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Volumn 53, Issue , 2002, Pages 357-375

The complex fate of α-ketoacids

Author keywords

Intermediary metabolism; Mitochondria; Protein structure; Pyruvate dehydrogenase; Regulation

Indexed keywords

2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); ACID; MULTIENZYME COMPLEX; OXIDOREDUCTASE; PYRUVATE DEHYDROGENASE COMPLEX;

EID: 0037002327     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.53.100301.135251     Document Type: Review
Times cited : (140)

References (88)
  • 1
    • 0001755965 scopus 로고    scopus 로고
    • 3-Methylcrotonyl-coenzyme A carboxylase is a component of the mitochondrial leucine catabolic pathway in plants
    • Anderson MD, Che P, Song J, Nikolau BJ, Wurtele ES. 1998. 3-methylcrotonyl-coenzyme A carboxylase is a component of the mitochondrial leucine catabolic pathway in plants. Plant Physiol. 118:1127-38
    • (1998) Plant Physiol. , vol.118 , pp. 1127-1138
    • Anderson, M.D.1    Che, P.2    Song, J.3    Nikolau, B.J.4    Wurtele, E.S.5
  • 3
    • 0030681260 scopus 로고    scopus 로고
    • The significance of digital gene expression profiles
    • Audic S, Claverie JM. 1997. The significance of digital gene expression profiles. Genome Res. 7:986-95
    • (1997) Genome Res. , vol.7 , pp. 986-995
    • Audic, S.1    Claverie, J.M.2
  • 4
    • 0024381352 scopus 로고
    • Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae
    • Behal RH, Browning KS, Hall TB, Reed LJ. 1989. Cloning and nucleotide sequence of the gene for protein X from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 86:8732-36
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8732-8736
    • Behal, R.H.1    Browning, K.S.2    Hall, T.B.3    Reed, L.J.4
  • 5
    • 0026571038 scopus 로고
    • Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria
    • Bourguignon J, Macherel D, Neuburger M, Douce R. 1992. Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria. Eur. J. Biochem. 204:865-73
    • (1992) Eur. J. Biochem. , vol.204 , pp. 865-873
    • Bourguignon, J.1    Macherel, D.2    Neuburger, M.3    Douce, R.4
  • 6
    • 0025139727 scopus 로고
    • Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner
    • Budde RJA, Randall DD. 1990. Pea leaf mitochondrial pyruvate dehydrogenase complex is inactivated in vivo in a light-dependent manner. Proc. Natl. Acad. Sci. USA 87:673-76
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 673-676
    • Budde, R.J.A.1    Randall, D.D.2
  • 7
    • 0001158320 scopus 로고
    • Some kinetic and regulatory properties of the pea chloroplast pyruvate dehydrogenase complex
    • Camp PJ, Miernyk JA, Randall DD. 1988. Some kinetic and regulatory properties of the pea chloroplast pyruvate dehydrogenase complex. Biochim. Biophys. Acta 993:269-75
    • (1988) Biochim. Biophys. Acta , vol.993 , pp. 269-275
    • Camp, P.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 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 PJ, Randall DD. 1985. Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex. A source of acetyl-CoA and NADH for fatty acid biosynthesis. Plant Physiol. 77:571-77
    • (1985) Plant Physiol. , vol.77 , pp. 571-577
    • Camp, P.J.1    Randall, D.D.2
  • 9
    • 0031877568 scopus 로고    scopus 로고
    • Molecular cloning, functional expression, and characterization of pyruvate dehydrogenase kinase from anaerobic muscle of the parasitic nematode Ascaris suum
    • Chen W, Huang X, Komuniecki PR, Komuniecki R. 1998. Molecular cloning, functional expression, and characterization of pyruvate dehydrogenase kinase from anaerobic muscle of the parasitic nematode Ascaris suum. Arch. Biochem. Biophys. 353:181-89
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 181-189
    • Chen, W.1    Huang, X.2    Komuniecki, P.R.3    Komuniecki, R.4
  • 10
    • 0033118374 scopus 로고    scopus 로고
