메뉴 건너뛰기




Volumn 3, Issue 3, 2009, Pages 279-290

Regulation of catalysis within cellular network: Metabolic and signaling implications of the 2-oxoglutarate oxidative decarboxylation

Author keywords

2 oxoglutarate dehydrogenase; Lipoic acid; Multienzyme complex; Neurodegeneration; Phosphorylation potential; Redox regulation; Thiamine deficiency; Tricarboxylic acid cycle

Indexed keywords

2 OXOGLUTARIC ACID; ADENINE NUCLEOTIDE; CALCIUM ION; COCARBOXYLASE; COENZYME A; MAGNESIUM ION; MANGANESE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXOGLUTARATE DEHYDROGENASE; PHOSPHATE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SUCCINYL COENZYME A; THIOCTIC ACID; THIOPHENE; THIOREDOXIN;

EID: 70449650368     PISSN: 18723136     EISSN: None     Source Type: Journal    
DOI: 10.2174/187231309789054904     Document Type: Review
Times cited : (20)

References (126)
  • 2
    • 1842665662 scopus 로고    scopus 로고
    • Mitochondrial signaling: The retrograde response
    • Butow RA, Avadhani NG. Mitochondrial signaling: the retrograde response. Mol Cell 2004; 14: 1-15.
    • (2004) Mol Cell , vol.14 , pp. 1-15
    • Butow, R.A.1    Avadhani, N.G.2
  • 4
    • 33747345950 scopus 로고    scopus 로고
    • Studying the Signaling Role of 2-Oxoglutaric Acid Using Analogs that Mimic the Ketone and Ketal Forms of 2-Oxoglutaric Acid
    • DOI 10.1016/j.chembiol.2006.06.009, PII S1074552106002195
    • Chen H, Laurent S, Bédu S, et al. Studying the signaling role of 2-oxoglutaric acid using analogs that mimic the ketone and ketal forms of 2-oxoglutaric acid. Chem Biol 2006; 13: 849-856 (Pubitemid 44247775)
    • (2006) Chemistry and Biology , vol.13 , Issue.8 , pp. 849-856
    • Chen, H.1    Laurent, S.2    Bedu, S.3    Ziarelli, F.4    Chen, H.-L.5    Cheng, Y.6    Zhang, C.-C.7    Peng, L.8
  • 5
    • 33645232465 scopus 로고    scopus 로고
    • The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate kinase
    • Chen YM, Ferrar TS, Lohmeier-Vogel EM, et al. The PII signal transduction protein of Arabidopsis thaliana forms an arginine-regulated complex with plastid N-acetyl glutamate kinase. J Biol Chem 2006; 281: 5726-5733
    • (2006) J Biol Chem , vol.281 , pp. 5726-5733
    • Chen, Y.M.1    Ferrar, T.S.2    Lohmeier-Vogel, E.M.3
  • 6
    • 33749259102 scopus 로고    scopus 로고
    • 2-Oxoglutarate downregulates expression of vascular endothelial growth factor and erythropoietin through decreasing hypoxia-inducible factor-1alpha and inhibits angiogenesis
    • DOI 10.1002/jcp.20733
    • Matsumoto K, Imagawa S, Obara N, et al. 2-Oxoglutarate downregulates expression of vascular endothelial growth factor and erythropoietin through decreasing hypoxia-inducible factor-1alpha and inhibits angiogenesis. J Cell Physiol 2006; 209: 333-340 (Pubitemid 44484623)
    • (2006) Journal of Cellular Physiology , vol.209 , Issue.2 , pp. 333-340
    • Matsumoto, K.1    Imagawa, S.2    Obara, N.3    Suzuki, N.4    Takahashi, S.5    Nagasawa, T.6    Yamamoto, M.7
  • 7
    • 1542288938 scopus 로고    scopus 로고
    • Global organization of metabolic fluxes in the bacterium Escherichia coli
    • Almaas E, Kovacs B, Vicsek T, Oltvai ZN, Barabasi AL. Global organization of metabolic fluxes in the bacterium Escherichia coli. Nature 2004; 427: 839-843
    • (2004) Nature , vol.427 , pp. 839-843
    • Almaas, E.1    Kovacs, B.2    Vicsek, T.3    Oltvai, Z.N.4    Barabasi, A.L.5
  • 9
    • 57749098561 scopus 로고    scopus 로고
    • Inhibition of 2-oxoglutarate dehydrogenase in potato tuber suggests the enzyme is limiting for respiration and confirms its importance in nitrogen assimilation
    • DOI 10.1104/pp.108.126219
    • Araujo WL, Nunes-Nesi A, Trenkamp S, Bunik VI, Fernie AR. Inhibition of 2-oxoglutarate dehydrogenase in potato tuber suggests the enzyme is limiting for respiration and confirms its importance in nitrogen assimilation. Plant Physiol 2008; 148: 1782-1796 (Pubitemid 352847455)
    • (2008) Plant Physiology , vol.148 , Issue.4 , pp. 1782-1796
    • Araujo, W.L.1    Nunes-Nesi, A.2    Trenkamp, S.3    Bunik, V.I.4    Fernie, A.R.5
  • 11
    • 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. (Pubitemid 41271193)
    • (2005) Molecular Neurobiology , vol.31 , Issue.1-3 , pp. 43-63
    • Gibson, G.E.1    Blass, J.P.2    Beal, M.F.3    Bunik, V.4
  • 12
    • 0034104813 scopus 로고    scopus 로고
    • 2-Ketoglutarate dehydrogenase deficiency with intermittent 2-ketoglutaric aciduria
    • DOI 10.1055/s-2000-15295
    • Dunckelmann RJ, Ebinger F, Schulze A, Wanders RJA, Rating D, Mayatepek E. 2-Ketoglutarate dehydrogenase deficiency with intermittent 2-ketoglutaric aciduria. Neuropediatrics 2000; 31: 35-38 (Pubitemid 30172984)
    • (2000) Neuropediatrics , vol.31 , Issue.1 , pp. 35-38
    • Dunckelmann, R.J.1    Ebinger, F.2    Schulze, A.3    Wanders, R.J.A.4    Rating, D.5    Mayatepek, E.6
  • 13
    • 63149092201 scopus 로고    scopus 로고
    • Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons
    • Kabysheva MS, Storozhevykh TP, Pinelis VG, Bunik VI. Synthetic regulators of the 2-oxoglutarate oxidative decarboxylation alleviate the glutamate excitotoxicity in cerebellar granule neurons. Biochem Pharmacol 2009; 77: 1531-1540
    • (2009) Biochem Pharmacol , vol.77 , pp. 1531-1540
    • Kabysheva, M.S.1    Storozhevykh, T.P.2    Pinelis, V.G.3    Bunik, V.I.4
  • 14
    • 69149103056 scopus 로고    scopus 로고
    • Phosphono analogs of 2-oxoglutarate protect cerebellar granule neurons upon glutamate excitotoxicity
    • in the press, MS ID 550034-1405258
    • Bunik VI, Kabysheva MS, Klimuk EI, Storozhevykh TP, Pinelis VG. Phosphono analogs of 2-oxoglutarate protect cerebellar granule neurons upon glutamate excitotoxicity. Ann NY Acad Sci 2009; in the press, MS ID 550034-1405258
    • (2009) Ann NY Acad Sci
    • Bunik, V.I.1    Kabysheva, M.S.2    Klimuk, E.I.3    Storozhevykh, T.P.4    Pinelis, V.G.5
  • 16
    • 52449084258 scopus 로고    scopus 로고
    • (2008) Novel isoform of 2-oxogluratate dehydrogenase is identified in brain, but not in heart
    • Bunik V, Kaehne T, Degtyarev D, Shcherbakova T, Reiser G. (2008) Novel isoform of 2-oxogluratate dehydrogenase is identified in brain, but not in heart. FEBS J 2008; 275: 4990-5006.
