A mutant pyruvate dehydrogenase complex of Escherichia coli deleted in the (alanine + proline)-rich region of the acetyltransferase component.
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.
Miles
J S
JS
Guest
J R
JR
Radford
S E
SE
Perham
R N
RN
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
D001426:Bacterial Proteins; D011768:Pyruvate Dehydrogenase Complex; D011392:Proline; D000123:Acetyltransferases; D000409:Alanine