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Original Articles

Thermally Induced Disintegration of the Bacillus stearothermophilus Dihydrolipoamide Dehydrogenase

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Pages 1923-1929 | Received 17 Mar 2000, Accepted 09 May 2000, Published online: 22 May 2014

  • 1) Henderson, C. E. and Perham, R. N., Purification of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and resolution of its four component polypeptides. Biochem. J., 189, 161-172 (1980).
  • . 1996. p. 1- 16.
  • 3) Mande, S. S., Sarfaty, S., Allen, M. D., Perham, R. N., and Hol, W. G., Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Structure, 4, 277-286 (1996).
  • 4) Izard, T., Evarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A., and Hol, W. G. J., Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc. Natl. Acad. Sci., 96, 1240-1245 (1999).
  • 5) Hiromasa, Y., Aso, Y., and Yamashita, S., Thermal disassembly of pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. Biosci. Biotechnol. Biochem., 62, 1904-1905 (1994).
  • 6) Hiromasa, Y., Aso, Y., Yamashita, S., Aikawa, Y., and Ishiguro, M., Further studies on thermal denaturation of pyruvate dehydrogenase complex from Bacillus stearothermophilus. Biosci. Biotechnol. Biochem., 61, 1126-1132 (1997).
  • 7) Witzmann, S. and Bisswanger, H., The pyruvate dehydrogenase complex from thermophilic organisms: thermal stability and re-association from the enzyme components. Biochim. Biophys. Acta, 1385, 341-352 (1998).
  • 8) Hiromasa, Y., Aso, Y., Yamashita, S., and Aikawa, Y., Homogeneity of the pyruvate dehydrogenase multienzyme complex from Bacillus stearothermophilus. J. Biochem., 117, 467-470 (1995).
  • 9) Hiromasa, Y., Aso, Y., and Yamashita, S., Purification of the pyruvate dehydrogenase complex from an extreme thermophile, Bacillus caldolyticus, and its thermal stability. Biosci. Biotechnol. Biochem., 57, 1062-1066 (1993).
  • . 1976.
  • 11) Aso, Y., Hiromasa, Y., Aikawa, Y., Meno, K., and Ishiguro, M., Potassium iodide-induced changes in pyruvate dehydrogenase complex from Bacillus stearothermophilus. Biosci. Biotechnol. Biochem., 62, 108-116 (1998).
  • 12) Ogasahara, K., Koike, K., Hamada, M., and Hiraoka, T., Interaction of hydrophobic probes with the apoenzyme of pig heart lipoamide dehydrogenase. J. Biochem., 79, 967-975 (1976).
  • 13) Packman, L. C., Borges, A., and Perham, R. N., Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase of the pyruvate dehydrogenase complex from Bacillus stearothermophilus. Biochem. J., 252, 79-86 (1988).
  • 14) Borges, A., Hawkins, C. F., Packman, L. C., and Perham, R. N., Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Eur. J. Biochem., 194, 95-102 (1990).
  • . 1996. p. 53- 70.
  • 16) van Berkel, W. J. H., Regelink, A. G., Beintema, J. J., and de Kok, A., The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii. Eur. J. Biochem., 202, 1049-1055 (1991).
  • 17) van Berkel, W. J. H., Benen, J. A. E., and Snoek, M. C., On the FAD-induced dimerization of apo-lipoamide dehydrogenase from Azotobacter vinelandii and Pseudomonas fluorescens. Kinetics of reconstitution. Eur. J. Biochem., 197, 769-779 (1991).
  • 18) de Kok, A., Hengeveld, A.F., Martin, A., and Westphal, A.H., The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria. Biochim. Biophys. Acta, 1385, 353-366 (1998).

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