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Báo cáo khoa học: Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

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The enzymes pyruvate decarboxylase (E1) and dihydro-lipoyl dehydrogenase (E3) bind tightly but in a mutuallyexclusive manner to the peripheral subunit-binding domain(PSBD) of dihydrolipoyl acetyltransferase in the pyruvatedehydrogenase multienzyme complex of Bacillus stearo-thermophilus. The use of directed mutagenesis, surfaceplasmon resonance detection and isothermal titrationmicrocalorimetry revealed that several positively chargedresidues of the PSBD, most notably Arg135, play animportant part in the interaction with both E1 and E3,whereas Met131 makes a significant contribution to thebinding of E1 only. ...
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Báo cáo khoa học: Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

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