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首页> 外文期刊>Physical chemistry chemical physics: PCCP >Flipped regiospecificity in L434F mutant of 8-lipoxygenase
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Flipped regiospecificity in L434F mutant of 8-lipoxygenase

机译：L434F突变体在8-脂氧酶的突变体中翻转细胞分子

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摘要

Lipoxygenases are non-heme iron containing enzymes that catalyze oxygenation of poly-unsaturated fatty acids in different animal and plant species with extremely high regio- and stereospecificity. Nature employs 8-lipoxygenase to produce 8R-hydroperoxide from the oxygenation of arachidonic acid. A single-point L434F mutation of 8-lipoxygenase alters the regio- and stereospecificity of the final products, with a product ratio of 66 : 34 for 8R- and 12S-hydroperoxide, respectively. A molecular level explanation of this flipped regiospecificity is presented in this work on the basis of molecular dynamics simulations and transition network analysis of oxygen migration in the protein matrix. Phe434 is shown to exist in two conformations, the so-called open and closed conformations. In the closed conformation, the phenyl group of Phe434 shields the C8 site of the substrate, thereby preventing access of the oxygen molecule to this site, which leads to a quenching of the 8R-product. On the other hand, both closed and open conformations of Phe434 allow the oxygen molecule to approach the pro-Sface of the C12 site of the substrate, which enhances the propensity of the 12S-hydroperoxide.
机译：脂氧合酶是含有酶非血红素铁的该多不饱和脂肪酸在不同的动物和植物物种具有极高区域选择性和立体定向性催化氧化。性质采用8脂氧合酶以从花生四烯酸的氧合产生8R-氢过氧化物。分别为34和8R- 12S-氢过氧化物，：8脂氧合酶改变了区域选择性和立体定向性的最终产品，具有66的产物比率为单点L434F突变。这个翻转区域专一的分子水平说明被呈现在分子动力学模拟和蛋白质基质氧迁移的转移网络分析的基础上，这项工作。 Phe434被示出为存在于两种构象，即所谓的打开和闭合的构象。在闭合构象，Phe434的苯基屏蔽基板的C8部位，从而防止此位点，其通向8R副产物的骤冷的氧分子的访问。在另一方面，Phe434的两个封闭式和开放式构象使氧分子接近衬底，这增强了12S-氢过氧化物的倾向的部位C12的促Sface。

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