Endothelial nitric oxide synthase is myristylated.
Endothelial nitric oxide synthase is myristylated.
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内皮一氧化氮合酶被肉豆蔻酰化。
DOI：
10.1016/0014-5793(92)80816-y
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发表时间：
1992
期刊：
影响因子：
3.5
通讯作者：
Murad,F
中科院分区：
文献类型：
--
作者：
Pollock,JS;Klinghofer,V;Förstermann,U;Murad,F
内皮细胞中负责合成内皮衍生的松弛因子和/或一氧化氮的酶被描述为颗粒酶，而一氧化氮合酶的其他亚型则是可溶性酶。在这里，我们报道了内皮细胞代谢地将肉豆蔻酸盐(C14)而不是棕榈酸酯(C16)结合到一氧化氮合酶中。我们推测，内皮来源的一氧化氮合酶是一种颗粒酶，因为蛋白质的脂肪酸酰化直接或通过另一种膜结合蛋白将酶‘锚定’到膜上。
The enzyme responsible for the synthesis of endothelium‐derived relaxing factor and/or nitric oxide in the endothelium has been described as a particulate enzyme, whereas other isoforms of nitric oxide synthase are soluble enzymes. Here we are reporting that endothelial cells metabolically incorporate myristate (C14), but not palmitate (C16), into nitric oxide synthase. We are postulating that the endothelial‐derived nitric oxide synthase is a particulate enzyme because of the fatty acid acylation of the protein which ‘anchors’ the enzyme into the membrane either directly or via another membrane‐bound protein.