    • Nematode pyruvate dehydrogenase kinases: Role of the C-terminus in binding of the dihydrolipoyl transacetylase core of the pyruvate dehydrogenase complex
    • Chen W, Komuniecki PR, Komuniecki R. 1999. Nematode pyruvate dehydrogenase kinases: role of the C-terminus in binding of the dihydrolipoyl transacetylase core of the pyruvate dehydrogenase complex. Biochem. J. 339:103-9
    • (1999) Biochem. J. , vol.339 , pp. 103-109
    • Chen, W.1    Komuniecki, P.R.2    Komuniecki, R.3
  • 11
  • 12
    • 0019332668 scopus 로고
    • Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Pre-steady state kinetics and physical studies
    • Craig DW, Wedding RT. 1980. Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Pre-steady state kinetics and physical studies. J. Biol. Chem. 255:5769-75
    • (1980) J. Biol. Chem. , vol.255 , pp. 5769-5775
    • Craig, D.W.1    Wedding, R.T.2
  • 13
    • 0019332668 scopus 로고
    • Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Steady state kinetic studies
    • Craig DW, Wedding RT. 1980. Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Steady state kinetic studies. J. Biol. Chem. 255:5763-68
    • (1980) J. Biol. Chem. , vol.255 , pp. 5763-5768
    • Craig, D.W.1    Wedding, R.T.2
  • 14
    • 0028039125 scopus 로고
    • Pyruvate dehydrogenase complexes from the equine nematode, Parascaris equorum, and the canine cestode, Dipylidium caninum, helminths exhibiting anaerobic mitochondrial metabolism
    • Diaz F, Komuniecki RW. 1994. Pyruvate dehydrogenase complexes from the equine nematode, Parascaris equorum, and the canine cestode, Dipylidium caninum, helminths exhibiting anaerobic mitochondrial metabolism. Mol. Biochem. Parasitol. 67:289-99
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 289-299
    • Diaz, F.1    Komuniecki, R.W.2
  • 16
    • 0023655846 scopus 로고
    • 2-Oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: Interaction via a common coenzyme A pool
    • Dry IB, Wiskich JT. 1987. 2-oxoglutarate dehydrogenase and pyruvate dehydrogenase activities in plant mitochondria: interaction via a common coenzyme A pool. Arch. Biochem. Biophys. 257:92-99
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 92-99
    • Dry, I.B.1    Wiskich, J.T.2
  • 17
    • 0034113956 scopus 로고    scopus 로고
    • Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system
    • Faure M, Bourguignon J, Neuburger M, Macherel D, Sieker L, et al. 2000. Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. Eur. J. Biochem. 267:2890-98
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2890-2898
    • Faure, M.1    Bourguignon, J.2    Neuburger, M.3    Macherel, D.4    Sieker, L.5
  • 18
    • 0034102077 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA clones for the E1β and E2 subunits of the branched-chain α-ketoacid dehydrogenase complex in Arabidopsis
    • Fujiki Y, Sato T, Ito M, Watanabe A. 2000. Isolation and characterization of cDNA clones for the E1β and E2 subunits of the branched-chain α-ketoacid dehydrogenase complex in Arabidopsis. J. Biol. Chem. 275:6007-13
    • (2000) J. Biol. Chem. , vol.275 , pp. 6007-6013
    • Fujiki, Y.1    Sato, T.2    Ito, M.3    Watanabe, A.4
  • 19
    • 0001235725 scopus 로고
    • Light regulation of leaf mitochondrial pyruvate dehydrogenase complex
    • Gemel J, Randall DD. 1992. Light regulation of leaf mitochondrial pyruvate dehydrogenase complex. Plant Physiol. 100:908-14
    • (1992) Plant Physiol. , vol.100 , pp. 908-914
    • Gemel, J.1    Randall, D.D.2
  • 21
    • 0034913239 scopus 로고    scopus 로고
    • The origin and early evolution of mitochondria
    • Gray MW, Burger G, Lang BF. 2001. The origin and early evolution of mitochondria. Genome Biol. 2:1018.1-8.5
    • (2001) Genome Biol. , vol.2 , pp. 10181-10185
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 22
    • 0020047207 scopus 로고
    • Has the endosymbiont hypothesis been proven?
