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Volumn 71, Issue 2, 2008, Pages 874-890

Structure-function relationships in the 2-oxo acid dehydrogenase family: Substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins

Author keywords

2 oxo acid dehydrogenase; 2 oxo 4 hydroxyglutarate; 2 oxoadipate; DHTKD1; Glyoxylate; Lipoic acid; Neurodegeneration; OGDHL; Thiamine diphosphate

Indexed keywords

2 OXOACID DEHYDROGENASE; 2 OXOGLUTARIC ACID; ACETALDEHYDE; CALCIUM ION; CARBOXYLIC ACID DERIVATIVE; GLYOXYLIC ACID; OXOGLUTARATE DEHYDROGENASE;

EID: 41149139014     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21766     Document Type: Article
Times cited : (76)

References (93)
  • 1
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham RN. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu Rev Biochem 2000;69:961-1004.
    • (2000) Annu Rev Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 2
    • 0036545372 scopus 로고    scopus 로고
    • Substrate channeling in 2-oxo acid dehydrogenase multienzyme complexes
    • Perham RN, Jones DD, Chauhan HJ, Howard MJ. Substrate channeling in 2-oxo acid dehydrogenase multienzyme complexes. Biochem Soc Trans 2002;30:47-51.
    • (2002) Biochem Soc Trans , vol.30 , pp. 47-51
    • Perham, R.N.1    Jones, D.D.2    Chauhan, H.J.3    Howard, M.J.4
  • 3
    • 33751303926 scopus 로고    scopus 로고
    • Molecular architecture of the pyruvate dehydrogenase complex: Bridging the gap
    • Smolle M, Lindsay JG. Molecular architecture of the pyruvate dehydrogenase complex: bridging the gap. Biochem Soc Trans 2006;34:815-818.
    • (2006) Biochem Soc Trans , vol.34 , pp. 815-818
    • Smolle, M.1    Lindsay, J.G.2
  • 5
    • 0028342532 scopus 로고
    • Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamid dehydrogenase
    • Hein S, Steinbuchel A. Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamid dehydrogenase. J Bacteriol 1994;176:4394-4408.
    • (1994) J Bacteriol , vol.176 , pp. 4394-4408
    • Hein, S.1    Steinbuchel, A.2
  • 6
    • 0031591386 scopus 로고    scopus 로고
    • Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis
    • De la Sierra IL, Pernot L, Prange T, Saludjian P, Schiltz M, Fourme R, Padron G. Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis. J Mol Biol 1997;269:129-141.
    • (1997) J Mol Biol , vol.269 , pp. 129-141
    • De la Sierra, I.L.1    Pernot, L.2    Prange, T.3    Saludjian, P.4    Schiltz, M.5    Fourme, R.6    Padron, G.7
  • 8
    • 0036096734 scopus 로고    scopus 로고
    • Functional role for a 2-oxo acid dehydrogenase in the halophilic archaeon Haloferax volcanii
    • Wanner C, Soppa J. Functional role for a 2-oxo acid dehydrogenase in the halophilic archaeon Haloferax volcanii. J Bacteriol 2002;184:3114-3121.
    • (2002) J Bacteriol , vol.184 , pp. 3114-3121
    • Wanner, C.1    Soppa, J.2
  • 9
    • 0030444169 scopus 로고    scopus 로고
    • Molecular cloning of the Corinebacterium glutamicum (Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase
    • Usuda Y, Tujimoto N, Abe C, Asakura Y, Kimura E, Kawahara Y, Kurahashi O, Matsui H. Molecular cloning of the Corinebacterium glutamicum (Brevibacterium lactofermentum' AJ12036) odhA gene encoding a novel type of 2-oxoglutarate dehydrogenase. Microbiology 1996;142:3347-3354.
    • (1996) Microbiology , vol.142 , pp. 3347-3354
    • Usuda, Y.1    Tujimoto, N.2    Abe, C.3    Asakura, Y.4    Kimura, E.5    Kawahara, Y.6    Kurahashi, O.7    Matsui, H.8
  • 10
    • 33744950488 scopus 로고    scopus 로고
    • Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the Odhl protein
    • Niebisch A, Kabus A, Schulz C, Weil B, Bott M. Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the Odhl protein. J Biol Chem 2006;281:12300-12307.
    • (2006) J Biol Chem , vol.281 , pp. 12300-12307
    • Niebisch, A.1    Kabus, A.2    Schulz, C.3    Weil, B.4    Bott, M.5
  • 11
    • 33644912328 scopus 로고    scopus 로고
    • Disruption of sucA, which encodes the E1 subunit of alpha-ketoglutarate dehydrogenase, affects the survival of Nitrosomonas europaea in stationary phase
    • Hommes NG, Kurth EG, Sayavedra-Soto LA, Arp DJ. Disruption of sucA, which encodes the E1 subunit of alpha-ketoglutarate dehydrogenase, affects the survival of Nitrosomonas europaea in stationary phase. J Bacteriol 2006;188:343-347.
