2 LIPOYL DOMAINS IN THE DIHYDROLIPOAMIDE ACETYLTRANSFERASE CHAIN OF THE PYRUVATE-DEHYDROGENASE MULTIENZYME COMPLEX OF STREPTOCOCCUS-FAECALIS

被引：23

作者：

ALLEN, AG ^{[1
]}

PERHAM, RN ^{[1
]}

机构：

[1] UNIV CAMBRIDGE, CAMBRIDGE CTR MOLEC RECOGNIT, DEPT BIOCHEM, TENNIS COURT RD, CAMBRIDGE CB2 1QW, ENGLAND

来源：

FEBS LETTERS | 1991年 / 287卷 / 1-2期

基金：

英国惠康基金;

关键词：

PYRUVATE DEHYDROGENASE COMPLEX; LIPOYL DOMAIN; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; DNA SEQUENCE; STREPTOCOCCUS-FAECALIS;

D O I：

10.1016/0014-5793(91)80052-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：206 / 210

页数：5

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