Tweezing the cofactor preference of gymnosperm pinene synthase
Tweezing the cofactor preference of gymnosperm pinene synthase
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DOI：
10.1080/09168451.2018.1459465
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发表时间：
2018-01-01
影响因子：
1.6
通讯作者：
Umeno, Daisuke
中科院分区：
文献类型：
--
作者：
Tashiro, Miki;Ono, Koyo;Umeno, Daisuke
裸子植物单萜脱氢酶的细胞活性由于其对锰的需求而大部分受损，锰在微生物细胞中是缺乏的。通过位点饱和诱变的残基相邻的金属结合谷氨酸，我们发现，蒎烯合酶是高度可变的，在这个位置，但大大改变了他们的金属结合的偏好，从而迅速提高异源宿主的细胞性能。
The cellular activities of gymnosperms monoterpene synthases are largely compromised due to their requirement for manganese, which is deficient in microbial cells. Through site-saturation mutagenesis of the residue adjacent to metal-binding glutamate, we found that pinene synthase is highly mutable at this position yet drastically alter their metal binding preference, thereby quickly improving the cellular performance in heterologous hosts.