    • (2008) FEBS J , vol.275 , pp. 4990-5006
    • Bunik, V.1    Kaehne, T.2    Degtyarev, D.3    Shcherbakova, T.4    Reiser, G.5
  • 17
    • 0021451569 scopus 로고
    • Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase
    • Spencer ME, Darlison MG, Stephens PE, Duckenfield IK, Guest JR. Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. Eur J Biochem 1984; 141: 361-374
    • (1984) Eur J Biochem , vol.141 , pp. 361-374
    • Spencer, M.E.1    Darlison, M.G.2    Stephens, P.E.3    Duckenfield, I.K.4    Guest, J.R.5
  • 18
    • 0024387073 scopus 로고
    • Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively
    • Carlsson P, Hederstedt L. Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively. J Bacteriol 1989; 171: 3667-3672
    • (1989) J Bacteriol , vol.171 , pp. 3667-3672
    • Carlsson, P.1    Hederstedt, L.2
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0025345741 scopus 로고
    • Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase
    • Repetto B, Tzagoloff A. Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase. Mol Cell Biol 1990; 10: 4221-4232 (Pubitemid 20227306)
    • (1990) Molecular and Cellular Biology , vol.10 , Issue.8 , pp. 4221-4232
    • Repetto, B.1    Tzagoloff, A.2
  • 22
    • 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
  • 23
    • 0027935643 scopus 로고
    • Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex
    • DOI 10.1111/j.1432-1033.1994.tb20010.x
    • Nakano K, Takase C, Sakamoto T, et al. Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur J Biochem 1994; 224: 179-189 (Pubitemid 24267120)
    • (1994) European Journal of Biochemistry , vol.224 , Issue.1 , pp. 179-189
    • Nakano, K.1    Takase, C.2    Sakamoto, T.3    Nakagawa, S.4    Inazawa, J.5    Ohta, S.6    Matuda, S.7
  • 24
    • 0034925982 scopus 로고    scopus 로고
    • Human dihydrolipoamide dehydrogenase gene transcription is mediated by cAMP-response element-like site and TACGAC direct repeat
    • DOI 10.1016/S1357-2725(01)00061-9, PII S1357272501000619
    • Yang HS, Morris JI, Wang Q, Korotchkina LG, Kwon M, Patel MS. Human dihydrolipoamide dehydrogenase gene transcription is mediated by cAMP-response element-like site and TACGAC direct repeat. Int J Biochem Cell Biol 2001; 33: 902-913 (Pubitemid 32667498)
    • (2001) International Journal of Biochemistry and Cell Biology , vol.33 , Issue.9 , pp. 902-913
    • Yang, H.-S.1    Morris, J.I.2    Wang, Q.3    Korotchkina, L.G.4    Kwon, M.5    Patel, M.S.6
  • 26
    • 33744471646 scopus 로고    scopus 로고
    • Changes in the rat heart proteome induced by exercise training: Increased abundance of heat shock protein hsp20
    • DOI 10.1002/pmic.200401356
    • Boluyt MO, Brevick JL, Rogers DS, Randall MJ, Scalia AF, Li ZB. Changes in the rat heart proteome induced by exercise training: increased abundance of heat shock protein hsp20. Proteomics 2006; 6: 3154-3169 (Pubitemid 43806411)
    • (2006) Proteomics , vol.6 , Issue.10 , pp. 3154-3169
    • Boluyt, M.O.1    Brevick, J.L.2    Rogers, D.S.3    Randall, M.J.4    Scalia, A.F.5    Li, Z.B.6
  • 27
    • 33845440787 scopus 로고    scopus 로고
    • Proteomic identification of altered proteins in skeletal muscle during chronic potassium depletion: Implications for hypokalemic myopathy
    • DOI 10.1021/pr060136h
    • Thongboonkerd V, Kanlaya R, Sinchaikul S, Parichatikanond P, Chen ST, Malasit P. Proteomic identification of altered proteins in skeletal muscle during chronic potassium depletion: implications for hypokalemic myopathy. J Proteome Res 2006; 5: 3326-3335 (Pubitemid 44904324)
    • (2006) Journal of Proteome Research , vol.5 , Issue.12 , pp. 3326-3335
    • Thongboonkerd, V.1    Kanlaya, R.2    Sinchaikul, S.3    Parichatikanond, P.4    Chen, S.-T.5    Malasit, P.6
  • 28
    • 17644381300 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12: Effects of oxygen availability and ArcA
    • Salmon KA, Hung SP, Steffen NR, et al. Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA. J Biol Chem 2005; 280: 15084-15096
    • (2005) J Biol Chem , vol.280 , pp. 15084-15096
    • Salmon, K.A.1    Hung, S.P.2    Steffen, N.R.3
  • 29
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft V, Eubel H, Jänsch L, Werhahn W, Braun HP. Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol 2001; 127: 1694-1710
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jänsch, L.3    Werhahn, W.4    Braun, H.P.5
  • 30
    • 0033918381 scopus 로고    scopus 로고
    • Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate
    • Bunik V, Westphal AH, de Kok A. Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate. Eur J Biochem 2000; 267: 3583-3591
    • (2000) Eur J Biochem , vol.267 , pp. 3583-3591
    • Bunik, V.1    Westphal, A.H.2    De Kok, A.3
  • 31
    • 22444440271 scopus 로고
    • Regulation of α-ketoglutarate dehydrogenase activity in Acinetobacter
    • Weitzman PDJ. Regulation of α-ketoglutarate dehydrogenase activity in Acinetobacter. FEBS Lett 1972; 22: 323-326
    • (1972) FEBS Lett , vol.22 , pp. 323-326
    • Weitzman, P.D.J.1
  • 32
    • 0017859430 scopus 로고
    • Regulatory properties of the α- Ketoglutarate dehydrogenase complex of Acetobacter xylinum
    • Kornfeld S, Benziman M, Milner Y. Regulatory properties of the α- ketoglutarate dehydrogenase complex of Acetobacter xylinum. J Biol Chem 1978; 253: 5678-5684
    • (1978) J Biol Chem , vol.253 , pp. 5678-5684
    • Kornfeld, S.1    Benziman, M.2    Milner, Y.3
  • 33
    • 0015239349 scopus 로고
    • Nucleotide activation of cauliflower ketoglutarate dehydrogenase
    • Wedding RT, Black MK. Nucleotide activation of cauliflower ketoglutarate dehydrogenase. J Biol Chem 1971; 246: 1638-1643
    • (1971) J Biol Chem , vol.246 , pp. 1638-1643
    • Wedding, R.T.1    Black, M.K.2
  • 34
    • 0015523255 scopus 로고
    • Mammalian α-keto acid dehydrogenase complexes. VII. Resolution and reconstitution of the pig heart 2-oxoglutarate dehydrogenase complex
    • Tanaka N, Koike K, Hamada M, Otsuka KI, Suematsu T, Koike M. Mammalian α-keto acid dehydrogenase complexes. VII. Resolution and reconstitution of the pig heart 2-oxoglutarate dehydrogenase complex. J Biol Chem 1972; 247: 4043-4049
