The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component.

摘要: The nucleotide sequence of the aceF gene, which encodes dihydrolipoamide acetyltransferase component (E2) pyruvate dehydrogenase complex Escherichia coli K12, has been determined using dideoxy chain-termination method. gene comprises 1887 base pairs (629 codons excluding initiation codon AUG); it is preceded by a short intercistronic segment 14 containing good ribosomal binding site, and followed closely potential rho-independent terminator. results extend 1980 previously sequenced 3780 structural (aceE) (E1) they confirm that aceE are proximal distal genes ace operon. The amino terminus, carboxy-terminal acid composition subunit predicted from in excellent agreement with previous studies purified protein. molecular weight (Mr= 65959) confirms experimental values derived sedimentation equilibrium analysis indicates higher (78 000–89 000) have reported due to unusual features protein lead anomalous mobilities during sodium dodecyl sulphate/polyacrylamide gel electrophoresis filtration. primary structure fully supports conclusions, based on limited tryptic proteolysis, possesses two heterologous domains: lipoyl domain catalytic domain. corresponds amino-terminal It acidic contains three remarkably homologous repeating units approximately 100 acids, each possessing site region characteristically rich alanine proline residues. occupies most residual polypeptide segment.