Article
Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli.
The Biochemical journal - 1 Oct 1990
Ali S T, Guest J R
Abstract excerpt
The dihydrolipoamide acetyltransferase subunit (E2p) of the pyruvate dehydrogenase complex of Escherichia coli has three highly conserved and tandemly repeated lipoyl domains, each containing approx. 80 amino acid residues. These domains are covalently modified with lipoyl groups bound in amide linkage to the N6-amino groups of specific lysine residues, and the cofactors perform essential roles in the formation...
Topics
- Acetylation
- Acetyltransferases
- Amino Acid Sequence
- Ammonium Sulfate
- Dihydrolipoyllysine-Residue Acetyltransferase
- Escherichia coli
- Gene Expression
- Hot Temperature
- Hydrogen-Ion Concentration
- Isoelectric Point