    • (1972) J Biol Chem , vol.247 , pp. 4043-4049
    • Tanaka, N.1    Koike, K.2    Hamada, M.3    Otsuka, K.I.4    Suematsu, T.5    Koike, M.6
  • 35
    • 0019740081 scopus 로고
    • 2-Oxoglutarate dehydrogenase complex from bovine-adrenal-cortex mitochondria. Purification and partial characterization
    • Strumilo SA, Taranda NI, Senkevich SB, Vinogradov VV. 2-Oxoglutarate dehydrogenase complex from bovine-adrenal-cortex mitochondria. Purification and partial characterization. Acta Biol Med Germ 1981; 40: 257-264
    • (1981) Acta Biol Med Germ , vol.40 , pp. 257-264
    • Strumilo, S.A.1    Taranda, N.I.2    Senkevich, S.B.3    Vinogradov, V.V.4
  • 36
    • 0016254851 scopus 로고
    • Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase
    • Koike K, Hamada M, Tanaka N, Otsuka K, Ogasahara K, Koike M. Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase. J Biol Chem 1974; 249: 3836-3842
    • (1974) J Biol Chem , vol.249 , pp. 3836-3842
    • Koike, K.1    Hamada, M.2    Tanaka, N.3    Otsuka, K.4    Ogasahara, K.5    Koike, M.6
  • 37
    • 70449677973 scopus 로고
    • Investigation of the interaction of thiamine pyrophosphate with muscle α-ketoglutarate dehydrogenase
    • Gomazkova VS, Stafeeva OA, Laufer AI, Severin SE. Investigation of the interaction of thiamine pyrophosphate with muscle α-ketoglutarate dehydrogenase. Dokl AN USSR 1981; 259: 477-480
    • (1981) Dokl AN USSR , vol.259 , pp. 477-480
    • Gomazkova, V.S.1    Stafeeva, O.A.2    Laufer, A.I.3    Severin, S.E.4
  • 38
    • 0032573506 scopus 로고    scopus 로고
    • Cooperativity and flexibility of active sites in homodimeric transketolase
    • DOI 10.1016/S0014-5793(98)01423-9, PII S0014579398014239
    • Kovina MV, Kochetov GA. Cooperativity and flexibility of active sites in homodimeric transketolase. FEBS Lett 1998; 440: 81-84 (Pubitemid 28558740)
    • (1998) FEBS Letters , vol.440 , Issue.1-2 , pp. 81-84
    • Kovina, M.V.1    Kochetov, G.A.2
  • 39
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase
    • DOI 10.1074/jbc.M300339200
    • 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 (Pubitemid 36806439)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 21240-21246
    • Ciszak, E.M.1    Korotchkina, L.G.2    Dominiak, P.M.3    Sidhu, S.4    Patel, M.S.5
  • 40
    • 7444244483 scopus 로고    scopus 로고
    • A molecular switch and proton wire synchronize the active sites in thiamine enzymes
    • Frank, RA, 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.1    Titman, C.M.2    Pratap, J.V.3    Luisi, B.F.4    Perham, R.N.5
  • 41
    • 0025024108 scopus 로고
    • Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH
    • DOI 10.1016/0014-5793(90)81166-L
    • Bunik VI, Buneeva OA, Gomazkova VS. Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH. FEBS Lett 1990; 269: 252-254 (Pubitemid 20245364)
    • (1990) FEBS Letters , vol.269 , Issue.1 , pp. 252-254
    • Bunik, V.I.1    Buneeva, O.A.2    Gomazkova, V.S.3
  • 42
    • 0029550761 scopus 로고
    • Thiamine pyrophosphate as an effector of 2-oxoglutarate dehydrogenase complex from European bison heart
    • Strumilo S, Markiewicz J. Thiamine pyrophosphate as an effector of 2-oxoglutarate dehydrogenase complex from European bison heart. Biochem Mol Biol Int 1995; 37: 101-106 (Pubitemid 26177882)
    • (1995) Biochemistry and Molecular Biology International , vol.37 , Issue.1 , pp. 101-106
    • Strumilo, S.1    Markiewicz, J.2
  • 43
    • 34047185249 scopus 로고    scopus 로고
    • Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
    • Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J Mol Biol 2007; 368: 639-651
    • (2007) J Mol Biol , vol.368 , pp. 639-651
    • Frank, R.A.1    Price, A.J.2    Northrop, F.D.3    Perham, R.N.4    Luisi, B.F.5
  • 44
    • 0037009346 scopus 로고    scopus 로고
    • Kinetic and spectral investigation of allosteric interaction of coenzymes with 2-oxo acid dehydrogenase complexes
    • DOI 10.1016/S0022-2860(02)00255-7, PII S0022286002002557
    • Strumilo S, Czygier M, Kondracikowska J, Dobrzyn P, Czerniecki J. Kinetic and spectral investigation of allosteric interaction of coenzymes with 2-oxo acid dehydrogenase complexes. J Mol Struct 2002; 614: 221-226 (Pubitemid 34987731)
    • (2002) Journal of Molecular Structure , vol.614 , Issue.1-3 , pp. 221-226
    • Strumilo, S.1    Czygier, M.2    Kondracikowska, J.3    Dobrzyn, P.4    Czerniecki, J.5
  • 46
    • 61549133968 scopus 로고    scopus 로고
    • Biomarkers in alcohol misuse: Their role in the prevention and detection of thiamine deficiency
    • Mancinelli R, Ceccanti M. Biomarkers in alcohol misuse: their role in the prevention and detection of thiamine deficiency. Alcohol Alcohol 2009; 44: 177-182
    • (2009) Alcohol Alcohol , vol.44 , pp. 177-182
    • Mancinelli, R.1    Ceccanti, M.2
  • 47
    • 0029116717 scopus 로고
    • Reduced activities of thiaminedependent enzymes in brains of alcoholics in the absence of Wernicke's encephalopathy
    • Lavoie J, Butterworth RF. Reduced activities of thiaminedependent enzymes in brains of alcoholics in the absence of Wernicke's encephalopathy. Alcohol Clin Exp Res 1995; 19: 1073-1077
    • (1995) Alcohol Clin Exp Res , vol.19 , pp. 1073-1077
    • Lavoie, J.1    Butterworth, R.F.2
  • 48
    • 0024756978 scopus 로고
    • Optimization of hydroxythiamine treatment regimen in vitaminological research
    • Zimatkina TI, Oparin DA, Ostrovskii YM. Optimization of hydroxythiamine treatment regimen in vitaminological research. Vopr Med Khim 1989; 61: 105-108
    • (1989) Vopr Med Khim , vol.61 , pp. 105-108
    • Zimatkina, T.I.1    Oparin, D.A.2    Ostrovskii, Y.M.3
  • 49
    • 51649099329 scopus 로고    scopus 로고
    • Region-selective alterations of glucose oxidation and amino acid synthesis in the thiamine- Deficient rat brain: A re-evaluation using 1H/13C nuclear magnetic resonance spectroscopy
    • Navarro D, Zwingmann C, Butterworth RF. Region-selective alterations of glucose oxidation and amino acid synthesis in the thiamine- deficient rat brain: a re-evaluation using 1H/13C nuclear magnetic resonance spectroscopy. J Neurochem 2008; 106: 603-612
