Two lipoyl domains in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis.
A fragment of DNA incorporating the gene, pdhC, that encodes the dihydrolipoamide acetyltransferase (E2) chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis was cloned and a DNA sequence of 2360 bp was determined. The pdhC gene (1620 bp) corresponds to an E2 chain of 539 amino acid residues, Mr 56,466, comprising two lipoyl domains, a peripheral subunit-binding domain and an acetyltransferase domain, linked together by regions of polypeptide chain rich in alanine, proline and charged amino acids. The S. faecalis E2 chain differs in the number of its lipoyl domains from the E2 chains of all bacterial pyruvate dehydrogenase complexes hitherto described.
Allen
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Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, UK.
Perham
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D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D008969:Molecular Sequence Data; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D004269:DNA, Bacterial; D011768:Pyruvate Dehydrogenase Complex; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase