Enzymological and physiological consequences of restructuring the lipoyl domain content of the pyruvate dehydrogenase complex of Escherichia coli

The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK 2 Author for correspondence: John R. Guest. Tel: + 44 114 282 4406/3. Fax: +44 114 272 8697. ABSTRACT The core-forming lipoate acetyltransferase (E2p) subu...

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Veröffentlicht in:	Microbiology (Society for General Microbiology) 1997-02, Vol.143 (2), p.457-466
Hauptverfasser:	Guest, John R, Attwood, Margaret M, Machado, Rosane S, Matqi, Khalil Y, Shaw, John E, Turner, Sarah L
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetyltransferases - genetics Acetyltransferases - metabolism Bacteriology Biological and medical sciences Biotechnology Dihydrolipoyllysine-Residue Acetyltransferase Escherichia coli Escherichia coli - enzymology Escherichia coli - growth & development Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Industrial Microbiology Metabolism. Enzymes Methods. Procedures. Technologies Microbiology Operon - genetics Protein Conformation Protein Engineering Pyruvate Dehydrogenase Complex - genetics Pyruvate Dehydrogenase Complex - metabolism Repetitive Sequences, Nucleic Acid Thioctic Acid
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