    • Gray MW, Doolittle WF. 1982. Has the endosymbiont hypothesis been proven? Microbiol. Rev. 46:1-42
    • (1982) Microbiol. Rev. , vol.46 , pp. 1-42
    • Gray, M.W.1    Doolittle, W.F.2
  • 23
    • 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. 1995. Cloning and characterization of a dihydrolipoamide acetyltransferase (E2) subunit of the pyruvate dehydrogenase complex from Arabidopsis thaliana. J. Biol. Chem. 270:5412-17
    • (1995) J. Biol. Chem. , vol.270 , pp. 5412-5417
    • Guan, Y.1    Rawsthorne, S.2    Scofield, G.3    Shaw, P.4    Doonan, J.5
  • 24
    • 0022373235 scopus 로고
    • Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Guest JR, Lewis HM, Graham LD, Packman LC, Perham RN. 1985. Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 185:743-54
    • (1985) J. Mol. Biol. , vol.185 , pp. 743-754
    • Guest, J.R.1    Lewis, H.M.2    Graham, L.D.3    Packman, L.C.4    Perham, R.N.5
  • 25
    • 0030877451 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex
    • Harris RA, Bowker-Kinley MM, Wu P, Jeng J, Popov KM. 1997. Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. J. Biol. Chem. 272:19746-51
    • (1997) J. Biol. Chem. , vol.272 , pp. 19746-19751
    • Harris, R.A.1    Bowker-Kinley, M.M.2    Wu, P.3    Jeng, J.4    Popov, K.M.5
  • 26
    • 0032522244 scopus 로고    scopus 로고
    • Expression of pyruvate dehydrogenase isoforms during the aerobic/anaerobic transition in the development of the parasitic nematode Ascaris suum: Altered stoichiometry of phosphorylation/inactivation
    • Huang YJ, Walker D, Chen W, Klingbeil M, Komuniecki R. 1998. Expression of pyruvate dehydrogenase isoforms during the aerobic/anaerobic transition in the development of the parasitic nematode Ascaris suum: altered stoichiometry of phosphorylation/inactivation. Arch. Biochem. Biophys. 352:263-70
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 263-270
    • Huang, Y.J.1    Walker, D.2    Chen, W.3    Klingbeil, M.4    Komuniecki, R.5
  • 27
    • 0022969384 scopus 로고
    • Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex
    • Jilka JM, Rahmatullah M, Kazemi M, Roche TE. 1986. Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex. J. Biol. Chem. 261:1858-67
    • (1986) J. Biol. Chem. , vol.261 , pp. 1858-1867
    • Jilka, J.M.1    Rahmatullah, M.2    Kazemi, M.3    Roche, T.E.4
  • 28
    • 0030859530 scopus 로고    scopus 로고
    • Cloning and molecular analyses of the Arabidopsis thaliana plastid pyruvate dehydrogenase subunits
    • Johnston ML, Luethy MH, Miernyk JA, Randall DD. 1997. Cloning and molecular analyses of the Arabidopsis thaliana plastid pyruvate dehydrogenase subunits. Biochim. Biophys. Acta 1321:200-6
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 200-206
    • Johnston, M.L.1    Luethy, M.H.2    Miernyk, J.A.3    Randall, D.D.4
  • 29
    • 0033948019 scopus 로고    scopus 로고
    • Import, processing, and assembly of the α- and β-subunits of chloroplast pyruvate dehydrogenase
    • Johnston ML, Miernyk JA, Randall DD. 2000. Import, processing, and assembly of the α- and β-subunits of chloroplast pyruvate dehydrogenase. Planta 211:72-76
    • (2000) Planta , vol.211 , pp. 72-76
    • Johnston, M.L.1    Miernyk, J.A.2    Randall, D.D.3
  • 30
    • 0022492836 scopus 로고
    • Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxoacid dehydrogenase complex
    • Jones SMA, Yeaman SJ. 1986. Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxoacid dehydrogenase complex. Biochem. J. 237:621-23
    • (1986) Biochem. J. , vol.237 , pp. 621-623
    • Jones, S.M.A.1    Yeaman, S.J.2
  • 31
    • 0034047473 scopus 로고    scopus 로고
    • The role of pyruvate dehydrogenase and acetylcoenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds
    • Ke J, Behal RH, Back SL, Nikolau BJ, Wurtele ES, Oliver DJ. 2000. The role of pyruvate dehydrogenase and acetylcoenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds. Plant Physiol. 123:497-508
    • (2000) Plant Physiol. , vol.123 , pp. 497-508
