Time‐resolved fluorescence studies on mutants of the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii

FEBS Letters

Westphal, Adrie H.¹  Berg, Axel¹  Schulze, Egbert¹  de Kok, Arie¹ 

[1] Department of Biochemistry, Agricultural University, Wageningen, The Netherlands

关键词: Dihydrolipoyl transacetylase;    Pyruvate dehydrogenase complex;    Time-resolved fluorescence;    Mobility;   

DOI  :  10.1016/0014-5793(90)81047-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fluorescence anisotropy decays were measured for the wild-type dihydrolipoyl transacetylase (E2) component of pyruvate dehydrogenase complex from Azotobacter vinelandii and E. coli and for E2-mutants from A. vinelandii in which the alanine-proline-rich sequence between the binding domain and the catalytic domain is partially or completely deleted. In both E2-mutants the rotational mobility of the lipoyl domain and the overall activity after reconstitution of the complex are significantly decreased indicating the important role of the deleted sequence for the movement of the lipoyl domain and the transfer of substrates between the different active sites within the complex.

【 授权许可】

Unknown