    • (2006) J Bacteriol , vol.188 , pp. 343-347
    • Hommes, N.G.1    Kurth, E.G.2    Sayavedra-Soto, L.A.3    Arp, D.J.4
  • 12
    • 0037039818 scopus 로고    scopus 로고
    • Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein
    • Bryk R, Lima CD, Erdjument-Bromage H, Tempst P, Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 2002;295:1073-1077.
    • (2002) Science , vol.295 , pp. 1073-1077
    • Bryk, R.1    Lima, C.D.2    Erdjument-Bromage, H.3    Tempst, P.4    Nathan, C.5
  • 13
    • 0024268196 scopus 로고
    • Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase
    • Oku H, Kaneda T. Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase. J Biol Chem 1988;263:18386-18396.
    • (1988) J Biol Chem , vol.263 , pp. 18386-18396
    • Oku, H.1    Kaneda, T.2
  • 14
    • 0027288094 scopus 로고
    • The primary structure of branched-chain α-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other α-oxo acid dehydrogenases
    • Wang G-F, Kuriki T, Roy KL, Kaneda T. The primary structure of branched-chain α-oxo acid dehydrogenase from Bacillus subtilis and its similarity to other α-oxo acid dehydrogenases. Eur J Biochem 1993;1091-1099.
    • (1993) Eur J Biochem , pp. 1091-1099
    • Wang, G.-F.1    Kuriki, T.2    Roy, K.L.3    Kaneda, T.4
  • 15
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WGJ. Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat Struct Biol 1999;785-792.
    • (1999) Nat Struct Biol , pp. 785-792
    • Aevarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.J.5
  • 16
    • 0034653468 scopus 로고    scopus 로고
    • Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease
    • Aevarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WGJ. Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure 2000;8:277-291.
    • (2000) Structure , vol.8 , pp. 277-291
    • Aevarsson, A.1    Chuang, J.L.2    Wynn, R.M.3    Turley, S.4    Chuang, D.T.5    Hol, W.G.J.6
  • 18
    • 1642355234 scopus 로고    scopus 로고
    • Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography
    • Nakai T, Nakagawa N, Maoka N, Masui R, Kuramitsu S, Kamiya N. Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography. J Mol Biol 2004;337:1011-1033.
    • (2004) J Mol Biol , vol.337 , pp. 1011-1033
    • Nakai, T.1    Nakagawa, N.2    Maoka, N.3    Masui, R.4    Kuramitsu, S.5    Kamiya, N.6
  • 19
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase
    • Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS. Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J Biol Chem 2003;278:21240-21246.
    • (2003) J Biol Chem , vol.278 , pp. 21240-21246
    • Ciszak, E.M.1    Korotchkina, L.G.2    Dominiak, P.M.3    Sidhu, S.4    Patel, M.S.5
  • 20
    • 0027479683 scopus 로고
    • Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase
    • Muller YA, Schulz GE. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 1993;259:965-967.
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.E.2
  • 21
    • 32044451080 scopus 로고    scopus 로고
    • Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate
    • Cavazza C, Contreras-Martel C, Pieulle L, Chabriere E, Hatchikian EC, Fontecilla-Camps JC. Flexibility of thiamine diphosphate revealed by kinetic crystallographic studies of the reaction of pyruvate-ferredoxin oxidoreductase with pyruvate. Structure 2006;14:217-224.
    • (2006) Structure , vol.14 , pp. 217-224
    • Cavazza, C.1    Contreras-Martel, C.2    Pieulle, L.3    Chabriere, E.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 23
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution
    • Dyda F, Furey W, Swaminathan S, Sax M, Farrenkopf B, Jordan F. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Å resolution. Biochemistry 1993;32:6165-6170.
    • (1993) Biochemistry , vol.32 , pp. 6165-6170
    • Dyda, F.1    Furey, W.2    Swaminathan, S.3    Sax, M.4    Farrenkopf, B.5    Jordan, F.6
  • 24
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins CF, Borges A, Perham RN. A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett 1989;255:77-82.
    • (1989) FEBS Lett , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 25
    • 0027265567 scopus 로고
    • The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex
    • Robinson BH, Chun K. The relationships between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex. FEBS Lett 1993;328:99-102.
    • (1993) FEBS Lett , vol.328 , pp. 99-102
    • Robinson, B.H.1    Chun, K.2
  • 26
    • 0027515306 scopus 로고
    • Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids
    • Sundstrom M, Lindqvist Y, Schneider G, Hellman U, Ronne H. Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids. J Biol Chem 1993;268:24346-24352.
