First and second sphere interactions accelerate non-native N-alkylation catalysis by the thermostable, methanol-tolerant B12-dependent enzyme MtaC.
First and second sphere interactions accelerate non-native N-alkylation catalysis by the thermostable, methanol-tolerant B12-dependent enzyme MtaC.
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第一球体和第二球体相互作用通过热稳定、耐甲醇的 B12 依赖性酶 MtaC 加速非天然 N-烷基化催化。
DOI：
10.1039/d3cc01071f
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发表时间：
2023
期刊：
影响因子：
--
通讯作者：
Lewis,JaredC
中科院分区：
文献类型：
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作者：
Kumar,Amardeep;Yang,Xinhang;Li,Jianbin;Lewis,JaredC
类咕啉蛋白 MtaC 天然参与甲基转移酶催化，使用重氮乙酸乙酯催化苯胺的 N-烷基化。我们的结果表明，B12 支架对自由基化学和极性化学的天然偏好如何转化为非天然催化，这可以指导选择用于生物催化的 B12 依赖性蛋白质。 MtaC 还具有高热稳定性和有机溶剂耐受性，即使在纯甲醇中也能保持折叠状态。
The corrinoid protein MtaC, which is natively involved in methyl transferase catalysis, catalyzes N-alkylation of aniline using ethyl diazoacetate. Our results show how the native preference of B12 scaffolds for radical versus polar chemistry translates to non-native catalysis, which could guide selection of B12-dependent proteins for biocatalysis. MtaC also has high thermal stability and organic solvent tolerance, remaining folded even in pure methanol.