Conversing proteinaceous enzyme behavior into nanomaterials is intriguing academically, but the threshold from mimicry to accessing sophisticated biological entities has not yet been crossed. Herein, we disclosed the pan-glycoside hydrolases-like (p-GHs-like) activities of Cu₃P and Cu₂O nanoparticles and decently confirmed their consistent catalytic mechanism as natural glycoside hydrolase, that is, the precise bond breaking, anomeric carbon configuration and catalytic attack mode. We then introduced p-GHs-like NPs into Escherichia coli to establish a feedback regulatory model for the β-D-glucuronidase (expressed by uidA) that was initially expressed in trace amounts. An upregulation of uidA from 72 to 1000 counts was induced by the p-GHs-like activities via pre-released β-glucuronides derivatives, further contributing to 1–2 orders enhancement of the enzyme production. We unearthed the specific catalytic mechanism to unlock a black box of enzyme-like inorganic feedback on the natural enzyme synthesis process, pushing mimicry leaped to physiological behavior.

将蛋白质酶行为转化为纳米材料在学术上很有趣，但尚未跨越从模仿到获取复杂生物实体的门槛。_{在此，我们公开了 Cu 3} P 和 Cu ₂ O 纳米粒子的类泛糖苷水解酶 (p-GHs-like) 活性，并恰当地证实了它们与天然糖苷水解酶一致的催化机制，即精确的键断裂、异头碳配置和催化攻击模式。然后，我们将 p-GHs 样 NPs 引入大肠杆菌中，以建立 β- D 的反馈调节模型。- 最初以微量表达的葡萄糖醛酸酶（由 uidA 表达）。p-GHs 样活性通过预释放的 β-葡糖苷酸衍生物诱导 uidA 从 72 计数上调到 1000 计数，进一步促进酶产量提高 1-2 个数量级。我们发掘了特定的催化机制，打开了天然酶合成过程中类酶无机反馈的黑匣子，推动拟态跃升为生理行为。