    • (2008) J Neurochem , vol.106 , pp. 603-612
    • Navarro, D.1    Zwingmann, C.2    Butterworth, R.F.3
  • 50
    • 0020857020 scopus 로고
    • Activity of thiamine pyrophosphate-dependent enzymes in the rats after oxythiamine administration
    • Strumilo SA, Senkevich SB, Galitskii EA, Vinogradov VV. Activity of thiamine pyrophosphate-dependent enzymes in the rats after oxythiamine administration. Biull Eksp Biol Med 1983; 96: 42-44
    • (1983) Biull Eksp Biol Med , vol.96 , pp. 42-44
    • Strumilo, S.A.1    Senkevich, S.B.2    Galitskii, E.A.3    Vinogradov, V.V.4
  • 51
    • 0030034972 scopus 로고    scopus 로고
    • Different extent of inhibition of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase both containing endogenous thiamine pyrophosphate, by some anticoenzyme analogues
    • Strumilo S, Czygier M, Markiewicz J. Different extent of inhibition of pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase both containing endogenous thiamine pyrophosphate, by some anticoenzyme analogues. J Enzyme Inhib 1995; 10: 65-72. (Pubitemid 26022478)
    • (1996) Journal of Enzyme Inhibition , vol.10 , Issue.1 , pp. 65-72
    • Strumilo, S.1    Czygier, M.2    Markiewicz, J.3
  • 52
    • 0021270198 scopus 로고
    • Effect of oxythiamine on adrenal thiamine pyrophosphate-dependent enzyme activities
    • Strumilo SA, Senkevich SB, Vinogradov VV. Effect of oxythiamine on adrenal thiamine pyrophosphate-dependent enzyme activities. Biomed Biochim Acta 1984; 43: 159-163
    • (1984) Biomed Biochim Acta , vol.43 , pp. 159-163
    • Strumilo, S.A.1    Senkevich, S.B.2    Vinogradov, V.V.3
  • 53
    • 33646594715 scopus 로고    scopus 로고
    • Pyrithiamine as a substrate for thiamine pyrophosphokinase
    • Liu JY, Timm DE, Hurley TD. Pyrithiamine as a substrate for thiamine pyrophosphokinase. J Biol Chem 2006; 281: 6601-6607
    • (2006) J Biol Chem , vol.281 , pp. 6601-6607
    • Liu, J.Y.1    Timm, D.E.2    Hurley, T.D.3
  • 54
    • 0027131501 scopus 로고
    • Thiamine-dependent enzyme changes in the brains of alcoholics: Relationship to the Wernicke- Korsakoff syndrome
    • Butterworth RF, Kril JJ, Harper CG. Thiamine-dependent enzyme changes in the brains of alcoholics: relationship to the Wernicke- Korsakoff syndrome. Alcohol Clin Exp Res 1993; 17: 1084-1088
    • (1993) Alcohol Clin Exp Res , vol.17 , pp. 1084-1088
    • Butterworth, R.F.1    Kril, J.J.2    Harper, C.G.3
  • 55
    • 60449109339 scopus 로고    scopus 로고
    • Thiamine deficiency-related brain dysfunction in chronic liver failure
    • Butterworth RF. Thiamine deficiency-related brain dysfunction in chronic liver failure. Metab Brain Dis 2009; 24: 189-196
    • (2009) Metab Brain Dis , vol.24 , pp. 189-196
    • Butterworth, R.F.1
  • 56
    • 61449205168 scopus 로고    scopus 로고
    • Update of cell damage mechanisms in thiamine deficiency: Focus on oxidative stress, excitotoxicity and inflammation
    • Epub ahead of print
    • Hazell AS, Butterworth RF. Update of cell damage mechanisms in thiamine deficiency: focus on oxidative stress, excitotoxicity and inflammation. Alcohol Alcohol 2009; [Epub ahead of print].
    • (2009) Alcohol Alcohol
    • Hazell, A.S.1    Butterworth, R.F.2
  • 57
    • 2342461628 scopus 로고    scopus 로고
    • Three thiamine analogues differently alter thiamine transport and metabolism in nervous tissue: An in vivo kinetic study using rats
    • Rindi G, Patrini C, Nauti A, Bellazzi R, Magni P. Three thiamine analogues differently alter thiamine transport and metabolism in nervous tissue: an in vivo kinetic study using rats. Metab Brain Dis 2003; 18: 245-263
    • (2003) Metab Brain Dis , vol.18 , pp. 245-263
    • Rindi, G.1    Patrini, C.2    Nauti, A.3    Bellazzi, R.4    Magni, P.5
  • 58
    • 0343060864 scopus 로고    scopus 로고
    • Modulation of 2-oxoglutarate dehydrogenase complex by inorganic phosphate, Mg (2+), and other effectors
    • Rodriguez-Zavala JS, Pardo JP, Moreno-Sanchez R. Modulation of 2-oxoglutarate dehydrogenase complex by inorganic phosphate, Mg (2+), and other effectors. Arch Biochem Biophys 2000; 379: 78-84.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 78-84
    • Rodriguez-Zavala, J.S.1    Pardo, J.P.2    Moreno-Sanchez, R.3
  • 59
    • 0348229020 scopus 로고    scopus 로고
    • Assembly of the Covalent Linkage between Lipoic Acid and Its Cognate Enzymes
    • DOI 10.1016/j.chembiol.2003.11.016
    • Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE. Assembly of the covalent linkage between lipoic acid and its cognate enzymes. Chem Biol 2003; 10: 1293-1302 (Pubitemid 38042731)
    • (2003) Chemistry and Biology , vol.10 , Issue.12 , pp. 1293-1302
    • Zhao, X.1    Miller, J.R.2    Jiang, Y.3    Marletta, M.A.4    Cronan, J.E.5
  • 60
    • 0035371135 scopus 로고    scopus 로고
    • Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria
    • DOI 10.1016/S0014-5793(01)02469-3, PII S0014579301024693
    • Morikawa T, Yasuno R, Wada H. Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria. FEBS Lett 2001; 498: 16-21. (Pubitemid 32522883)
    • (2001) FEBS Letters , vol.498 , Issue.1 , pp. 16-21
    • Morikawa, T.1    Yasuno, R.2    Wada, H.3
  • 61
    • 0031418198 scopus 로고    scopus 로고
    • Biosynthesis of lipoic acid and posttranslational modification with lipoic acid in Escherichia coli
    • Jordan SW, Cronan JE Jr. Biosynthesis of lipoic acid and posttranslational modification with lipoic acid in Escherichia coli. Meth Enzymol 1997; 279: 177-183
    • (1997) Meth Enzymol , vol.279 , pp. 177-183
    • Jordan, S.W.1    Cronan Jr., J.E.2
  • 62
    • 0031431663 scopus 로고    scopus 로고
    • Lipoylation of acyltransferase components of 2-oxo acid dehydrogenase complexes
    • DOI 10.1016/S0076-6879(97)79023-2
    • Quinn J. Lipoyalation of acyltransferase components of 2-oxo acid dehydrogenase complexes. Meth Enzymol 1997; 279: 193-202. (Pubitemid 28180075)
    • (1997) Methods in Enzymology , vol.279 , pp. 193-202
    • Quinn, J.1
  • 63
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli lipA is a lipoyl synthase: In vitro biosynthesis of lipoyalated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