    • Ke, J.1    Behal, R.H.2    Back, S.L.3    Nikolau, B.J.4    Wurtele, E.S.5    Oliver, D.J.6
  • 32
    • 0029978098 scopus 로고    scopus 로고
    • Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum
    • Klingbeil MM, Walker DJ, Arnette R, Sidawy E, Hayton K, et al. 1996. Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum. J. Biol. Chem. 271:5451-57
    • (1996) J. Biol. Chem. , vol.271 , pp. 5451-5457
    • Klingbeil, M.M.1    Walker, D.J.2    Arnette, R.3    Sidawy, E.4    Hayton, K.5
  • 33
    • 0032563138 scopus 로고    scopus 로고
    • Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
    • Knapp JE, Mitchell DT, Yazdi MA, Ernst SR, Reed LJ, Hackert ML. 1998. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280:655-68
    • (1998) J. Mol. Biol. , vol.280 , pp. 655-668
    • Knapp, J.E.1    Mitchell, D.T.2    Yazdi, M.A.3    Ernst, S.R.4    Reed, L.J.5    Hackert, M.L.6
  • 34
    • 0017223847 scopus 로고
    • Structure, assembly and function of mammalian alpha-keto acid dehydrogenase complexes
    • Koike M, Koike K. 1975. Structure, assembly and function of mammalian alpha-keto acid dehydrogenase complexes. Adv. Biophys. 9:187-227
    • (1975) Adv. Biophys. , vol.9 , pp. 187-227
    • Koike, M.1    Koike, K.2
  • 35
    • 0028327946 scopus 로고
    • Distribution of pyruvate dehydrogenase complex activities between chloroplast and mitochondria from leaves of different species
    • Lernmark U, Gardestrom P. 1994. Distribution of pyruvate dehydrogenase complex activities between chloroplast and mitochondria from leaves of different species. Plant Physiol. 106:1633-38
    • (1994) Plant Physiol. , vol.106 , pp. 1633-1638
    • Lernmark, U.1    Gardestrom, P.2
  • 36
    • 0034919355 scopus 로고    scopus 로고
    • Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings
    • Luethy MH, Gemel J, Johnston ML, Mooney BP, Miernyk JA, Randall DD. 2001. Developmental expression of the mitochondrial pyruvate dehydrogenase complex in pea (Pisum sativum) seedlings. Physiol. Plant. 112:559-66
    • (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
  • 38
    • 0013357655 scopus 로고    scopus 로고
    • The nucleotide sequence of a cDNA encoding the E1-beta subunit of the branched-chain alpha-keto acid dehydrogenase from Arabidopsis thaliana (Accession No. AF061638) (PGR98-133)
    • Luethy MH, Miernyk JA, Randall DD. 1998. The nucleotide sequence of a cDNA encoding the E1-beta subunit of the branched-chain alpha-keto acid dehydrogenase from Arabidopsis thaliana (Accession No. AF061638) (PGR98-133). Plant Physiol. 118:329
    • (1998) Plant Physiol. , vol.118 , pp. 329
    • Luethy, M.H.1    Miernyk, J.A.2    Randall, D.D.3
  • 39
    • 0034721739 scopus 로고    scopus 로고
    • Molecular evidence of a unique lipoamide dehydrogenase in plastids: Analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana
    • Lutziger I, Oliver D. 2000. Molecular evidence of a unique lipoamide dehydrogenase in plastids: analysis of plastidic lipoamide dehydrogenase from Arabidopsis thaliana. FEBS Lett. 484:12-16
    • (2000) FEBS Lett. , vol.484 , pp. 12-16
    • Lutziger, I.1    Oliver, D.2
  • 40
    • 0034777745 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding mitochondrial lipoamide dehydrogenase from Arabidopsis thaliana
    • Lutziger I, Oliver D. 2001. Characterization of two cDNAs encoding mitochondrial lipoamide dehydrogenase from Arabidopsis thaliana. Plant Physiol. 127:615-23
    • (2001) Plant Physiol. , vol.127 , pp. 615-623
    • Lutziger, I.1    Oliver, D.2
  • 41
    • 0026683759 scopus 로고
    • Construction and properties of pyruvate dehydrogenase complexes with up to nine lipoyl domains per lipoate acetyltransferase chain
    • Machado RS, Clark DP, Guest JR. 1992. Construction and properties of pyruvate dehydrogenase complexes with up to nine lipoyl domains per lipoate acetyltransferase chain. FEMS Microbiol. Lett. 79:243-48
    • (1992) FEMS Microbiol. Lett. , vol.79 , pp. 243-248
