Biochemical characterization of the very long-chain fatty acid elongase ELOVL7
Biochemical characterization of the very long-chain fatty acid elongase ELOVL7
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DOI：
10.1016/j.febslet.2011.09.024
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发表时间：
2011-10-20
期刊：
影响因子：
3.5
通讯作者：
Kihara, Akio
中科院分区：
文献类型：
--
作者：
Naganuma, Tatsuro;Sato, Yuichiro;Kihara, Akio
极长链脂肪酸（VLCFA）具有多种生理功能，并与许多疾病有关。VLCFA延伸的关键步骤是由延伸酶家族的成员催化的。哺乳动物有7个HPVL（HPVL 1 -7），但没有一个被纯化和分析。在目前的研究中，我们纯化了HPVL 7，并通过将其重组到脂蛋白体中来测量其活性。纯化后的BL 2 V17对C18碳链的酰基辅酶A具有较高的活性。计算的C18：3（n-3）-CoA和丙二酰-CoA的K（m）值均在μ M范围内。我们还发现，VLCFA循环的进展增强了CD 3VL 7活性。(C)2011年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Very long-chain fatty acids (VLCFAs) have a variety of physiological functions and are related to numerous disorders. The key step of VLCFA elongation is catalyzed by members of the elongase family, ELOVLs. Mammals have seven ELOVLs (ELOVL1-7), yet none of them has been purified and analyzed. In the presented study we purified ELOVL7 and measured its activity by reconstituting it into proteoliposomes. Purified ELOVL7 exhibited high activity toward acyl-CoAs with C18 carbon chain length. The calculated K(m) values toward C18: 3(n-3)-CoA and malonyl-CoA were both in the mu M range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.