    • (1993) J Biol Chem , vol.268 , pp. 24346-24352
    • Sundstrom, M.1    Lindqvist, Y.2    Schneider, G.3    Hellman, U.4    Ronne, H.5
  • 27
    • 0025868806 scopus 로고
    • Sequence conservation in the α and β subunits of pyruvate dehydrogenase and its similarity to branched-chain α-keto acid dehydrogenase
    • Wexler ID, Hemalatha SG, Patel MS. Sequence conservation in the α and β subunits of pyruvate dehydrogenase and its similarity to branched-chain α-keto acid dehydrogenase. FEBS Lett 1991;282:209-213.
    • (1991) FEBS Lett , vol.282 , pp. 209-213
    • Wexler, I.D.1    Hemalatha, S.G.2    Patel, M.S.3
  • 28
    • 0030837376 scopus 로고    scopus 로고
    • The pyruvate dehydrogenase complex of the chemolithoautotrophic bacterium Thiobacillus ferrooxidans has an unusual E2-E3 subunit fusion
    • Powles R, Rawlings D. The pyruvate dehydrogenase complex of the chemolithoautotrophic bacterium Thiobacillus ferrooxidans has an unusual E2-E3 subunit fusion. Microbiology 1997;143:2189-2195.
    • (1997) Microbiology , vol.143 , pp. 2189-2195
    • Powles, R.1    Rawlings, D.2
  • 29
    • 0028239903 scopus 로고
    • Expression in Escherichia coli of genes encoding the E1A and E1B subunits of the pyruvate dehydrogenase complex of Bacillus stearothermophilus and assembly of a functional E1 component (A2B2) in vitro
    • Lessard IAD, Perham RN. Expression in Escherichia coli of genes encoding the E1A and E1B subunits of the pyruvate dehydrogenase complex of Bacillus stearothermophilus and assembly of a functional E1 component (A2B2) in vitro. J Biol Chem 1994;269:10378-10383.
    • (1994) J Biol Chem , vol.269 , pp. 10378-10383
    • Lessard, I.A.D.1    Perham, R.N.2
  • 30
    • 0021447442 scopus 로고
    • Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12
    • Darlison MG, Spencer ME, Guest JR. Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate dehydrogenase of Escherichia coli K12. Eur J Biochem 1984;141:351-359.
    • (1984) Eur J Biochem , vol.141 , pp. 351-359
    • Darlison, M.G.1    Spencer, M.E.2    Guest, J.R.3
  • 31
    • 0032537555 scopus 로고    scopus 로고
    • Cloning, structure, chromosomal localization and promoter analysis of human 2-oxoglutarate dehydrogenase gene
    • Koike K. Cloning, structure, chromosomal localization and promoter analysis of human 2-oxoglutarate dehydrogenase gene. Biochim Biophys Acta 1998;1385:373-384.
    • (1998) Biochim Biophys Acta , vol.1385 , pp. 373-384
    • Koike, K.1
  • 33
    • 0025868849 scopus 로고
    • The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase
    • Matuda S, Nakano K, Ohta S, Saheki T, Kawanishi Y, Miyata T. The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase. Biochim Biophys Acta 1991;1089:1-7.
    • (1991) Biochim Biophys Acta , vol.1089 , pp. 1-7
    • Matuda, S.1    Nakano, K.2    Ohta, S.3    Saheki, T.4    Kawanishi, Y.5    Miyata, T.6
  • 35
    • 33947579630 scopus 로고    scopus 로고
    • Enzymecatalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases
    • Bunik VI, Schloss JV, Pinto JT, Gibson GE, Cooper AJL. Enzymecatalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases. Neurochem Res 2007;32:871-891.
    • (2007) Neurochem Res , vol.32 , pp. 871-891
    • Bunik, V.I.1    Schloss, J.V.2    Pinto, J.T.3    Gibson, G.E.4    Cooper, A.J.L.5
  • 36
    • 23244435445 scopus 로고    scopus 로고
    • The α-ketoglutarate dehydrogenase complex: A mediator between mitochondria and oxidative stress in neurodegeneration
    • Gibson GE, Blass JP, Beal MF, Bunik V The α-ketoglutarate dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration. Mol Neurobiol 2005;31:43-63.
    • (2005) Mol Neurobiol , vol.31 , pp. 43-63
    • Gibson, G.E.1    Blass, J.P.2    Beal, M.F.3    Bunik, V.4
  • 37
    • 0025021822 scopus 로고
    • The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1 Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component
    • Schulze E, Westphal AH, Hanemaaijer R, De Kok A. The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1 Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component. Eur J Biochem 1990;187:229-234.