    • Machado, R.S.1    Clark, D.P.2    Guest, J.R.3
  • 44
    • 0000321273 scopus 로고
    • Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase
    • Miernyk JA, Randall DD. 1987. Some properties of pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase. Plant Physiol. 83:306-10
    • (1987) Plant Physiol. , vol.83 , pp. 306-310
    • Miernyk, J.A.1    Randall, D.D.2
  • 45
    • 0000255885 scopus 로고    scopus 로고
    • Reversible phosphorylation as a mechanism for regulating activity of the mitochondrial pyruvate dehydrogenase complex
    • ed. IM Møller, P Gardestrom, K Glimelius, E Glaser. Leiden, The Neth.: Backhuys
    • Miernyk JA, Thelen JJ, Randall DD. 1998. Reversible phosphorylation as a mechanism for regulating activity of the mitochondrial pyruvate dehydrogenase complex. In Plant Mitochondria: From Gene to Function, ed. IM Møller, P Gardestrom, K Glimelius, E Glaser, pp. 321-27. Leiden, The Neth.: Backhuys
    • (1998) Plant Mitochondria: From Gene to Function , pp. 321-327
    • Miernyk, J.A.1    Thelen, J.J.2    Randall, D.D.3
  • 46
    • 0033569439 scopus 로고    scopus 로고
    • Plant mitochondrial 2-oxoglutarate dehydrogenase complex: Purification and characterization in potato
    • Millar AH, Hill SA, Leaver CJ. 1999. Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato. Biochem. J. 343:327-34
    • (1999) Biochem. J. , vol.343 , pp. 327-334
    • Millar, A.H.1    Hill, S.A.2    Leaver, C.J.3
  • 47
    • 0033568309 scopus 로고    scopus 로고
    • Characterization of the dihydrolipoamide acetyltransferase of the mitochondrial pyruvate dehydrogenase complex from potato and comparisons with similar enzymes in diverse plant species
    • Millar AH, Leaver CJ, Hill SA. 1999. Characterization of the dihydrolipoamide acetyltransferase of the mitochondrial pyruvate dehydrogenase complex from potato and comparisons with similar enzymes in diverse plant species. Eur. J. Biochem. 264:1-10
    • (1999) Eur. J. Biochem. , vol.264 , pp. 1-10
    • Millar, A.H.1    Leaver, C.J.2    Hill, S.A.3
  • 49
    • 0033868183 scopus 로고    scopus 로고
    • The dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched-chain α-ketoacid dehydrogenase complex forms a 24-mer core with octagonal symmetry
    • Mooney BP, Henzl MT, Miernyk JA, Randall DD. 2000. The dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched-chain α-ketoacid dehydrogenase complex forms a 24-mer core with octagonal symmetry. Protein Sci. 9:1334-39
    • (2000) Protein Sci. , vol.9 , pp. 1334-1339
    • Mooney, B.P.1    Henzl, M.T.2    Miernyk, J.A.3    Randall, D.D.4
  • 50
    • 0000649853 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA encoding the dihydrolipoylacyltransferase (E2) subunit of the branched-chain α-keto acid dehydrogenase complex from Arabidopsis thaliana (Accession No. AF038505) (PGR 98-071)
    • Mooney BP, Miernyk JA, Randall DD. 1998. Nucleotide sequence of a cDNA encoding the dihydrolipoylacyltransferase (E2) subunit of the branched-chain α-keto acid dehydrogenase complex from Arabidopsis thaliana (Accession No. AF038505) (PGR 98-071). Plant Physiol. 117:331
    • (1998) Plant Physiol. , vol.117 , pp. 331
    • Mooney, B.P.1    Miernyk, J.A.2    Randall, D.D.3
  • 51
    • 0013402548 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA encoding the E1α subunit of the branched-chain α-keto acid dehydrogenase complex from Arabidopsis thaliana (Accession No. AF077955) (PGR98-168)
    • Mooney BP, Miernyk JA, Randall DD. 1998. Nucleotide sequence of a cDNA encoding the E1α subunit of the branched-chain α-keto acid dehydrogenase complex from Arabidopsis thaliana (Accession No. AF077955) (PGR98-168). Plant Physiol. 118:711
    • (1998) Plant Physiol. , vol.118 , pp. 711
    • Mooney, B.P.1    Miernyk, J.A.2    Randall, D.D.3
  • 52
    • 0033150518 scopus 로고    scopus 로고
    • Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the pyruvate dehydrogenase complex (E2) from Arabidopsis