    • Miller JR, Busby RW, Jordan SW, et al. Escherichia coli lipA is a lipoyl synthase: in vitro biosynthesis of lipoyalated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 2000; 39: 15166-15178
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2    Jordan, S.W.3
  • 64
    • 0035800735 scopus 로고    scopus 로고
    • Purification, Characterization, and cDNA Cloning of Lipoate-activating Enzyme from Bovine Liver
    • DOI 10.1074/jbc.M101748200
    • Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y. Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J Biol Chem 2001; 276: 28819-28823 (Pubitemid 37451960)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.31 , pp. 28819-28823
    • Fujiwara, K.1    Takeuchi, S.2    Okamura-Ikeda, K.3    Motokawa, Y.4
  • 66
    • 0024382945 scopus 로고
    • Liberation of lipoate by human serum lipoamidase from bovine heart pyruvate dehydrogenase
    • Oizumi J, Hayakawa K. Liberation of lipoate by human serum lipoamidase from bovine heart pyruvate dehydrogenase. Biochem Biophys Res Commun 1989; 162: 658-663 (Pubitemid 19200890)
    • (1989) Biochemical and Biophysical Research Communications , vol.162 , Issue.2 , pp. 658-663
    • Oizumi, J.1    Hayakawa, K.2
  • 67
    • 0037352050 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase complexes in redox regulation: Role of the lipoate residues and thioredoxin
    • DOI 10.1046/j.1432-1033.2003.03470.x
    • Bunik V. 2-Oxo acid dehydrogenase complexes in redox regulation. Role of the lipoate residues and thioredoxin. Eur J Biochem 2003; 270: 1036-1042 (Pubitemid 36384437)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1036-1042
    • Bunik, V.I.1
  • 68
    • 77956936983 scopus 로고
    • Flavin-containing dehydrogenases
    • Boyer P, Ed.
    • Williams CH Jr. Flavin-containing dehydrogenases. In: Boyer P, Ed. Enzymes 1976; 13: 89-173.
    • (1976) Enzymes , vol.13 , pp. 89-173
    • Williams Jr., C.H.1
  • 70
    • 0018333111 scopus 로고
    • Regulation of α-ketoglutarate dehydrogenase complex from pigeon breast muscle
    • Gomazkova VS, Krasovskaya OE. Regulation of α-ketoglutarate dehydrogenase complex from pigeon breast muscle. Biokhimia 1979; 44: 1126-1136
    • (1979) Biokhimia , vol.44 , pp. 1126-1136
    • Gomazkova, V.S.1    Krasovskaya, O.E.2
  • 71
    • 0019485835 scopus 로고
    • Role of phosphate ions and divalent metals in the regulation of activity of the ketoglutarate dehydrogenase complex of the adrenal cortex
    • Russian
    • Strumilo SA, Taranda NI, Vinogradov VV. Role of phosphate ions and divalent metals in the regulation of activity of the ketoglutarate dehydrogenase complex of the adrenal cortex. Biokhimiia 1981; 46: 156-161 Russian.
    • (1981) Biokhimiia , vol.46 , pp. 156-161
    • Strumilo, S.A.1    Taranda, N.I.2    Vinogradov, V.V.3
  • 72
    • 0019890086 scopus 로고
    • Regulation of bovine kidney α-ketoglutarate dehydrogenase complex by calcium ions and adenine nucleotides. Effect on S0.5 for ketoglutarate
    • Lawlis BV, Roche TE. Regulation of bovine kidney α-ketoglutarate dehydrogenase complex by calcium ions and adenine nucleotides. Effect on S0.5 for ketoglutarate. Biochemistry 1981; 20: 2512-2518
    • (1981) Biochemistry , vol.20 , pp. 2512-2518
    • Lawlis, B.V.1    Roche, T.E.2
  • 73
    • 0029439354 scopus 로고
    • Some regulatory properties of the 2-oxoglutarate dehydrogenase complex from European bison heart
    • Markiewicz J, Strumilo S. Some regulatory properties of the 2-oxoglutarate dehydrogenase complex from European bison heart. Acta Biochim Polonica 1995; 42: 339-346
    • (1995) Acta Biochim Polonica , vol.42 , pp. 339-346
    • Markiewicz, J.1    Strumilo, S.2
  • 74
    • 0020336224 scopus 로고
    • Peculiarities of the regulation of the adrenal oxoglutarate dehydrogenase complex by NADH and adenosine diphosphate
    • Russian
    • Strumilo SA, Taranda NI, Vinogradov VV. Peculiarities of the regulation of the adrenal oxoglutarate dehydrogenase complex by NADH and adenosine diphosphate. Biokhimiia 1982; 47: 724-732 Russian
    • (1982) Biokhimiia , vol.47 , pp. 724-732
    • Strumilo, S.A.1    Taranda, N.I.2    Vinogradov, V.V.3
  • 75
    • 0021754240 scopus 로고
    • Elementary steps in the reaction mechanism of the α-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: Kinetics of succinylation and desuccinylation
    • Waskiewicz DE, Hammes GG. Elementary steps in the reaction mechanism of the α-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation. Biochemistry 1980; 23: 3136-3143
    • (1980) Biochemistry , vol.23 , pp. 3136-3143
    • Waskiewicz, D.E.1    Hammes, G.G.2
  • 76
    • 0015956014 scopus 로고
    • Regulation of mitochondrial ketoglutarate metabolism by product inhibition at α-ketoglutarate dehydrogenase
    • Smith CM, Bryla J, Williamson JR. Regulation of mitochondrial ketoglutarate metabolism by product inhibition at α-ketoglutarate dehydrogenase. J Biol Chem 1974; 249: 1497-1505
    • (1974) J Biol Chem , vol.249 , pp. 1497-1505
    • Smith, C.M.1    Bryla, J.2    Williamson, J.R.3
  • 77
    • 0017374072 scopus 로고
    • Purification and properties of pigeon breast muscle α-keto acid dehydrogenase complexes
    • Furuta S, Shindo Y, Hashimoto T. Purification and properties of pigeon breast muscle α-keto acid dehydrogenase complexes. J Biochem 1977; 81: 1839-1847
    • (1977) J Biochem , vol.81 , pp. 1839-1847
    • Furuta, S.1    Shindo, Y.2    Hashimoto, T.3
  • 78
    • 0019890079 scopus 로고
    • Inhibition of bovine kidney α-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 BV, Roche TE. Inhibition of bovine kidney α-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, B.V.1    Roche, T.E.2
  • 79
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • Bunik V, Sievers C. Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur J Biochem 2002; 269: 5004-5015
    • (2002) Eur J Biochem , vol.269 , pp. 5004-5015
    • Bunik, V.1    Sievers, C.2
  • 80
    • 47349131606 scopus 로고    scopus 로고
    • Store-operated Ca2+ entry in muscle physiology
    • Brotto M, Weisleder N, Ma J. Store-operated Ca2+ entry in muscle physiology. Curr Chem Biol 2007; 1: 87-95.