    • (1990) Eur J Biochem , vol.187 , pp. 229-234
    • Schulze, E.1    Westphal, A.H.2    Hanemaaijer, R.3    De Kok, A.4
  • 38
    • 33644876924 scopus 로고    scopus 로고
    • Birney E, Andrews D, Caccamo M, Chen Y, Clarke L, Coates G, Cox T, Cunningham F, Curwen V, Cutts T, Down T, Durbin R, Fernandez-Suarez XM, Flicek P, Graf S, Hammond M, Herrero J, Howe K, Iyer V, Jekosch K, Kahari A, Kasprzyk A, Keefe D, Kokocinski F, Kulesha E, London D, Longden I, Melsopp C, Meidl P, Overduin B, Parker A, Proctor G, Prlic A, Rae M, Rios D, Redmond S, Schuster M, Sealy I, Searle S, Severin J, Slater G, Smedley D, Smith J, Stabenau A, Stalker J, Trevanion S, Ureta-Vidal A, Vogel J, White S, Woodwark C, Hubbard TJ. Ensembl 2006. Nucl Acids Res 2006;34:D556-D561.
    • Birney E, Andrews D, Caccamo M, Chen Y, Clarke L, Coates G, Cox T, Cunningham F, Curwen V, Cutts T, Down T, Durbin R, Fernandez-Suarez XM, Flicek P, Graf S, Hammond M, Herrero J, Howe K, Iyer V, Jekosch K, Kahari A, Kasprzyk A, Keefe D, Kokocinski F, Kulesha E, London D, Longden I, Melsopp C, Meidl P, Overduin B, Parker A, Proctor G, Prlic A, Rae M, Rios D, Redmond S, Schuster M, Sealy I, Searle S, Severin J, Slater G, Smedley D, Smith J, Stabenau A, Stalker J, Trevanion S, Ureta-Vidal A, Vogel J, White S, Woodwark C, Hubbard TJ. Ensembl 2006. Nucl Acids Res 2006;34:D556-D561.
  • 39
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position-specific scoring matrices. J Mol Biol 1999;292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 40
    • 33645234725 scopus 로고    scopus 로고
    • Molecular structure of a 9-Mda icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopy
    • Milne JL, Wu X, Borgnia MJ, Lengyel JS, Brooks BR, Shi D, Perham RN, Subramaniam S. Molecular structure of a 9-Mda icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopy. J Biol Chem 2006;281:4364-4370.
    • (2006) J Biol Chem , vol.281 , pp. 4364-4370
    • Milne, J.L.1    Wu, X.2    Borgnia, M.J.3    Lengyel, J.S.4    Brooks, B.R.5    Shi, D.6    Perham, R.N.7    Subramaniam, S.8
  • 41
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: The role of polar. GxxxG-like and proline motifs
    • Senes A, Engel DE, DeGrado WF. Folding of helical membrane proteins: the role of polar. GxxxG-like and proline motifs. Curr Opin Struct Biol 2004;14:465-479.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 42
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • Small I, Peeters N, Legeai F, Lurin C. Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences. Proteomics 2004;4:1581-1590.
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 43
    • 84856980739 scopus 로고    scopus 로고
    • Horton P, Park K-J, Obayashi T, Nakai K.Protein subcellular localization prediction with WoLF PSORT. Proceedings of the 4th Annual Asia Pacific Bioinformatics Conference APBC06, Taipei, Taiwan; 2006. pp 39-48.
    • Horton P, Park K-J, Obayashi T, Nakai K.Protein subcellular localization prediction with WoLF PSORT. Proceedings of the 4th Annual Asia Pacific Bioinformatics Conference APBC06, Taipei, Taiwan; 2006. pp 39-48.
  • 44
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J Mol Biol 2000;300:1005-1016.
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 45
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG, Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 1996;241:779-786.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 46
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamin diphosphate dependent enzyme, at 2.5 Å resolution
    • Lindqvist Y, Schneider G, Ermler U, Sundstrom M. Three-dimensional structure of transketolase, a thiamin diphosphate dependent enzyme, at 2.5 Å resolution. EMBO J 1992;11:2373-2379.
    • (1992) EMBO J , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 47
    • 0026615820 scopus 로고
    • 2) biosynthesis: Evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and α-ketoglutarate decarboxylase activities
    • 2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and α-ketoglutarate decarboxylase activities. J Bacteriol 1992;174:8111-8118.
    • (1992) J Bacteriol , vol.174 , pp. 8111-8118
    • Palaniappan, C.1    Sharma, V.2    Hudspeth, M.E.S.3    Meganathan, R.4
  • 49
    • 3543034577 scopus 로고    scopus 로고
    • Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain α-keto acid decarboxylase/ dehydrogenase
    • Li J, Wynn RM, Machius M, Chuang JL, Karthikeyan S, Tomchick DR, Chuang DT. Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain α-keto acid decarboxylase/ dehydrogenase. J Biol Chem 2004;279:32968-32978.
