Activation of mitochondrial 2-oxoacid dehydrogenases by thioredoxin

Biological Chemistry

Volumn 378, Issue 10, 1997, Pages 1125-1130

  Bunik, Victoria ^a,b   Follmann, Hartmut ^c   Bisswanger, Hans ^b  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b UNIVERSITY OF TÜBINGEN   (Germany)

^c UNIVERSITY OF KASSEL   (Germany)

Author keywords

2 Oxoglutarate; Catalysis induced inactivation; Coenzyme A; Dihydrolipoate; PyruvateThiol disulfide exchange

Indexed keywords

2 OXOACID DEHYDROGENASE; CYSTEINE; DIHYDROLIPOATE; DITHIOTHREITOL; GLUTATHIONE DISULFIDE; MITOCHONDRIAL ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; THIOREDOXIN;

ANIMAL TISSUE; ARTICLE; CHLOROPLAST; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME INACTIVATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MITOCHONDRIAL RESPIRATION; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; SWINE;

ANIMALIA; ESCHERICHIA COLI; SUS SCROFA;

EID: 0030656589     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.10.1125     Document Type: Article

References (25)

1. Bodenstein, J., and Follmann, H. (1991). Characterization of two thioredoxins in pig heart including a new mitochondrial protein. Z. Naturforsch. 46c, 270-279.
2. Bodenstein-Lang, J., Buch, A., and Follmann, H. (1989). Animal and plant mitochondria contain specific thioredoxins. FEBS Lett. 258, 22-26.
3. Braun, H., Lichter, A., and Häberlein, I. (1996). Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme. Eur. J. Biochem. 240, 781-788.
4. Bunik, V.I., Buneeva, O.A., and Gomazkova, V.S. (1990). Change in α-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH. FEBS Lett. 269, 252-254.
5. Bunik, V.I., Buneeva, O.A., and Gomazkova, V.S. (1991). Regulation of cooperative properties of α-ketoglutarate dehydrogenase by thiol-disulfide exchange. Biokhimiya (Russ.) 56, 694-706.
6. Bunik, V.I., and Follmann, H. (1993). Thioredoxin reduction dependent on α-ketoacid oxidation by α-ketoacid dehydrogenase complexes. FEBS Lett. 336, 197-200.
7. Bunik, V., Shoubnikova, A., Löffelhardt, S., Bisswanger, H., Borbe, H.O., and Follmann, H. (1995). Using lipoate enantiomers and thioredoxin to study the mechanism of the 2-oxoacid-dependent dihydrolipoate production by the 2-oxoacid dehydrogenase complexes. FEBS Lett. 371, 167-170.
8. Bunik, V., Romash, O.G., and Gomazkova, V.S. (1990). Inactivation of α-ketoglutarate dehydrogenase during enzyme-catalyzed reaction. Biochem. Internat. 22, 967-976.
9. Bunik, V.I., and Pavlova, O.G. (1993). Inactivation of α-ketoglutarate dehydrogenase during oxidative decarboxylation of α-ketoadipic acid. FEBS Lett. 323, 166-170.
10. Follmann, H., and Häberlein, I. (1995/1996). Thioredoxins: Universal, yet specific thioldisulfide redox cofactors. Biofactors 6, 147-156.
11. Häberlein, I., and Vogeler, B. (1995). Completion of the thioredoxin reaction mechanism: Kinetic evidence for protein complexes between thioredoxin and fructose 1,6-bisphosphatase. Biochim. Biophys. Acta 1253, 169-174.
12. Holmgren, A. (1979a). Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632.
13. Holmgren, A. (1979b). Reduction of disulfides by thioredoxin. J. Biol. Chem. 254, 9113-9119.
14. Holmgren, A. (1989). Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-13966.
15. Kallis, G.B., and Holmgren, A. (1980). Differential reactivity of the functional sulfhydryl groups of cystein-32 and cystein-35 present in the reduced form of thioredoxin from Escherichia coli. J. Biol. Chem. 255, 10261-10265.
16. Konrad, A., Banze, M., and Follmann, H. (1996). Mitochondria of plant leaves contain two thioredoxins. Completion of the thioredoxin profile of higher plants. J. Plant Physiol. 49, 317-321.
17. LeMaster, D.M. (1996). Structural determinants of the catalytic reactivity of the buried cysteine of Escherichia coli thioredoxin. Biochemistry 35, 14876-14881.
18. McMinn, C.L., and Ottaway, J.H. (1977). Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart. Biochem. J. 161, 569-581.
19. Patel, M.S., and Harris, R.A. (1995). Mammalian α-keto acid dehydrogenase complexes: Gene regulation and genetic defects. FASEB J. 9, 1164-1172.
20. Reed, L.J., and Hackert, M.L. (1990). Structure-function relationships in dihydrolipoamide acyltransferases. J. Biol. Chem. 265, 8971-8974.
21. Rokutan, K., Kawai, K., and Asada, K. (1987). Inactivation of 2-oxoglutarate dehydrogenase in rat liver mitochondria by its substrate and t-butyl hydroperoxide. J. Biochem. 101, 415-422.
22. Russel, M. (1995). Thioredoxin genetics. Meth. Enzymol. 252, 264-274.
23. Spyrou, G., Enmark, E., Miranda-Vizuete, A., and Gustafsson, J.-A. (1997). Cloning and expression of a novel mammalian thioredoxin. J. Biol. Chem. 272, 2936-2941.
24. Stanley, C.J., and Perham, R.N. (1980). Purification of 2-oxo acid dehydrogenase multienzyme complexes from ox heart by a new method. Biochem. J. 191, 147-154.
25. Sumegi, B., and Alkonyi, I. (1983). Paracatalytic inactivation of pig heart pyruvate dehydrogenase complex. Arch. Biochem. Biophys. 223, 417-424.