    • (2007) Curr Chem Biol , vol.1 , pp. 87-95
    • Brotto, M.1    Weisleder, N.2    Ma, J.3
  • 81
    • 0018363365 scopus 로고
    • The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex
    • McCormack JG, Denton RM. The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochem J 1979; 180: 533-544
    • (1979) Biochem J , vol.180 , pp. 533-544
    • McCormack, J.G.1    Denton, R.M.2
  • 82
    • 0020794116 scopus 로고
    • Participation of Ca2+ in regulation of activity of oxoglutarate dehydrogenase complex from bovine adrenal cortex
    • Strumilo SA. Participation of Ca2+ in regulation of activity of oxoglutarate dehydrogenase complex from bovine adrenal cortex. Ukrainian Biochem J 1983; 55: 415-419
    • (1983) Ukrainian Biochem J , vol.55 , pp. 415-419
    • Strumilo, S.A.1
  • 83
    • 0028172376 scopus 로고
    • Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart
    • Nichols BJ, Rigoulet M, Denton RM. Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart. Biochem J 1994; 303: 461-465
    • (1994) Biochem J , vol.303 , pp. 461-465
    • Nichols, B.J.1    Rigoulet, M.2    Denton, R.M.3
  • 84
    • 0019881041 scopus 로고
    • A comparative study of the regulation by Ca2+ of the activities of the 2-oxoglutarate dehydrogenase complex and NAD-isocitrate dehydrogenase from variety of sources
    • McCormack JG, Denton RM. A comparative study of the regulation by Ca2+ of the activities of the 2-oxoglutarate dehydrogenase complex and NAD-isocitrate dehydrogenase from variety of sources. Biochem J 1981; 196: 619-624
    • (1981) Biochem J , vol.196 , pp. 619-624
    • McCormack, J.G.1    Denton, R.M.2
  • 85
    • 0021647875 scopus 로고
    • Cooperation of Ca2+ and pH in regulation of the activity of the 2-oxoglutarate dehydrogenase complex and its components from bovine kidney cortex
    • Pawelczyk T, Angielski S. Cooperation of Ca2+ and pH in regulation of the activity of the 2-oxoglutarate dehydrogenase complex and its components from bovine kidney cortex. Acta Biochim Polonica 1984; 31: 289-305.
    • (1984) Acta Biochim Polonica , vol.31 , pp. 289-305
    • Pawelczyk, T.1    Angielski, S.2
  • 86
    • 0030740265 scopus 로고    scopus 로고
    • 2+ on the catalytic function of heart muscle 2-oxoglutarate dehydrogenase complex
    • 2+ on the catalytic function of heart muscle 2-oxoglutarate dehydrogenase complex. Biochem Arch 1997; 13: 127-129
    • (1997) Biochem Arch , vol.13 , pp. 127-129
    • Markiewicz, J.1    Strumilo, S.2
  • 87
    • 33947579630 scopus 로고    scopus 로고
    • Enzymecatalyzed side reactions with molecular oxygen may contribute to cell signaling and neurodegenerative diseases
    • Bunik V, 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.1    Schloss, J.V.2    Pinto, J.T.3    Gibson, G.E.4    Cooper, A.J.L.5
  • 89
    • 0025043286 scopus 로고
    • Participation of adenosine diphosphate in regulation of the 2-oxoglutarate dehydrogenase complex from human heart
    • Ostrovtsova SA, Strumilo SA. Participation of adenosine diphosphate in regulation of the 2-oxoglutarate dehydrogenase complex from human heart. Biomed Biochim Acta 1990; 49: 515-517
    • (1990) Biomed Biochim Acta , vol.49 , pp. 515-517
    • Ostrovtsova, S.A.1    Strumilo, S.A.2
  • 90
    • 0019013534 scopus 로고
    • Kinetic and regulatory properties of α-ketoglutarate dehydrogenase complex from bovine adrenals
    • Strumilo SA, Vinogradov VV, Senkevich SB. Kinetic and regulatory properties of α-ketoglutarate dehydrogenase complex from bovine adrenals. Ukrainian Biochem J 1980; 52: 321-324
    • (1980) Ukrainian Biochem J , vol.52 , pp. 321-324
    • Strumilo, S.A.1    Vinogradov, V.V.2    Senkevich, S.B.3
  • 91
    • 0020715594 scopus 로고
    • Essential arginine residues for catalytic and regulatory functions of alpha-ketoglutarate dehydrogenase from pigeon breast muscle
    • Stafeeva OA, Gomazkova VS, Severin SE. Essential arginine residues for catalytic and regulatory functions of alpha-ketoglutarate dehydrogenase from pigeon breast muscle. Biochem Int 1983; 6: 315-321
    • (1983) Biochem Int , vol.6 , pp. 315-321
    • Stafeeva, O.A.1    Gomazkova, V.S.2    Severin, S.E.3
  • 92
    • 0021235230 scopus 로고
    • 2,3-Butanedione desensitization of bovine adrenal 2-oxoglutarate dehydrogenase to adenosine-5-diphosphate
    • Strumilo SA, Taranda NI, Vinogradov VV. 2,3-Butanedione desensitization of bovine adrenal 2-oxoglutarate dehydrogenase to adenosine-5-diphosphate. Biomed Biochim Acta 1984; 43: 237-240
    • (1984) Biomed Biochim Acta , vol.43 , pp. 237-240
    • Strumilo, S.A.1    Taranda, N.I.2    Vinogradov, V.V.3
  • 93
    • 22444432948 scopus 로고
    • Cooperative character of the interaction of adenosine-diphosphate with oxoglutarate dehydrogenase complex from adrenal cortex
    • Strumilo SA, Taranda NI, Vinogradov VV. Cooperative character of the interaction of adenosine-diphosphate with oxoglutarate dehydrogenase complex from adrenal cortex. Doklady AN BSSR 1983; 27: 269-271
    • (1983) Doklady AN BSSR , vol.27 , pp. 269-271
    • Strumilo, S.A.1    Taranda, N.I.2    Vinogradov, V.V.3
  • 94
    • 0019145230 scopus 로고
    • Relationship of free cytoplasmic pyrophosphate to liver glucose content and total pyrophosphate to cytoplasmic phosphorylation potential
    • Veech RL, Cook GA, King MT. Relationship of free cytoplasmic pyrophosphate to liver glucose content and total pyrophosphate to cytoplasmic phosphorylation potential. FEBS Lett 1980; 117: K65- 72.
