenase from leaves of pineapple (Ananas comosus)
    • +-dependent malate dehydrogenase from leaves of pineapple (Ananas comosus). Physiol. Plant. 2000, 108:240-248.
    • (2000) Physiol. Plant. , vol.108 , pp. 240-248
    • Cuevas, I.C.1    Podestá, F.E.2
  • 13
    • 0034652327 scopus 로고    scopus 로고
    • Regulation in metabolic systems under homeostatic flux control
    • Fridlyand L.E., Scheibe R. Regulation in metabolic systems under homeostatic flux control. Arch. Biochem. Biophys. 2000, 374:198-206.
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 198-206
    • Fridlyand, L.E.1    Scheibe, R.2
  • 14
    • 0001235725 scopus 로고
    • Light regulation of leaf mitochondrial pyruvate dehydrogenase complex: role of photorespiratory carbon metabolism
    • Gemel J., Randall D.D. Light regulation of leaf mitochondrial pyruvate dehydrogenase complex: role of photorespiratory carbon metabolism. Plant Physiol. 1992, 100:908-914.
    • (1992) Plant Physiol. , vol.100 , pp. 908-914
    • Gemel, J.1    Randall, D.D.2
  • 16
    • 0029346907 scopus 로고
    • Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis
    • Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J. Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis. Plant Physiol. 1995, 108:1623-1629.
    • (1995) Plant Physiol. , vol.108 , pp. 1623-1629
    • Grof, C.P.1    Winning, B.M.2    Scaysbrook, T.P.3    Hill, S.A.4    Leaver, C.J.5
  • 17
    • 0021520871 scopus 로고
    • Modulation of the activity of NAD-malic enzyme from Solanum tuberosum by changes in oligomeric state
    • Grover S.D., Wedding R.T. Modulation of the activity of NAD-malic enzyme from Solanum tuberosum by changes in oligomeric state. Arch. Biochem. Biophys. 1984, 234:418-425.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 418-425
    • Grover, S.D.1    Wedding, R.T.2
  • 18
    • 0028945792 scopus 로고
    • Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana
    • Guan Y., Rawsthorne S., Scofield G., Shaw P., Doonan J. Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana. J. Biol. Chem. 1995, 270:5412-5417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5412-5417
    • Guan, Y.1    Rawsthorne, S.2    Scofield, G.3    Shaw, P.4    Doonan, J.5
  • 20
    • 53049100891 scopus 로고    scopus 로고
    • Reactant stationary approximation in enzyme kinetics
    • Hanson S.M., Schnell S. Reactant stationary approximation in enzyme kinetics. J. Phys. Chem. A 2008, 112:8654-8658.
    • (2008) J. Phys. Chem. A , vol.112 , pp. 8654-8658
    • Hanson, S.M.1    Schnell, S.2
  • 21
    • 0142042960 scopus 로고    scopus 로고
    • Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves
    • Igamberdiev A.U., Gardeström P. Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves. Biochim. Biophys. Acta Bioenerg. 2003, 1606:117-125.
    • (2003) Biochim. Biophys. Acta Bioenerg. , vol.1606 , pp. 117-125
    • Igamberdiev, A.U.1    Gardeström, P.2
  • 22
    • 84856618188 scopus 로고    scopus 로고
    • 2 uptake by Rubisco: contribution of carbonic anhydrases and photorespiration to optimization of photosynthetic carbon assimilation
    • 2 uptake by Rubisco: contribution of carbonic anhydrases and photorespiration to optimization of photosynthetic carbon assimilation. Biosystems 2012, 107:158-166.
    • (2012) Biosystems , vol.107 , pp. 158-166
    • Igamberdiev, A.U.1    Roussel, M.R.2
  • 23
    • 0030744871 scopus 로고    scopus 로고
    • Involvement of cyanide-resistant and rotenone-insensitive pathways of mitochondrial electron transport during oxidation of glycine in higher plants
    • Igamberdiev A.U., Bykova N.V., Gardeström P. Involvement of cyanide-resistant and rotenone-insensitive pathways of mitochondrial electron transport during oxidation of glycine in higher plants. FEBS Lett. 1997, 412:265-269.
