De novo design of catalytic proteins
De novo design of catalytic proteins
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DOI：
10.1073/pnas.0404387101
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发表时间：
2004-08-10
影响因子：
11.1
通讯作者：
DeGrado, WF
中科院分区：
文献类型：
--
作者：
Kaplan, J;DeGrado, WF
催化蛋白的从头设计为我们对酶功能的理解提供了严格的测试，同时为新型催化剂的设计奠定了基础。在这里，我们描述了O-2依赖性酚氧化酶的结构，序列和活性的设计从第一原则。该蛋白催化4-氨基苯酚的双电子氧化（k（cat）/K-m = 1，500 M（-1.）min（-1））转化为相应的醌单亚胺。催化效率对蛋白质中甲基大小的变化敏感，说明了设计的特异性。
The de novo design of catalytic proteins provides a stringent test of our understanding of enzyme function, while simultaneously laying the groundwork for the design of novel catalysts. Here we describe the design of an O-2-dependent phenol oxidase whose structure, sequence, and activity are designed from first principles. The protein catalyzes the two-electron oxidation of 4-aminophenol (k(cat)/K-m = 1,500 M(-1.)min(-1)) to the corresponding quinone monoimine by using a diiron cofactor. The catalytic efficiency is sensitive to changes of the size of a methyl group in the protein, illustrating the specificity of the design.