    • (1980) FEBS Lett , vol.117
    • Veech, R.L.1    Cook, G.A.2    King, M.T.3
  • 95
    • 0020164856 scopus 로고
    • The role of ATP in regulation of the adrenal oxoglutarate dehydrogenase complex
    • Strumilo SA, Taranda NI, Vinogradov VV. The role of ATP in regulation of the adrenal oxoglutarate dehydrogenase complex. Vopr Med Khim 1982; 28: 59-61.
    • (1982) Vopr Med Khim , vol.28 , pp. 59-61
    • Strumilo, S.A.1    Taranda, N.I.2    Vinogradov, V.V.3
  • 96
    • 0018086356 scopus 로고
    • Homeostatic regulation of cellular energy metabolism
    • Erecinska M, Wilson DF. Homeostatic regulation of cellular energy metabolism. Trends Biochem Sci 1978; 3: 219-223
    • (1978) Trends Biochem Sci , vol.3 , pp. 219-223
    • Erecinska, M.1    Wilson, D.F.2
  • 98
    • 0037155880 scopus 로고    scopus 로고
    • Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase
    • Gazaryan IG, Krasnikov BF, Ashby GA, Thorneley RN, Kristal BS, Brown AM. Zinc is a potent inhibitor of thiol oxidoreductase activity and stimulates reactive oxygen species production by lipoamide dehydrogenase. J. Biol. Chem 2002; 277: 10064-10072
    • (2002) J. Biol. Chem , vol.277 , pp. 10064-10072
    • Gazaryan, I.G.1    Krasnikov, B.F.2    Ashby, G.A.3    Thorneley, R.N.4    Kristal, B.S.5    Brown, A.M.6
  • 99
    • 0034622573 scopus 로고    scopus 로고
    • Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme: A pulse radiolysis study
    • Hanine Lmoumene CEl, Conte D, Jacquot JP, Houee-Levin C. Redox properties of protein disulfide bond in oxidized thioredoxin and lysozyme: a pulse radiolysis study. Biochemistry 2000; 39: 9295-9301
    • (2000) Biochemistry , vol.39 , pp. 9295-9301
    • Cel, H.L.1    Conte, D.2    Jacquot, J.P.3    Houee-Levin, C.4
  • 100
    • 58149469744 scopus 로고    scopus 로고
    • Alpha-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ
    • Zündorf G, Kahlert S, Bunik VI, Reiser G. alpha-Ketoglutarate dehydrogenase contributes to production of reactive oxygen species in glutamate-stimulated hippocampal neurons in situ. Neurosci 2009; 158: 610-616
    • (2009) Neurosci , vol.158 , pp. 610-616
    • Zündorf, G.1    Kahlert, S.2    Bunik, V.I.3    Reiser, G.4
  • 101
    • 0032920176 scopus 로고    scopus 로고
    • Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes
    • Bunik V, Raddatz G, Lemaire S, Meyer Y, Jacquot J-P, Bisswanger H. Interaction of thioredoxins with target proteins: Role of particular structural elements and electrostatic properties of thioredoxins in their interplay with 2-oxoacid dehydrogenase complexes. Prot Sci 1999; 8: 65-74.
    • (1999) Prot Sci , vol.8 , pp. 65-74
    • Bunik, V.1    Raddatz, G.2    Lemaire, S.3    Meyer, Y.4    Jacquot, J.-P.5    Bisswanger, H.6
  • 102
    • 0034681508 scopus 로고    scopus 로고
    • Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thioldisulfide oxidoreductase
    • Bunik V. Increased catalytic performance of the 2-oxoacid dehydrogenase complexes in the presence of thioredoxin, a thioldisulfide oxidoreductase. J Mol Catal B Enzymatic 2000; 8: 165-174
    • (2000) J Mol Catal B Enzymatic , vol.8 , pp. 165-174
    • Bunik, V.1
  • 103
    • 34147137668 scopus 로고    scopus 로고
    • Thioredoxin 1 and thioredoxin 2 have opposed regulatory functions on hypoxiainducible factor-1alpha
    • Zhou J, Damdimopoulos AE, Spyrou G, Brüne B. Thioredoxin 1 and thioredoxin 2 have opposed regulatory functions on hypoxiainducible factor-1alpha. J Biol Chem 2007; 282: 7482-7490
    • (2007) J Biol Chem , vol.282 , pp. 7482-7490
    • Zhou, J.1    Damdimopoulos, A.E.2    Spyrou, G.3    Brüne, B.4
  • 104
    • 48749112811 scopus 로고    scopus 로고
    • Oxidative stress and thioredoxin system
    • Koharyova M, Kolarova M. Oxidative stress and thioredoxin system. Gen Physiol Biophys 2008; 27: 71-84.
