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Two lipoyl domains in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis
Author(s) -
Allen Andrew G.,
Perham Richard N.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80052-5
Subject(s) - pyruvate dehydrogenase complex , dihydrolipoyl transacetylase , dihydrolipoamide dehydrogenase , biochemistry , dehydrogenase , acetyltransferase , protein subunit , biology , gene , branched chain alpha keto acid dehydrogenase complex , pyruvate dehydrogenase phosphatase , chemistry , microbiology and biotechnology , enzyme , acetylation
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.