Two lipoyl domains in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis

FEBS Letters

Allen, Andrew G.¹  Perham, Richard N.¹ 

[1] Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK

关键词: Pyruvate dehydrogenase complex;    Lipoyl domain;    Dihydrolipoamide acetyltransferase: DNA sequence: Streptococcus faecalis;    PDH;    pyruvate dehydrogenase;    SDS;    sodium dodecylsulphate;   

DOI  :  10.1016/0014-5793(91)80052-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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. M _r 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.

【 授权许可】

Unknown