    • (2004) J Biol Chem , vol.279 , pp. 32968-32978
    • Li, J.1    Wynn, R.M.2    Machius, M.3    Chuang, J.L.4    Karthikeyan, S.5    Tomchick, D.R.6    Chuang, D.T.7
  • 51
    • 0038470825 scopus 로고    scopus 로고
    • 2) El component of 2-oxo acid dehydrogenase multienzyme complexes
    • 2) El component of 2-oxo acid dehydrogenase multienzyme complexes. Biochemistry 2003;42:6996-7002.
    • (2003) Biochemistry , vol.42 , pp. 6996-7002
    • Fries, M.1    Jung, H.-I.2    Perham, R.N.3
  • 52
    • 0035830937 scopus 로고    scopus 로고
    • + ion-binding site residues in human mitochondrial branched-chain α-keto acid decarboxylase/dehydrogenase
    • + ion-binding site residues in human mitochondrial branched-chain α-keto acid decarboxylase/dehydrogenase. J Biol Chem 2001;276:4168-4174.
    • (2001) J Biol Chem , vol.276 , pp. 4168-4174
    • Wynn, R.M.1    Ho, R.2    Chuang, J.L.3    Chuang, D.T.4
  • 53
    • 0008584183 scopus 로고    scopus 로고
    • Study of 2-oxoglutarate dehydrogenase by the method of chemical modification of amino acid residues
    • Kurganov BI, Nagradova NK, Lavrik OI, editors, New York: Nova Science;
    • Bunik VI, Gomazkova VS. Study of 2-oxoglutarate dehydrogenase by the method of chemical modification of amino acid residues. In: Kurganov BI, Nagradova NK, Lavrik OI, editors. Chemical modification of enzymes. New York: Nova Science; 1996. pp 479-521.
    • (1996) Chemical modification of enzymes , pp. 479-521
    • Bunik, V.I.1    Gomazkova, V.S.2
  • 54
    • 0031218739 scopus 로고    scopus 로고
    • Inactivation of alpha-ketoglutarate dehydrogenase during its enzymatic reaction
    • Bunik VI, Pavlova OG. Inactivation of alpha-ketoglutarate dehydrogenase during its enzymatic reaction. Biochemistry (Mosc) 1997;62:973-982.
    • (1997) Biochemistry (Mosc) , vol.62 , pp. 973-982
    • Bunik, V.I.1    Pavlova, O.G.2
  • 55
    • 7444244483 scopus 로고    scopus 로고
    • A molecular switch and proton wire synchronize the active sites in thiamine enzymes
    • Frank RAW, Titman CM, Pratap JV, Luisi BF, Perham RN. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science 2004;306:872-876.
    • (2004) Science , vol.306 , pp. 872-876
    • Frank, R.A.W.1    Titman, C.M.2    Pratap, J.V.3    Luisi, B.F.4    Perham, R.N.5
  • 56
    • 0033918381 scopus 로고    scopus 로고
    • Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for the formation of a precatalytic complex
    • Bunik VI, Westphal AH, DeKok A. Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for the formation of a precatalytic complex Eur J Biochem 2000;267:3583-3591.
    • (2000) Eur J Biochem , vol.267 , pp. 3583-3591
    • Bunik, V.I.1    Westphal, A.H.2    DeKok, A.3
  • 57
    • 0020841382 scopus 로고
    • Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in Bacillus subtilis
    • Lowe PN, Hodgson JA, Perham RN. Dual role of a single multienzyme complex in the oxidative decarboxylation of pyruvate and branched-chain 2-oxo acids in Bacillus subtilis. Biochem J 1983;215:133-140.
    • (1983) Biochem J , vol.215 , pp. 133-140
    • Lowe, P.N.1    Hodgson, J.A.2    Perham, R.N.3
  • 58
    • 0025372107 scopus 로고
    • Cloning and sequence analysis of the genes encoding the A and B subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Hawkins CF, Borges A, Perham RN. Cloning and sequence analysis of the genes encoding the A and B subunits of the E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Eur J Biochem 1990;191:337-346.
    • (1990) Eur J Biochem , vol.191 , pp. 337-346
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 59
    • 0025160796 scopus 로고
    • Secretory S complex of Bacillus subtilis: Sequence analysis and identity to pyruvate dehydrogenase
    • Hemilä H, Palva A, Paulin L, Arvidson S, Palva I. Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase. J Bacteriol 1993;172:5052-5063.
    • (1993) J Bacteriol , vol.172 , pp. 5052-5063
    • Hemilä, H.1    Palva, A.2    Paulin, L.3    Arvidson, S.4    Palva, I.5
  • 60
    • 0037168586 scopus 로고    scopus 로고
    • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA. Mammalian Gene Collection Program Team. Generation and ini
    • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA. Mammalian Gene Collection Program Team. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci USA 2002;99:16899-16903.