    • (1997) FEBS Lett. , vol.412 , pp. 265-269
    • Igamberdiev, A.U.1    Bykova, N.V.2    Gardeström, P.3
  • 24
    • 0034742741 scopus 로고    scopus 로고
    • The role of photorespiration in redox and energy balance of photosynthetic plant cells: a study with a barley mutant deficient in glycine decarboxylase
    • Igamberdiev A.U., Bykova N.V., Lea P.J., Gardeström P. The role of photorespiration in redox and energy balance of photosynthetic plant cells: a study with a barley mutant deficient in glycine decarboxylase. Physiol. Plant. 2001, 111:427-438.
    • (2001) Physiol. Plant. , vol.111 , pp. 427-438
    • Igamberdiev, A.U.1    Bykova, N.V.2    Lea, P.J.3    Gardeström, P.4
  • 25
    • 0028259187 scopus 로고
    • In vivo mitochondrial pyruvate dehydrogenase activity, studied by rapid fractionation of barley leaf protoplasts
    • Krömer S., Lernmark U., Gardeström P. In vivo mitochondrial pyruvate dehydrogenase activity, studied by rapid fractionation of barley leaf protoplasts. J. Plant Physiol. 1994, 144:485-490.
    • (1994) J. Plant Physiol. , vol.144 , pp. 485-490
    • Krömer, S.1    Lernmark, U.2    Gardeström, P.3
  • 27
    • 0028327946 scopus 로고
    • Distribution of pyruvate dehydrogenase complex activities between chloroplasts and mitochondria from leaves of different species
    • Lernmark U., Gardeström P. Distribution of pyruvate dehydrogenase complex activities between chloroplasts and mitochondria from leaves of different species. Plant Physiol. 1994, 106:1633-1638.
    • (1994) Plant Physiol. , vol.106 , pp. 1633-1638
    • Lernmark, U.1    Gardeström, P.2
  • 28
    • 0014567276 scopus 로고
    • Alpha-keto acid dehydrogenase complexes. XI. Comparative studies of regulatory properties of the pyruvate dehydrogenase complexes from kidney, heart, and liver mitochondria
    • Linn T.C., Pettit F.H., Hucho F., Reed L.J. Alpha-keto acid dehydrogenase complexes. XI. Comparative studies of regulatory properties of the pyruvate dehydrogenase complexes from kidney, heart, and liver mitochondria. Proc. Natl. Acad. Sci. U. S. A. 1969, 64:227-234.
    • (1969) Proc. Natl. Acad. Sci. U. S. A. , vol.64 , pp. 227-234
    • Linn, T.C.1    Pettit, F.H.2    Hucho, F.3    Reed, L.J.4
  • 29
    • 0034919355 scopus 로고    scopus 로고
    • Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings
    • Luethy M.H., Gemel J., Johnston M.L., Mooney B.P., Miernyk J.A., Randall D.D. Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings. Physiol. Plant. 2001, 112:559-566.
    • (2001) Physiol. Plant. , vol.112 , pp. 559-566
    • Luethy, M.H.1    Gemel, J.2    Johnston, M.L.3    Mooney, B.P.4    Miernyk, J.A.5    Randall, D.D.6
  • 30
    • 0001082984 scopus 로고
    • Control of the Krebs cycle in Arum spadix
    • Mac Dougall A.J., apRees T. Control of the Krebs cycle in Arum spadix. J. Plant Physiol. 1990, 137:683-690.
    • (1990) J. Plant Physiol. , vol.137 , pp. 683-690
    • Mac Dougall, A.J.1    Aprees, T.2
  • 31
    • 0002675681 scopus 로고
    • Some properties of plant mitochondrial pyruvate dehydrogenase kinases
    • Plenum, London, A.L. Moore, R.B. Beechey (Eds.)