    • (2008) Gen Physiol Biophys , vol.27 , pp. 71-84
    • Koharyova, M.1    Kolarova, M.2
  • 105
    • 0027215408 scopus 로고
    • Inactivation of alpha-ketoglutarate dehydrogenase during oxidative decarboxylation of alfa-ketoadipic acid
    • Bunik VI, Pavlova OG. Inactivation of alpha-ketoglutarate dehydrogenase during oxidative decarboxylation of alfa-ketoadipic acid. FEBS Lett 1993; 323: 166-170 (Pubitemid 223027201)
    • (1993) FEBS Letters , vol.323 , Issue.1-2 , pp. 166-170
    • Bunik, V.I.1    Pavlova, O.G.2
  • 106
    • 0031218739 scopus 로고    scopus 로고
    • Inactivation of alpha-ketoglutarate dehydrogenase during its enzymatic reaction
    • Moscow
    • Bunik VI, Pavlova OG. Inactivation of alpha-ketoglutarate dehydrogenase during its enzymatic reaction. Biochemistry (Moscow) 1997; 62: 973-982
    • (1997) Biochemistry , vol.62 , pp. 973-982
    • Bunik, V.I.1    Pavlova, O.G.2
  • 107
    • 0031216377 scopus 로고    scopus 로고
    • Inhibition of α-ketoglutarate dehydrogenase from pigeon breast muscle by the structural analogs of substarte
    • Bunik VI, Pavlova OG. Inhibition of α-ketoglutarate dehydrogenase from pigeon breast muscle by the structural analogs of substarte. Biochemistry 1997; 62: 1012-1020
    • (1997) Biochemistry , vol.62 , pp. 1012-1020
    • Bunik, V.I.1    Pavlova, O.G.2
  • 109
    • 0026070649 scopus 로고
    • Effect of α-ketoglutarate and its structural analogues on hysteretic properties of α-ketoglutarate dehydrogenase
    • Bunik VI, Romash OG, Gomazkova VS. Effect of α-ketoglutarate and its structural analogues on hysteretic properties of α-ketoglutarate dehydrogenase. FEBS Lett 1991; 278: 147-150
    • (1991) FEBS Lett , vol.278 , pp. 147-150
    • Bunik, V.I.1    Romash, O.G.2    Gomazkova, V.S.3
  • 110
    • 0014940726 scopus 로고
    • Kinetic aspects of regulation of metabolic processes. the hysteretic enzyme concept
    • Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J Biol Chem 1970; 245: 5788-5799
    • (1970) J Biol Chem , vol.245 , pp. 5788-5799
    • Frieden, C.1
  • 111
    • 33744950488 scopus 로고    scopus 로고
    • Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein
    • DOI 10.1074/jbc.M512515200
    • Niebisch A, Kabus A, Schultz C, Weil B, Bott M. Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein. J Biol Chem 2006; 281: 12300-12307 (Pubitemid 43855314)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12300-12307
    • Niebisch, A.1    Kabus, A.2    Schultz, C.3    Weil, B.4    Bott, M.5
  • 112
    • 34548499343 scopus 로고    scopus 로고
    • Offering surprises: TCA cycle regulation in Corynebacterium glutamicum
    • Bott M. Offering surprises: TCA cycle regulation in Corynebacterium glutamicum. Trends Microbiol 2007; 15: 417-425
    • (2007) Trends Microbiol , vol.15 , pp. 417-425
    • Bott, M.1
  • 113
    • 34548008354 scopus 로고    scopus 로고
    • Glutamate production by Corynebacterium glutamicum: Dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG
    • Schultz C, Niebisch A, Gebel L. Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG. Appl Microbiol Biotechnol 2007; 76: 691-700.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 691-700
    • Schultz, C.1    Niebisch, A.2    Gebel, L.3
  • 115
    • 0023116918 scopus 로고
    • Inactivation of 2-Oxoglutarate dehydrogenase in rat liver mitochondria by its substrate and t-butyl hydroperoxide
    • Rokutan K, Kawai K, Asada K. Inactivation of 2-oxoglutarate dehydrogenase in rat liver mitochondrial by its substrate and t-butyl hydroperoxide. J Biochem 1987; 101: 415-422 (Pubitemid 17004313)
    • (1987) Journal of Biochemistry , vol.101 , Issue.2 , pp. 415-422
    • Rokutan, K.1    Kawai, K.2    Asada, K.3
  • 116
    • 0021427125 scopus 로고
    • Enzyme inactivation in the reaction process. Regulatory role
    • Varfolomeev SD. Enzyme inactivation in the reaction process. Regulatory role. Biokhimiya 1984; 49: 723-735
    • (1984) Biokhimiya , vol.49 , pp. 723-735
    • Varfolomeev, S.D.1
  • 117
    • 0023644742 scopus 로고
    • The macrokinetic behavior of an enzymatic system with an enzyme inactivated in the reaction
    • Sudina GF, Kobelkov GM, Varfolomeev SD. The macrokinetic behavior of an enzymatic system with an enzyme inactivated in the reaction. Biotechnol Bioeng 1987; 29: 625-632
    • (1987) Biotechnol Bioeng , vol.29 , pp. 625-632
    • Sudina, G.F.1    Kobelkov, G.M.2    Varfolomeev, S.D.3
  • 118
    • 0034666260 scopus 로고    scopus 로고
    • The cytotoxic lipid peroxidation product, 4-hydroxy-2-nonenal, specifically inhibits decarboxylating dehydrogenases in the matrix of plant mitochondria
    • Millar AH, Leaver CJ. The cytotoxic lipid peroxidation product, 4-hydroxy-2-nonenal, specifically inhibits decarboxylating dehydrogenases in the matrix of plant mitochondria. FEBS Lett 2000; 481: 117-121
    • (2000) FEBS Lett , vol.481 , pp. 117-121
    • Millar, A.H.1    Leaver, C.J.2
  • 119
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • Humphries KM, Szweda LI. Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 1998; 37: 15835-15841
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 120
    • 0142213541 scopus 로고    scopus 로고
    • Age-Related Increase in 4-Hydroxynonenal Adduction to Rat Heart alpha-Ketoglutarate Dehydrogenase Does Not Cause Loss of Its Catalytic Activity
    • Moreau R, Heath SH, Doneanu CE, Lindsay JG, Hagen TM. Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity. Antioxid Redox Signal 2003; 5: 517-527 (Pubitemid 37315138)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.5 , pp. 517-527
    • Moreau, R.1    Heath, S.-H.D.2    Doneanu, C.E.3    Lindsay, J.G.4    Hagen, T.M.5
  • 121
    • 0035341962 scopus 로고    scopus 로고
    • Protection by thiols of the mitochondrial complexes from 4-hydroxy-2-nonenal
    • DOI 10.1016/S0891-5849(01)00491-9, PII S0891584901004919
    • Korotchkina LG, Yang H, Tirosh O, Packer L, Patel MS. Protection by thiols of the mitochondrial complexes from 4-hydroxy-2-nonenal. Free Radic Biol Med 2001; 30: 992-999 (Pubitemid 32333029)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.9 , pp. 992-999
    • Korotchkina, L.G.1    Yang, H.-S.2    Tirosh, O.3    Packer, L.4    Patel, M.S.5
  • 122
    • 37849043898 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: Glutathionylation and protection of lipoic acid
    • Applegate MA, Humphries KM, Szweda LI. Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid. Biochemistry 2008; 47: 473-478
    • (2008) Biochemistry , vol.47 , pp. 473-478
    • Applegate, M.A.1    Humphries, K.M.2    Szweda, L.I.3
  • 123
    • 0345146921 scopus 로고    scopus 로고
    • Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
    • Nulton-Persson AC, Starke DW, Mieyal JJ, Szweda LI. Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 2003; 42: 4235-4242
    • (2003) Biochemistry , vol.42 , pp. 4235-4242
    • Nulton-Persson, A.C.1    Starke, D.W.2    Mieyal, J.J.3    Szweda, L.I.4
  • 125
    • 0030812593 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha- Ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length
    • Cooper AJ, Sheu KR, Burke JR, et al. Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha- ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length. Proc Natl Acad Sci USA 1997; 94: 12604-12609
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12604-12609
    • Cooper, A.J.1    Sheu, K.R.2    Burke, J.R.3
  • 126
    • 3042641843 scopus 로고    scopus 로고
    • 0
    • DOI 10.1074/jbc.M314148200
    • MacDonald MJ, Husain RD, Hoffmann-Benning S, Baker TR. Immunochemical identification of coenzyme Q0-dihydrolipoamide adducts in the E2 components of the alpha-ketoglutarate and pyruvate dehydrogenase complexes partially explains the cellular toxicity of coenzyme Q0. J Biol Chem 2004; 279: 27278-27285 (Pubitemid 38812567)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27278-27285
    • MacDonald, M.J.1    Husain, R.D.2    Hoffmann-Benning, S.3    Baker, T.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.