  • 61
    • 9144252038 scopus 로고    scopus 로고
    • Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H
    • Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S. Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet 2004;36:40-45.
  • 62
    • 0033615363 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new c DNA clones from brain which code for large proteins in vitro
    • Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O. Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new c DNA clones from brain which code for large proteins in vitro. DNA Res 1999;6:337-345.
    • (1999) DNA Res , vol.6 , pp. 337-345
    • Nagase, T.1    Ishikawa, K.2    Kikuno, R.3    Hirosawa, M.4    Nomura, N.5    Ohara, O.6
  • 63
    • 0034738923 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new c DNA clones from brain which code for large proteins in vitro
    • Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O. Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new c DNA clones from brain which code for large proteins in vitro. DNA Res 2000;7:273-281.
    • (2000) DNA Res , vol.7 , pp. 273-281
    • Nagase, T.1    Kikuno, R.2    Nakayama, M.3    Hirosawa, M.4    Ohara, O.5
  • 64
    • 0028351616 scopus 로고
    • Localization of the gene (OGDH) coding for the E1k component of the alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
    • Szabo P, Cai X, Ali G, Blass JP. Localization of the gene (OGDH) coding for the E1k component of the alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2. Genomics 1994;20:324-326.
    • (1994) Genomics , vol.20 , pp. 324-326
    • Szabo, P.1    Cai, X.2    Ali, G.3    Blass, J.P.4
  • 65
    • 0035852328 scopus 로고    scopus 로고
    • Prediction of organellar targeting signals
    • Emanuelsson O, von Heijne G. Prediction of organellar targeting signals. Biochim Biophys Acta 2001;1541:114-119.
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 114-119
    • Emanuelsson, O.1    von Heijne, G.2
  • 66
    • 0019890086 scopus 로고
    • Regulation of bovine kidney alpha-ketoglutarate dehydrogenase complex by calcium ion and adenine nucleotides. Effects on S0.5 for alpha-ketoglutarate
    • Lawlis VB, Roche TE. Regulation of bovine kidney alpha-ketoglutarate dehydrogenase complex by calcium ion and adenine nucleotides. Effects on S0.5 for alpha-ketoglutarate. Biochemistry 1981;20:2512-2518.
    • (1981) Biochemistry , vol.20 , pp. 2512-2518
    • Lawlis, V.B.1    Roche, T.E.2
  • 67
    • 0019890079 scopus 로고
    • Inhibition of bovine kidney alpha-ketoglutarate dehydrogenase complex by reduced nicotinamide adenine dinucleotide in the presence or absence of calcium ion and effect of adenosine 5′-diphosphate on reduced nicotinamide adenine dinucleotide inhibition
    • Lawlis VB, Roche TE. Inhibition of bovine kidney alpha-ketoglutarate dehydrogenase complex by reduced nicotinamide adenine dinucleotide in the presence or absence of calcium ion and effect of adenosine 5′-diphosphate on reduced nicotinamide adenine dinucleotide inhibition. Biochemistry 1981;20:2519-2524.
    • (1981) Biochemistry , vol.20 , pp. 2519-2524
    • Lawlis, V.B.1    Roche, T.E.2
  • 68
    • 0024855185 scopus 로고
    • 2+ in the hormonal regulation of the activities of pyruvate dehydrogenase and oxoglutarate dehydrogenase complexes
    • 2+ in the hormonal regulation of the activities of pyruvate dehydrogenase and oxoglutarate dehydrogenase complexes. Ann NY Acad Sci 1989;573:206-217.
    • (1989) Ann NY Acad Sci , vol.573 , pp. 206-217
    • Rutter, G.A.1    McCormack, J.G.2    Midgley, P.J.W.3    Denton, R.M.4
  • 69
    • 5144226338 scopus 로고    scopus 로고
    • The DxDxDG motif for calcium binding: Multiple structural contexts and implications for evolution
    • Rigden DJ, Galperin MY. The DxDxDG motif for calcium binding: multiple structural contexts and implications for evolution. J Mol Biol 2004;343:971-984.
    • (2004) J Mol Biol , vol.343 , pp. 971-984
    • Rigden, D.J.1    Galperin, M.Y.2
  • 70
    • 0032508722 scopus 로고    scopus 로고
    • Subunit interactions in the mammalian α-ketoglutarate dehydrogenase complex: Evidence for direct association of the α-ketoglutarate dehydrogenase (E1) and dihydrolipoamide dehydrogenase (E3) components
    • McCartney RG, Rice JE, Sanderson S, Bunik VI, Lindsay H, Lindsay JG. Subunit interactions in the mammalian α-ketoglutarate dehydrogenase complex: evidence for direct association of the α-ketoglutarate dehydrogenase (E1) and dihydrolipoamide dehydrogenase (E3) components. J Biol Chem 1998;273:24158-24164.
    • (1998) J Biol Chem , vol.273 , pp. 24158-24164
    • McCartney, R.G.1    Rice, J.E.2    Sanderson, S.3    Bunik, V.I.4    Lindsay, H.5    Lindsay, J.G.6
  • 71
    • 0037014599 scopus 로고    scopus 로고
    • Identification of the E2-binding residues in the N-terminal domain of E1 of a prokaryotic pyruvate dehydrogenase complex
    • Hengeveld AF, de Kok A. Identification of the E2-binding residues in the N-terminal domain of E1 of a prokaryotic pyruvate dehydrogenase complex. FEBS Lett 2002;522:173-176.
    • (2002) FEBS Lett , vol.522 , pp. 173-176
    • Hengeveld, A.F.1    de Kok, A.2
  • 72
    • 8344289722 scopus 로고    scopus 로고
    • Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit
    • Park YH, Wei W, Zhou L, Nemeria N, Jordan F. Amino-terminal residues 1-45 of the Escherichia coli pyruvate dehydrogenase complex E1 subunit interact with the E2 subunit and are required for activity of the complex but not for reductive acetylation of the E2 subunit. Biochemistry 2004;43:14037-14046.
    • (2004) Biochemistry , vol.43 , pp. 14037-14046
    • Park, Y.H.1    Wei, W.2    Zhou, L.3    Nemeria, N.4    Jordan, F.5
  • 73
    • 0025024108 scopus 로고    scopus 로고
    • Bunik VI, Buneeva OA, Gomazkova VS. Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH. FEBS Lett 1990;269:252-254.
    • Bunik VI, Buneeva OA, Gomazkova VS. Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH. FEBS Lett 1990;269:252-254.
  • 74
    • 0032573506 scopus 로고    scopus 로고
    • Cooperativity and flexibility of active sites in homodimeric transketolase
    • Kovina MV, Kochetov GA. Cooperativity and flexibility of active sites in homodimeric transketolase. FEBS Lett 1998;440:81-84.
    • (1998) FEBS Lett , vol.440 , pp. 81-84
    • Kovina, M.V.1    Kochetov, G.A.2
  • 75
    • 26644459701 scopus 로고    scopus 로고
    • Multiple modes of active center communication in thiamin diphosphate-dependent enzymes
    • Jordan F, Nemeria NS, Sergienko E. Multiple modes of active center communication in thiamin diphosphate-dependent enzymes. Acc Chem Res 2005;38:755-763.
    • (2005) Acc Chem Res , vol.38 , pp. 755-763
    • Jordan, F.1    Nemeria, N.S.2    Sergienko, E.3
  • 76
    • 0032516465 scopus 로고    scopus 로고
    • The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
    • Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D. The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry 1998;37:9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Muscate, A.2    McLeish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 77
    • 0034533110 scopus 로고    scopus 로고
    • Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis
    • Chauhan HJ, Domingo GJ, Jung H-I, Perham RN. Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis. Eur J Biochem 2000;267:7158-7169.
    • (2000) Eur J Biochem , vol.267 , pp. 7158-7169
    • Chauhan, H.J.1    Domingo, G.J.2    Jung, H.-I.3    Perham, R.N.4
  • 78
    • 0024952220 scopus 로고
    • Organization and functioning of muscle pyruvate dehydrogenase active centers
    • Khailova LS, Korochkina LG, Severin SE. Organization and functioning of muscle pyruvate dehydrogenase active centers. Ann NY Acad Sci 1989;573:36-54.
    • (1989) Ann NY Acad Sci , vol.573 , pp. 36-54
    • Khailova, L.S.1    Korochkina, L.G.2    Severin, S.E.3
  • 79
    • 0018355912 scopus 로고
    • Purification and characterization of branched-chain α-ketoacid dehydrogenase from bovine liver mitochondria
    • Danner DJ, Lemmon SK, Besharse JC, Elsas LJ, II. Purification and characterization of branched-chain α-ketoacid dehydrogenase from bovine liver mitochondria. J Biol Chem 1979;254:5522-5526.
    • (1979) J Biol Chem , vol.254 , pp. 5522-5526
    • Danner, D.J.1    Lemmon, S.K.2    Besharse, J.C.3    Elsas II, L.J.4
  • 80
    • 0019785027 scopus 로고
    • Purification of branched-chain α-ketoacid dehydrogenase complex from Pseudomonas putida
    • Sokatch JR, McCully V, Roberts CM. Purification of branched-chain α-ketoacid dehydrogenase complex from Pseudomonas putida. J Bacteriol 1981;148:647-652.