    • Miernyk J.A., Randall D.D. Some properties of plant mitochondrial pyruvate dehydrogenase kinases. Plant Mitochondria 1987, 223-226. Plenum, London. A.L. Moore, R.B. Beechey (Eds.).
    • (1987) Plant Mitochondria , pp. 223-226
    • Miernyk, J.A.1    Randall, D.D.2
  • 32
    • 0000321273 scopus 로고
    • Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase
    • Miernyk J.A., Randall D.D. Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase. Plant Physiol. 1987, 83:311-315.
    • (1987) Plant Physiol. , vol.83 , pp. 311-315
    • Miernyk, J.A.1    Randall, D.D.2
  • 33
    • 0000321273 scopus 로고
    • Some kinetic and regulatory properties of the pea mitochondrial pyruvate dehydrogenase complex
    • Miernyk J.A., Randall D.D. Some kinetic and regulatory properties of the pea mitochondrial pyruvate dehydrogenase complex. Plant Physiol. 1987, 83:306-310.
    • (1987) Plant Physiol. , vol.83 , pp. 306-310
    • Miernyk, J.A.1    Randall, D.D.2
  • 34
    • 0032530354 scopus 로고    scopus 로고
    • Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato
    • Millar A.H., Knorpp C., Leaver C.J., Hill S.A. Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato. Biochem. J. 1998, 334:571-576.
    • (1998) Biochem. J. , vol.334 , pp. 571-576
    • Millar, A.H.1    Knorpp, C.2    Leaver, C.J.3    Hill, S.A.4
  • 36
    • 0027145202 scopus 로고
    • The regulation of pyruvate dehydrogenase activity in pea leaf mitochondria. The effect of respiration and oxidative phosphorylation
    • Moore A.L., Gemel J., Randall D.D. The regulation of pyruvate dehydrogenase activity in pea leaf mitochondria. The effect of respiration and oxidative phosphorylation. Plant Physiol. 1993, 103:1431-1435.
    • (1993) Plant Physiol. , vol.103 , pp. 1431-1435
    • Moore, A.L.1    Gemel, J.2    Randall, D.D.3
  • 37
    • 0020827956 scopus 로고
    • Symbolism and terminology in enzyme kinetics. Recommendations 1981
    • Nomenclature Committee of IUB Symbolism and terminology in enzyme kinetics. Recommendations 1981. Biochem. J. 1983, 213:561-571.
    • (1983) Biochem. J. , vol.213 , pp. 561-571
  • 38
    • 0027949710 scopus 로고
    • 2 and light responses of Coccomyxa, Chlamydomonas reinhardtii and barley protoplasts
    • 2 and light responses of Coccomyxa, Chlamydomonas reinhardtii and barley protoplasts. Plant Cell Environ. 1994, 17:65-72.
    • (1994) Plant Cell Environ. , vol.17 , pp. 65-72
    • Palmqvist, K.1    Ögren, E.2    Lernmark, U.3
  • 39
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel M.S., Roche T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 1990, 4:3224-3233.
    • (1990) FASEB J. , vol.4 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 40
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson G.L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 1977, 83:346-356.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 41
    • 0017712704 scopus 로고
    • Plant pyruvate dehydrogenase complex purification, characterization and regulation by metabolites and phosphorylation
    • Randall D.D., Rubin P.M., Fenko M. Plant pyruvate dehydrogenase complex purification, characterization and regulation by metabolites and phosphorylation. Biochim. Biophys. Acta 1977, 485:336-349.
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 336-349
    • Randall, D.D.1    Rubin, P.M.2    Fenko, M.3
  • 43
    • 1542500858 scopus 로고
    • Pyruvate dehydrogenase complexes from Ricinus communis endosperm
    • Rapp B.J., Miernyk J.A., Randall D.D. Pyruvate dehydrogenase complexes from Ricinus communis endosperm. J. Plant Physiol. 1987, 127:293-306.