    • Mooney BP, Miernyk JA, Randall DD. 1999. Cloning and characterization of the dihydrolipoamide S-acetyltransferase subunit of the pyruvate dehydrogenase complex (E2) from Arabidopsis. Plant Physiol. 120:443-51
    • (1999) Plant Physiol. , vol.120 , pp. 443-451
    • Mooney, B.P.1    Miernyk, J.A.2    Randall, D.D.3
  • 54
    • 0034067488 scopus 로고    scopus 로고
    • Staphylococcal protein A as a fusion partner directs secretion of the E1a and E1/β subunits of pea mitochondrial pyruvate dehydrogenase by Bacillus subtilis
    • Moreno JI, Miernyk JA, Randall DD. 2000. Staphylococcal protein A as a fusion partner directs secretion of the E1a and E1/β subunits of pea mitochondrial pyruvate dehydrogenase by Bacillus subtilis. Protein Expr. Purif. 18:242-48
    • (2000) Protein Expr. Purif. , vol.18 , pp. 242-248
    • Moreno, J.I.1    Miernyk, J.A.2    Randall, D.D.3
  • 55
    • 0020483026 scopus 로고
    • Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
    • Odessey R. 1982. Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity. Biochem. J. 204:353-56
    • (1982) Biochem. J. , vol.204 , pp. 353-356
    • Odessey, R.1
  • 57
    • 0022465302 scopus 로고
    • Role of branched-chain 2-oxoacid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism
    • Paxton R, Scislowski PWD, Davis J, Harris RA. 1986. Role of branched-chain 2-oxoacid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism. Biochem. J. 234:295-303
    • (1986) Biochem. J. , vol.234 , pp. 295-303
    • Paxton, R.1    Scislowski, P.W.D.2    Davis, J.3    Harris, R.A.4
  • 58
    • 2442728373 scopus 로고
    • Purification and characterization of branched-chain α-ketoacid dehydrogenase complex of bovine kidney
    • Pettit FH, Yeaman SJ, Reed LJ. 1978. Purification and characterization of branched-chain α-ketoacid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA 75:1881-85
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1881-1885
    • Pettit, F.H.1    Yeaman, S.J.2    Reed, L.J.3
  • 59
    • 0002166304 scopus 로고    scopus 로고
    • Regulation of leaf mitochondrial pyruvate dehydrogenase complex activity by reversible phosphorylation
    • eds. PR Shewry, NG Halford, R Hooley. Oxford, UK: Clarendon
    • Randall DD, Miernyk JA, David NR, Gemel J, Luethy MH. 1996. Regulation of leaf mitochondrial pyruvate dehydrogenase complex activity by reversible phosphorylation. In Protein Phosphorylation in Plants, eds. PR Shewry, NG Halford, R Hooley, pp. 87-103. Oxford, UK: Clarendon
    • (1996) Protein Phosphorylation in Plants , pp. 87-103
    • Randall, D.D.1    Miernyk, J.A.2    David, N.R.3    Gemel, J.4    Luethy, M.H.5
  • 61
    • 0017712704 scopus 로고
    • Plant pyruvate dehydrogenase complex purification, characterization and regulation by metabolites and phosphorylation
    • Randall DD, Rubin PM, Fenko M. 1977. Plant pyruvate dehydrogenase complex purification, characterization and regulation by metabolites and phosphorylation. Biochim. Biophys. Acta 485:336-49
    • (1977) Biochim. Biophys. Acta , vol.485 , pp. 336-349
    • Randall, D.D.1    Rubin, P.M.2    Fenko, M.3
  • 62
    • 0013356447 scopus 로고
    • Pyruvate dehydrogenase complex from germinating castor bean endosperm
    • Rapp BJ, Randall DD. 1980. Pyruvate dehydrogenase complex from germinating castor bean endosperm. Plant Physiol. 65:314-18
    • (1980) Plant Physiol. , vol.65 , pp. 314-318
    • Rapp, B.J.1    Randall, D.D.2
  • 64
    • 0035914303 scopus 로고    scopus 로고
    • A trail of research from lipoic acid to α-keto acid dehydrogenase complexes
    • Reed LJ. 2001. A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J. Biol. Chem. 276:38329-36
    • (2001) J. Biol. Chem. , vol.276 , pp. 38329-38336
    • Reed, L.J.1
  • 65
    • 0001457057 scopus 로고
    • Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids
    • Reid EE, Thompson P, Lyttle CR, Dennis DT. 1977. Pyruvate dehydrogenase complex from higher plant mitochondria and proplastids. Plant Physiol. 59:842-48
    • (1977) Plant Physiol. , vol.59 , pp. 842-848
    • Reid, E.E.1    Thompson, P.2    Lyttle, C.R.3    Dennis, D.T.4
  • 66
    • 0035224979 scopus 로고    scopus 로고
    • Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms
    • Roche TE, Baker J, Yan X, Hiromasa Y, Gong X, et al. 2001. Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms. Prog. Nucleic Acid Res. Mol. Biol. 70:33-75
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.70 , pp. 33-75
    • Roche, T.E.1    Baker, J.2    Yan, X.3    Hiromasa, Y.4    Gong, X.5
  • 67
    • 0035029530 scopus 로고    scopus 로고
    • Pyruvate:NADP+ oxidoreductase from the mitochondrion of Euglena gracilis and from the Api-complexan Crytosproidium parvum: A biochemical relic linking pyruvate metabolism in mitochondriate and amitochondriate protists
    • Rotte C, Stejskal F, Zhu G, Keithly JS, Keithly Martin. 2001. Pyruvate:NADP+ oxidoreductase from the mitochondrion of Euglena gracilis and from the Api-complexan Crytosproidium parvum: a biochemical relic linking pyruvate metabolism in mitochondriate and amitochondriate protists. Mol. Biol. Evol. 18:710-20
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 710-720
    • Rotte, C.1    Stejskal, F.2    Zhu, G.3    Keithly, J.S.4    Keithly, M.5
  • 68
    • 0000702257 scopus 로고
    • Regulation of pea mitochondrial pyruvate dehydrogenase complex: Does photorespiratory ammonium influence mitochondrial carbon metabolism?
    • Schuller KA, Randall DD. 1989. Regulation of pea mitochondrial pyruvate dehydrogenase complex: Does photorespiratory ammonium influence mitochondrial carbon metabolism? Plant Physiol. 89:1207-12
    • (1989) Plant Physiol. , vol.89 , pp. 1207-1212
    • Schuller, K.A.1    Randall, D.D.2
  • 69
    • 0020789034 scopus 로고
    • The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component
    • Stephens PE, Darlison MG, Lewis HM, Guest JR. 1983. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur. J. Biochem. 133:481-89
    • (1983) Eur. J. Biochem. , vol.133 , pp. 481-489
    • Stephens, P.E.1    Darlison, M.G.2    Lewis, H.M.3    Guest, J.R.4
  • 71
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408:796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 72
    • 0024264831 scopus 로고
    • Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex
    • Thekkumkara TJ, Ho L, Wexler ID, Pons G, Liu TC, Patel MS. 1988. Nucleotide sequence of a cDNA for the dihydrolipoamide acetyltransferase component of human pyruvate dehydrogenase complex. FEBS Lett. 240:45-48
    • (1988) FEBS Lett. , vol.240 , pp. 45-48
    • Thekkumkara, T.J.1    Ho, L.2    Wexler, I.D.3    Pons, G.4    Liu, T.C.5    Patel, M.S.6
  • 73
    • 0001330567 scopus 로고    scopus 로고
    • Nucleotide and deduced amino acid sequences of the pyruvate dehydrogenase kinase from Arabidopsis thaliana (Accession No. AF039406) (PGR98-192)
    • Thelen JJ, Miernyk JA, Randall DD. 1998. Nucleotide and deduced amino acid sequences of the pyruvate dehydrogenase kinase from Arabidopsis thaliana (Accession No. AF039406) (PGR98-192). Plant Physiol. 118:1533
    • (1998) Plant Physiol. , vol.118 , pp. 1533
    • Thelen, J.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 74
    • 0033080473 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of the mitochondrial pyruvate dehydrogenase from maize
    • Thelen JJ, Miernyk JA, Randall DD. 1999. Molecular cloning and expression analysis of the mitochondrial pyruvate dehydrogenase from maize. Plant Physiol. 119:635-43
    • (1999) Plant Physiol. , vol.119 , pp. 635-643
    • Thelen, J.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 75
    • 0034234737 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase from Arabidopsis thaliana: A protein histidine kinase that phosphorylates serine residues
    • Thelen JJ, Miernyk JA, Randall DD. 2000. Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues. Biochem. J. 349:195-201
    • (2000) Biochem. J. , vol.349 , pp. 195-201
    • Thelen, J.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 76
