一种硼酸酶

IF 42.8 1区 化学 Q1 CHEMISTRY, PHYSICAL Nature Catalysis Pub Date : 2024-05-29 DOI:10.1038/s41929-024-01176-7
Francesco Zamberlan
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引用次数: 0

摘要

研究人员最初在乳球菌多药抗性调节蛋白二聚体疏水腔的不同位置加入了 pBoF,以提供不同的化学环境,使硼酸能够加速外消旋安息香和羟胺之间的缩合反应,生成相应的肟。在第 89 位插入 pBoF 可催化反应并区分底物的对映体,从而产生硼酸依赖性肟合成酶(BOS)。研究小组提出,蛋白质环境导致了一种对映体的优先转化,使羟基酮产物的动力学解析成为可能。最初的丙氨酸扫描发现近端残基对催化活性至关重要,而进一步的定向进化则发现了 BOS_EHL,一种含有 Phe93Glu、Met8His 和 Ala92Leu 突变的变体:这种变体的 E 值(两种对映体的催化速率之比)高达 146,观察到的速率常数增加了 33 倍,而其反应在接近 50% 转化率时停止,原因是消耗了安息香底物的首选对映体。在调查了安息香芳基环的范围后,研究人员收集了有关 BOS_EHL 的高分辨率质谱、11B NMR 和 X 射线晶体学数据,以了解其作用机制。这些数据证实,硼酸催化作用是通过羟基定向硼酸在水中的既定机制进行的。催化位点与蛋白质支架之间的这种相互作用对于所展示的新自然立体选择性酶反应性至关重要,这使得生物催化调色板可以扩展到非生物化学,例如这种立体选择性、可编程的硼生物催化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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A boronic enzyme
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来源期刊
Nature Catalysis
Nature Catalysis Chemical Engineering-Bioengineering
CiteScore
52.10
自引率
1.10%
发文量
140
期刊介绍: Nature Catalysis serves as a platform for researchers across chemistry and related fields, focusing on homogeneous catalysis, heterogeneous catalysis, and biocatalysts, encompassing both fundamental and applied studies. With a particular emphasis on advancing sustainable industries and processes, the journal provides comprehensive coverage of catalysis research, appealing to scientists, engineers, and researchers in academia and industry. Maintaining the high standards of the Nature brand, Nature Catalysis boasts a dedicated team of professional editors, rigorous peer-review processes, and swift publication times, ensuring editorial independence and quality. The journal publishes work spanning heterogeneous catalysis, homogeneous catalysis, and biocatalysis, covering areas such as catalytic synthesis, mechanisms, characterization, computational studies, nanoparticle catalysis, electrocatalysis, photocatalysis, environmental catalysis, asymmetric catalysis, and various forms of organocatalysis.
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