ELOVL7 超长链脂肪酸延长酶的生化特性分析。

Biochemical characterization of the very long-chain fatty acid elongase ELOVL7.

机构信息

Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo, Japan.

出版信息

FEBS Lett. 2011 Oct 20;585(20):3337-41. doi: 10.1016/j.febslet.2011.09.024. Epub 2011 Sep 22.

DOI:10.1016/j.febslet.2011.09.024

PMID:21959040

Abstract

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 μM range. We also found that progression of the VLCFA cycle enhances ELOVL7 activity.

摘要

长链脂肪酸（VLCFAs）具有多种生理功能，与许多疾病有关。VLCFA 延伸的关键步骤是由延伸酶家族成员 ELOVLs 催化的。哺乳动物有七种 ELOVLs（ELOVL1-7），但没有一种被纯化和分析过。在本研究中，我们纯化了 ELOVL7，并通过将其重新组装到质体中测量了它的活性。纯化的 ELOVL7 对具有 18 个碳链长度的酰基辅酶 A 表现出很高的活性。对 C18:3(n-3)-CoA 和丙二酰辅酶 A 的计算 K(m) 值均在μM 范围内。我们还发现，VLCFA 循环的进展增强了 ELOVL7 的活性。