Further studies on thermal denaturation of pyruvate dehydrogenase complex from Bacillus stearothermophilus.
Thermally induced changes in pyruvate dehydrogenase complex (PDC) from B. stearothermophilus were examined mainly at temperatures from 60 degrees to 70 degrees C. Accompanied by inactivation of pyruvate decarboxylase, light scattering decreased, and ANS fluorescence increased. These changes including the inactivation were approximately first-order reactions, and the values of rate constants were greatly dependent on temperature. Chromatographic studies showed that any polypeptides were in associated forms and that final products were aggregates (> 230S) and an assembly (48S) smaller than PDC. The aggregates and assembly were rich in decarboxylase and lipoate acetyltransferase, respectively. It was suggested that, during the thermal denaturation, a decarboxylase was dissociated from PDC and immediately involved in aggregates.
Hiromasa
Y
Y
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Aso
Y
Y
Yamashita
S
S
Aikawa
Y
Y
Ishiguro
M
M
D002850:Chromatography, Gel; D004789:Enzyme Activation; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D006358:Hot Temperature; D008027:Light; D011489:Protein Denaturation; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000378:metabolism*; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013997:Time Factors
D011768:Pyruvate Dehydrogenase Complex