    • (1987) J. Plant Physiol. , vol.127 , pp. 293-306
    • Rapp, B.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 44
    • 0024073689 scopus 로고
    • Interpreting non-competitive inhibition
    • Rehm H., Becker C.M. Interpreting non-competitive inhibition. Trends Pharmacol. Sci. 1988, 9:316-317.
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 316-317
    • Rehm, H.1    Becker, C.M.2
  • 45
    • 0001457057 scopus 로고
    • Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids
    • Reid E.E., Thompson P., Lyttle C.R., Dennis D.T. Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids. Plant Physiol. 1977, 59:842-848.
    • (1977) Plant Physiol. , vol.59 , pp. 842-848
    • Reid, E.E.1    Thompson, P.2    Lyttle, C.R.3    Dennis, D.T.4
  • 46
    • 0017807868 scopus 로고
    • Plant pyruvate dehydrogenase complex: analysis of the kinetic properties and metabolite regulation
    • Rubin P.M., Zahler W.L., Randall D.D. Plant pyruvate dehydrogenase complex: analysis of the kinetic properties and metabolite regulation. Arch. Biochem. Biophys. 1978, 188:70-77.
    • (1978) Arch. Biochem. Biophys. , vol.188 , pp. 70-77
    • Rubin, P.M.1    Zahler, W.L.2    Randall, D.D.3
  • 47
    • 0000702257 scopus 로고
    • Regulation of pea mitochondrial pyruvate dehydrogenase complex. Does photorespiratory ammonium influence mitochondrial carbon metabolism
    • Schuller K.A., Randall D.D. Regulation of pea mitochondrial pyruvate dehydrogenase complex. Does photorespiratory ammonium influence mitochondrial carbon metabolism. Plant Physiol. 1989, 89:1207-1212.
    • (1989) Plant Physiol. , vol.89 , pp. 1207-1212
    • Schuller, K.A.1    Randall, D.D.2
  • 48
    • 0025275081 scopus 로고
    • Mechanism of pyruvate inhibition of plant pyruvate dehydrogenase kinase and synergism with ADP
    • Schuller K.A., Randall D.D. Mechanism of pyruvate inhibition of plant pyruvate dehydrogenase kinase and synergism with ADP. Arch. Biochem. Biophys. 1990, 278:211-216.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 211-216
    • Schuller, K.A.1    Randall, D.D.2
  • 49
    • 0000781180 scopus 로고
    • Monovalent cation activation of plant pyruvate dehydrogenase kinase
    • Schuller K.A., Gemel J., Randall D.D. Monovalent cation activation of plant pyruvate dehydrogenase kinase. Plant Physiol. 1993, 102:139-143.
    • (1993) Plant Physiol. , vol.102 , pp. 139-143
    • Schuller, K.A.1    Gemel, J.2    Randall, D.D.3
  • 50
    • 0033178510 scopus 로고    scopus 로고
    • An unusual case of 'uncompetitive activation' by ascorbic acid: purification and kinetic properties of a myrosinase from Raphanus sativus seedlings
    • Shikita M., Fahey J.W., Golden T.R., Holtzclaw W.D., Talalay P. An unusual case of 'uncompetitive activation' by ascorbic acid: purification and kinetic properties of a myrosinase from Raphanus sativus seedlings. Biochem. J. 1999, 341:725-732.
    • (1999) Biochem. J. , vol.341 , pp. 725-732
    • Shikita, M.1    Fahey, J.W.2    Golden, T.R.3    Holtzclaw, W.D.4    Talalay, P.5
  • 51
    • 0000644785 scopus 로고
    • Immunological comparison of the pyruvate dehydrogenase complexes from pea mitochondria and chloroplasts
    • Taylor A.E., Cogdell R.I., Lindsay J.G. Immunological comparison of the pyruvate dehydrogenase complexes from pea mitochondria and chloroplasts. Planta 1992, 188:225-231.
