Component X of mammalian pyruvate dehydrogenase complex: Structural and functional relationship to the lipoate acetyltransferase (E2) component

FEBS Letters

Neagle, James¹  Dunbar, Bryan²  Lindsay, J.Gordon¹  De Marcucci, Olga¹ 

[1] Department of Biochemistry, University of Glasgow, Glasgow G12 8QQ, Scotland;Department of Biochemistry, University of Aberdeen, Aberdeen, AB9 1AS, Scotland

关键词: Pyruvate dehydrogenase complex;    Component X;    Lipoyl domain;    Homology;    Component E2;    (Bovine heart);   

DOI  :  10.1016/0014-5793(89)80919-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The lipoate acetyltransferase (E2, M _r 70 000) and protein X (M _r 51 000) subunits of the bovine pyruvate dehydrogenase multienzyme complex (PDC) core assembly are antigenically distinct polypeptides. However comparison of the N-terminal amino acid sequence of the E2 and X polypeptides reveals significant homology between the two components. Selective tryptic release of the ¹⁴C-labelled acetylated lipoyl domains of E2 and protein X from native PDC generates stable, radiolabelled 34 and 15 kDa fragments, respectively. Thus, in contrast to E2 which contains two tandemly-arranged lipoyl domains, protein X appears to contain only a single lipoyl domain located at its N-terminus.

【 授权许可】

Unknown