Báo cáo khoa học: Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
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A15N-labelled peripheral-subunit binding domain (PSBD) of the dihydro-lipoyl acetyltransferase (E2p) and the dimer of a solubilized interfacedomain (E3int) derived from the dihydrolipoyl dehydrogenase (E3) wereused to investigate the basis of the interaction of E2p with E3 in the assem-bly of the pyruvate dehydrogenase multienzyme complex ofBacillus stearo-thermophilus. Thirteen of the 55 amino acids in the PSBD show significantchanges in either or both of the15N and1H amide chemical shifts whenthe PSBD forms a 1 : 1 complex with E3int. ...
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Báo cáo khoa học: Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
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