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首页> 外文期刊>Journal of Molecular Biochemistry >Insights into the structure and 3D spatial arrangement of the b-ketoacyl carrier protein synthases
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Insights into the structure and 3D spatial arrangement of the b-ketoacyl carrier protein synthases

机译：洞察b-酮酰基载体蛋白合酶的结构和3D空间排列

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The b-ketoacyl carrier protein synthases (the KAS enzymes) are key enzymes that can be used as potential anti-Plasmodium drug targets. In bacteria, three KAS enzymes have been identified (KAS I, KAS II and KAS III), whilst in Plasmodium a KAS I/II and KAS III enzyme has been reported. The protein has a total of four active sites, which have been found to be different to each other, rather than four copies of the same active site. The active sites differ not only in the type of interaction they establish with the ligand, but, in the case of Cerulenin as a ligand, the active sites of the KAS I/II enzyme also differ in the number of residues involved in the ligand protein interaction. This is very interesting biochemically, because these differences imply that the affinity of each active site for binding to the ligand might be different as well.
机译：b-酮酰基载体蛋白合成酶（KAS酶）是可用作潜在抗疟原虫药物靶标的关键酶。在细菌中，已鉴定出三种KAS酶（KAS I，KAS II和KAS III），而在疟原虫中，已报道了KAS I / II和KAS III酶。该蛋白质共有四个活性位点，发现它们彼此不同，而不是同一活性位点的四个拷贝。活性位点不仅在它们与配体建立的相互作用类型上不同，而且在天青素作为配体的情况下，KAS I / II酶的活性位点在配体蛋白中涉及的残基数上也不同相互作用。这在生化上是非常有趣的，因为这些差异意味着每个活性位点与配体结合的亲和力也可能不同。

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