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首页> 外文期刊>Biochemistry >The 1.85 Å Structure of an 8R-Lipoxygenase Suggests a General Model for Lipoxygenase Product Specificity
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The 1.85 Å Structure of an 8R-Lipoxygenase Suggests a General Model for Lipoxygenase Product Specificity

机译：1.85Å8R-脂氧合酶的结构表明脂氧合酶产物特异性的通用模型

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摘要

Lipoxygenases (LOX) play pivotal roles in the biosynthesis of leukotrienes and other biologicallynactive eicosanoids derived from arachidonic acid. A mechanistic understanding of substrate recognition,nwhen lipoxygenases that recognize the same substrate generate different products, can be used to help guidenthe design of enzyme-specific inhibitors. We report here the 1.85A ° resolution structure of an 8R-lipoxygenasenfrom Plexaura homomalla, an enzyme with a sequence ∼40% identical to that of human 5-LOX. The structurenreveals a U-shaped channel, defined by invariant amino acids, that would allow substrate access to thencatalytic iron. We demonstrate that mutations within the channel significantly impact enzyme activity andnpropose a novel model for substrate binding potentially applicable to other members of this enzyme family.
机译：脂氧合酶（LOX）在白三烯和其他衍生自花生四烯酸的生物活性类花生酸的生物合成中起关键作用。当识别相同底物的脂氧合酶产生不同的产物时，对底物识别的机械理解可用于帮助指导酶特异性抑制剂的设计。我们在这里报告了来自Plexaura homomalla的8R-脂加氧酶的1.85A°分辨率结构，该酶的序列与人5-LOX的序列约40％相同。该结构揭示了一个由不变氨基酸定义的U形通道，该通道将允许底物接近随后的催化铁。我们证明了通道内的突变会显着影响酶的活性，并提出了一种新的底物结合模型，可能适用于该酶家族的其他成员。

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