Article
Purification and cellular localization of wild type and mutated dihydrolipoyltransacetylases from Azotobacter vinelandii and Escherichia coli expressed in E. coli.
Biochimica et biophysica acta - 27 Mar 1992
Schulze E, Westphal A H, Veenhuis M, de Kok A
Abstract excerpt
Wild type dihydrolipoyltransacetylase(E2p)-components from the pyruvate dehydrogenase complex of A. vinelandii or E. coli, and mutants of A. vinelandii E2p with stepwise deletions of the lipoyl domains or the alanine- and proline-rich region between the binding and the catalytic domain have been overexpressed in E. coli TG2. The high expression of A. vinelandii wild type E2p (20% of cellular protein) and of a...
Topics
- Acetyltransferases
- Amino Acid Sequence
- Azotobacter vinelandii
- Base Sequence
- Cloning, Molecular
- Dihydrolipoyllysine-Residue Acetyltransferase
- Escherichia coli
- Gene Expression
- Genes, Bacterial
- Immunohistochemistry