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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Redesigning the monovalent cation specificity of an enzyme
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Redesigning the monovalent cation specificity of an enzyme

机译：重新设计酶的单价阳离子特异性

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摘要

Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K~+, whereas a few of them show preferential activation by Na~+. The monovalent cation specificity of these enzymes remains elusive in molecular terms and has not been reengineered by site-directed mutagenesis. Here we demonstrate that thrombin, a Na~+-activated allosteric enzyme involved in vertebrate blood clotting, can be converted into a K~+-specific enzyme by redesigning a loop that shapes the entrance to the cation-binding site. The conversion, however, does not result into a K~+-activated enzyme.
机译：单价阳离子激活的酶在植物和动物界中占有重要地位。这些酶中的大多数被K〜+特异性激活，而少数酶则显示出Na〜+优先激活。这些酶的单价阳离子特异性在分子上仍然难以捉摸，并且尚未通过定点诱变进行重新设计。在这里，我们证明了凝血酶是一种参与脊椎动物血液凝固的Na〜+激活的变构酶，可以通过重新设计形成阳离子结合位点入口的环将其转化为K〜+特异性酶。然而，该转化不会导致K +活化的酶。

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