title: A mutant pyruvate dehydrogenase complex of Escherichia coli deleted in the (alanine + proline)-rich region of the acetyltransferase component.
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.
authors.forename: J S
authors.initials: JS
authors.lastname: Miles
authors.forename: J R
authors.initials: JR
authors.lastname: Guest
authors.forename: S E
authors.initials: SE
authors.lastname: Radford
authors.forename: R N
authors.initials: RN
authors.lastname: Perham
mesh_terms: D000123:Acetyltransferases / Q000235:genetics / Q000378:metabolism; D000409:Alanine; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D011392:Proline; D011487:Protein Conformation; D011768:Pyruvate Dehydrogenase Complex / Q000235:genetics* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D011768:Pyruvate Dehydrogenase Complex; D011392:Proline; D000123:Acetyltransferases; D000409:Alanine