The surprising diversity of Δ6-desaturase substrates
The surprising diversity of Δ6-desaturase substrates
复制标题
DOI：
10.1042/bst0320086
复制
发表时间：
2004-02-01
影响因子：
3.9
通讯作者：
Legrand, P
中科院分区：
文献类型：
--
作者：
Guillou, H;D'Andrea, S;Legrand, P
编码Delta6-去饱和酶(FADS2)的单基因在哺乳动物中已被分离和鉴定。这种Delta6-clesaturase在多不饱和脂肪酸(PUFAs)的生物合成中起着重要作用。它催化生物合成长链多不饱和脂肪酸所需的亚油酸(C-18：2n-6)和α-亚麻酸(C-18：3n-3)的限速脱饱和反应。此外，最近的研究提供了强有力的证据表明，这种Delta6-去饱和酶也作用于n-6和n-3系列的24碳多不饱和脂肪酸。通过不同研究人员的互补工作，已经确定了这种Delta6-去饱和酶的另一种底物。这种Delta6-去饱和酶作用于饱和脂肪酸棕榈酸(C-16：0)，导致十六碳烯酸(C-16：1n-10)的生物合成。
A single gene encoding a Delta6-desaturase (FADS2) has been isolated and characterized in mammalian species. This Delta6-clesaturase plays a major role in the biosynthesis of PUFAs (polyunsaturated fatty acids). it catalyses the rate-limiting desaturation of linoleic acid (C-18:2 n - 6) and alpha-linolenic acid (C-18:3 n - 3) required for the biosynthesis of long-chain PUFAs. Moreover, recent studies have provided strong evidence that this Delta6-desaturase also acts on 24-carbon PUFAs of both the n - 6 and n - 3 series. Another substrate of this Delta6-desaturase has been identified through complementary works from different investigators. This Delta6-desaturase acts on a saturated fatty acid, palmitic acid (C-16:0), leading to the newly characterized biosynthesis of hexadecenoic acid (C-16:1 n - 10) or sapienate.