    • 0033618390 scopus 로고    scopus 로고
    • The dihydrolipoamide S-acetyltransferase subunit of the mitochondrial pyruvate dehydrogenase complex from maize contains a single lipoyl domain
    • Thelen JJ, Muszynski MG, David NR, Luethy MH, Elthon TE, et al. 1999. The dihydrolipoamide S-acetyltransferase subunit of the mitochondrial pyruvate dehydrogenase complex from maize contains a single lipoyl domain. J. Biol. Chem. 274:21769-75
    • (1999) J. Biol. Chem. , vol.274 , pp. 21769-21775
    • Thelen, J.J.1    Muszynski, M.G.2    David, N.R.3    Luethy, M.H.4    Elthon, T.E.5
  • 77
  • 78
    • 0000721845 scopus 로고    scopus 로고
    • Heterogeneity of mitochondrial protein biogenesis during primary leaf development in barley
    • Thompson P, Bowsher CG, Tobin AK. 1998. Heterogeneity of mitochondrial protein biogenesis during primary leaf development in barley. Plant Physiol. 118:1089-99
    • (1998) Plant Physiol. , vol.118 , pp. 1089-1099
    • Thompson, P.1    Bowsher, C.G.2    Tobin, A.K.3
  • 79
    • 0013364505 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 80
    • 84912764146 scopus 로고
    • Purification of the chloroplast pyruvate dehydrogenase from spinach and maize mesophyll
    • Treede H-J, Heise K-P. 1986. Purification of the chloroplast pyruvate dehydrogenase from spinach and maize mesophyll. Z. Naturforsch. Teil C 41:149-55
    • (1986) Z. Naturforsch. Teil C , vol.41 , pp. 149-155
    • Treede, H.-J.1    Heise, K.-P.2
  • 81
    • 0015239349 scopus 로고
    • Nucleotide activation of cauliflower alpha-keto-glutarate dehydrogenase
    • Wedding RT, Black MK. 1971. Nucleotide activation of cauliflower alpha-keto-glutarate dehydrogenase. J. Biol. Chem. 246:1638-43
    • (1971) J. Biol. Chem. , vol.246 , pp. 1638-1643
    • Wedding, R.T.1    Black, M.K.2
  • 82
    • 0034521752 scopus 로고    scopus 로고
    • A new set of Arabidopsis expressed sequence tags from developing seeds. The metabolic pathway from carbohydrates to seed oil
    • White JA, Todd J, Newman T, Focks N, Girke T, et al. 2000. A new set of Arabidopsis expressed sequence tags from developing seeds. The metabolic pathway from carbohydrates to seed oil. Plant Physiol. 124:1582-94
    • (2000) Plant Physiol. , vol.124 , pp. 1582-1594
    • White, J.A.1    Todd, J.2    Newman, T.3    Focks, N.4    Girke, T.5
  • 83
    • 0001184797 scopus 로고
    • Pyruvate dehydrogenase complex from chloroplasts of Pisum sativum
    • Williams M, Randall DD. 1979. Pyruvate dehydrogenase complex from chloroplasts of Pisum sativum. Plant Physiol. 64:1099-103
    • (1979) Plant Physiol. , vol.64 , pp. 1099-1103
    • Williams, M.1    Randall, D.D.2
  • 85
    • 0028129831 scopus 로고
    • In vitro reconstitution of the 24-meric inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: Requirement for chaperonins GroEL and GroES
    • Wynn RM, Davie JR, Zhi W, Cox RP, Chuang DT. 1994. In vitro reconstitution of the 24-meric inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES. Biochemistry 33: 8962-68
    • (1994) Biochemistry , vol.33 , pp. 8962-8968
    • Wynn, R.M.1    Davie, J.R.2    Zhi, W.3    Cox, R.P.4    Chuang, D.T.5
  • 86
    • 0024578239 scopus 로고
    • The 2-oxoacid dehydrogenase complexes: Recent advances
    • Yeaman SJ. 1989. The 2-oxoacid dehydrogenase complexes: recent advances. Biochem. J. 257:625-32
    • (1989) Biochem. J. , vol.257 , pp. 625-632
    • Yeaman, S.J.1
  • 88
    • 0033390795 scopus 로고    scopus 로고
    • Effects of antisense repression of an Arabidopsis thaliana pyruvate dehydrogenase kinase cDNA on plant development
    • Zou J, Qi Q, Katavic V, Marillia EF, Taylor DC. 1999. Effects of antisense repression of an Arabidopsis thaliana pyruvate dehydrogenase kinase cDNA on plant development. Plant Mol. Biol. 41:837-49
    • (1999) Plant Mol. Biol. , vol.41 , pp. 837-849
    • Zou, J.1    Qi, Q.2    Katavic, V.3    Marillia, E.F.4    Taylor, D.C.5


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