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, 913 (2), 117-21

A Mutant Pyruvate Dehydrogenase Complex of Escherichia Coli Deleted in the (Alanine + Proline)-Rich Region of the Acetyltransferase Component

A Mutant Pyruvate Dehydrogenase Complex of Escherichia Coli Deleted in the (Alanine + Proline)-Rich Region of the Acetyltransferase Component

J S Miles et al. Biochim Biophys Acta.

Abstract

The acetyltransferase chains of the pyruvate dehydrogenase complex of Escherichia coli contain conformationally mobile (alanine + proline)-rich segments that link the lipoyl domains to each other and to the subunit-binding and catalytic domain, and facilitate the intramolecular coupling of active sites in the complex. A deletion of 12 of the 32 residues of the (Ala + Pro)-rich segment of an acetyltransferase containing only one lipoyl domain was made by deleting the corresponding segment of the aceF gene. A pyruvate dehydrogenase complex was still produced and the catalytic activity of the restructured complex, including active-site coupling, was not detectably impaired.

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