    • (1981) J Bacteriol , vol.148 , pp. 647-652
    • Sokatch, J.R.1    McCully, V.2    Roberts, C.M.3
  • 81
    • 0022647559 scopus 로고
    • Resolution of branched-chain oxo acid dehydrogenase complex of Pseudomonas aeruginosa PAO
    • McCully V, Burns G, Sokatch JR. Resolution of branched-chain oxo acid dehydrogenase complex of Pseudomonas aeruginosa PAO. Biochem J 1986;233:737-742.
    • (1986) Biochem J , vol.233 , pp. 737-742
    • McCully, V.1    Burns, G.2    Sokatch, J.R.3
  • 82
    • 0019511136 scopus 로고
    • Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli
    • Bisswanger H. Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli. J Biol Chem 1981;256:815-822.
    • (1981) J Biol Chem , vol.256 , pp. 815-822
    • Bisswanger, H.1
  • 83
    • 33646859093 scopus 로고    scopus 로고
    • A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct
    • Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. J Biol Chem 2006;281:15296-15303.
    • (2006) J Biol Chem , vol.281 , pp. 15296-15303
    • Arjunan, P.1    Sax, M.2    Brunskill, A.3    Chandrasekhar, K.4    Nemeria, N.5    Zhang, S.6    Jordan, F.7    Furey, W.8
  • 84
    • 23444459343 scopus 로고    scopus 로고
    • The molecular origins of specificity in the assembly of a multienzyme complex
    • Frank RA, Pratap JV, Pei XY, Perham RN, Luisi BF. The molecular origins of specificity in the assembly of a multienzyme complex. Structure 2005;13:1119-1130.
    • (2005) Structure , vol.13 , pp. 1119-1130
    • Frank, R.A.1    Pratap, J.V.2    Pei, X.Y.3    Perham, R.N.4    Luisi, B.F.5
  • 85
    • 0007644072 scopus 로고    scopus 로고
    • Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus
    • Domingo GJ, Chauhan HJ, Lessard IA, Fuller C, Perham RN. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. Eur J Biochem 1999;266:1136-1146.
    • (1999) Eur J Biochem , vol.266 , pp. 1136-1146
    • Domingo, G.J.1    Chauhan, H.J.2    Lessard, I.A.3    Fuller, C.4    Perham, R.N.5
  • 86
    • 0025991224 scopus 로고
    • Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site
    • Nakano K, Matuda S, Yamanaka T, Tsubouchi H, Nakagawa S, Titani K, Ohta S, Miyata T. Purification and molecular cloning of succinyltransferase of the rat alpha-ketoglutarate dehydrogenase complex. Absence of a sequence motif of the putative E3 and/or E1 binding site. J Biol Chem 1991;266:19013-19017.
    • (1991) J Biol Chem , vol.266 , pp. 19013-19017
    • Nakano, K.1    Matuda, S.2    Yamanaka, T.3    Tsubouchi, H.4    Nakagawa, S.5    Titani, K.6    Ohta, S.7    Miyata, T.8
  • 88
    • 0016411063 scopus 로고
    • DL-2-keto-4-hydroxyglutarate-1
    • Maitra U, Dekker EE. DL-2-keto-4-hydroxyglutarate-1. Methods Enzymol 1975;41:115-118.
    • (1975) Methods Enzymol , vol.41 , pp. 115-118
    • Maitra, U.1    Dekker, E.E.2
  • 89
    • 41149092650 scopus 로고
    • The inhibition of several tricarboxylic acid cycle enzymes by gamma-hydroxy-alpha-ketoglutarate
    • Payes B, Laties GG. The inhibition of several tricarboxylic acid cycle enzymes by gamma-hydroxy-alpha-ketoglutarate. Biochem Biophys Res Commun 1963;10:460-466.
    • (1963) Biochem Biophys Res Commun , vol.10 , pp. 460-466
    • Payes, B.1    Laties, G.G.2
  • 90
    • 0019320683 scopus 로고
    • Evidence for the identity and some comparative properties of α-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity
    • Gupta SC, Dekker EE. Evidence for the identity and some comparative properties of α-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity. J Biol Chem 1980;255:1107-1112.
    • (1980) J Biol Chem , vol.255 , pp. 1107-1112
    • Gupta, S.C.1    Dekker, E.E.2
  • 92
  • 93
    • 0023655551 scopus 로고
    • Formation and utilization of acetoin, an unusual product of pyruvate metabolism by Ehrlich and AS30-D tumor mitochondria
    • Baggetto LG, Lehninger AL. Formation and utilization of acetoin, an unusual product of pyruvate metabolism by Ehrlich and AS30-D tumor mitochondria. J Biol Chem 1987;262:9535-9541.
    • (1987) J Biol Chem , vol.262 , pp. 9535-9541
    • Baggetto, L.G.1    Lehninger, A.L.2


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