A Completely De Novo ATPase from Combinatorial Protein Design
A Completely De Novo ATPase from Combinatorial Protein Design
复制标题
来自组合蛋白质设计的完全 De Novo ATP 酶
DOI：
10.1021/jacs.0c02954
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发表时间：
2020
影响因子：
15
通讯作者：
Hecht, Michael H.
中科院分区：
文献类型：
--
作者：
Wang, Michael S.;Hecht, Michael H.
我们对生物化学的理解是基于这样一种观察：所有的生命都来自于其他生命——正如巴斯德所说，所有的生命都是体外的。扩大我们的生化词汇的关键一步是概括生物催化使用非自然序列，而不是来自共同祖先。在这里，我们描述了一种完全水解ATP的酶。该蛋白被设计为缺乏β-薄片结构，并被镁竞争性地抑制，这两个特性与天然atp酶不同。
Our understanding of biological chemistry is shaped by the observation that all life comes from other life—as Pasteur put it,omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completelyde novothat hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases.