FEBS Letters | |
Component X of mammalian pyruvate dehydrogenase complex: Structural and functional relationship to the lipoate acetyltransferase (E2) component | |
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
【 预 览 】
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RO201912020292359ZK.pdf | 559KB | download |