EXPRESSION AND LIPOYLATION IN ESCHERICHIA-COLI OF THE INNER LIPOYL DOMAIN OF THE E2-COMPONENT OF THE HUMAN PYRUVATE-DEHYDROGENASE COMPLEX

被引：42
作者：
QUINN, J
DIAMOND, AG
MASTERS, AK
BROOKFIELD, DE
WALLIS, NG
YEAMAN, SJ
机构：
[1] UNIV NEWCASTLE UPON TYNE, SCH MED, DEPT BIOCHEM & GENET, NEWCASTLE UPON TYNE NE2 4HH, ENGLAND
[2] UNIV NEWCASTLE UPON TYNE, SCH MED, DEPT IMMUNOL & MED, NEWCASTLE UPON TYNE NE2 4HH, ENGLAND
[3] UNIV SHEFFIELD, DEPT MOLEC BIOL & BIOTECHNOL, SHEFFIELD S10 2UH, ENGLAND
[4] UNIV CAMBRIDGE, DEPT BIOCHEM, CAMBRIDGE CTR MOLEC RECOGNIT, CAMBRIDGE CB2 1QW, ENGLAND
来源：
BIOCHEMICAL JOURNAL | 1993年 / 289卷
基金：
英国惠康基金;
关键词：
D O I：
10.1042/bj2890081
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：
The dihydrolipoamide acetyltransferase subunit (E2p) of mammalian pyruvate dehydrogenase complex has two highly conserved lipoyl domains each modified with a lipoyl cofactor bound in amide linkage to a specific lysine residue. A sub-gene encoding the inner lipoyl domain of human E2p has been over-expressed in Escherichia coli. Two forms of the domain have been purified, corresponding to lipoylated and non-lipoylated species. The apo-domain can be lipoylated in vitro with partially purified E. coli lipoate protein ligase, and the lipoylated domain can be reductively acetylated by human E1p (pyruvate dehydrogenase). Availability of the two forms will now allow detailed biochemical and structural studies of the human lipoyl domains.
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收藏
页码：81 / 85
页数：5
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