    • (1992) Planta , vol.188 , pp. 225-231
    • Taylor, A.E.1    Cogdell, R.I.2    Lindsay, J.G.3
  • 52
    • 0001218473 scopus 로고    scopus 로고
    • Partial purification and characterization of the maize mitochondrial pyruvate dehydrogenase complex
    • Thelen J.J., Miernyk J.A., Randall D.D. Partial purification and characterization of the maize mitochondrial pyruvate dehydrogenase complex. Plant Physiol. 1998, 116:1443-1450.
    • (1998) Plant Physiol. , vol.116 , pp. 1443-1450
    • Thelen, J.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 54
    • 0345074089 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase complex activity in plant cells
    • Tovar-Méndez A., Miernyk J.A., Randall D.D. Regulation of pyruvate dehydrogenase complex activity in plant cells. Eur. J. Biochem. 2003, 270:1043-1049.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1043-1049
    • Tovar-Méndez, A.1    Miernyk, J.A.2    Randall, D.D.3
  • 55
    • 48949120193 scopus 로고    scopus 로고
    • Coimmunopurification of phosphorylated bacterial- and plant-type phosphoenolpyruvate carboxylases with the plastidial pyruvate dehydrogenase complex from developing castor oil seeds
    • Uhrig R.G., O'Leary B., Spang H.E., MacDonald J.A., She Y.M., Plaxton W.C. Coimmunopurification of phosphorylated bacterial- and plant-type phosphoenolpyruvate carboxylases with the plastidial pyruvate dehydrogenase complex from developing castor oil seeds. Plant Physiol. 2008, 146:1346-1357.
    • (2008) Plant Physiol. , vol.146 , pp. 1346-1357
    • Uhrig, R.G.1    O'Leary, B.2    Spang, H.E.3    MacDonald, J.A.4    She, Y.M.5    Plaxton, W.C.6
  • 56
    • 0042345186 scopus 로고
    • Some requirements for pyruvate oxidation by plant mitochondrial preparations
    • Walker D.A., Beevers H. Some requirements for pyruvate oxidation by plant mitochondrial preparations. Biochem. J. 1956, 62:120-127.
    • (1956) Biochem. J. , vol.62 , pp. 120-127
    • Walker, D.A.1    Beevers, H.2
  • 57
    • 0029981211 scopus 로고    scopus 로고
    • Enzyme inhibition in open systems. Superiority of uncompetitive agents
    • Westley A.M., Westley J. Enzyme inhibition in open systems. Superiority of uncompetitive agents. J. Biol. Chem. 1996, 271:5347-5352.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5347-5352
    • Westley, A.M.1    Westley, J.2
  • 58
    • 0000163072 scopus 로고
    • The tricarboxylic acid cycle in plant mitochondria: its operation and regulation
    • Springer, Berlin, R. Douce, D.A. Day (Eds.)
    • Wiskich J.T., Dry I.B. The tricarboxylic acid cycle in plant mitochondria: its operation and regulation. Higher Plant Cell Respiration 1985, 281-313. Springer, Berlin. R. Douce, D.A. Day (Eds.).
    • (1985) Higher Plant Cell Respiration , pp. 281-313
    • Wiskich, J.T.1    Dry, I.B.2
  • 59
    • 0001075709 scopus 로고
    • Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria. Implications for photorespiratory metabolism
    • Wiskich J.T., Bryce J.H., Day D.A., Dry I.B. Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria. Implications for photorespiratory metabolism. Plant Physiol. 1990, 93:611-616.
    • (1990) Plant Physiol. , vol.93 , pp. 611-616
    • Wiskich, J.T.1    Bryce, J.H.2    Day, D.A.3    Dry, I.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.