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无氧性ergothioneine生物合成的结构和机制基础

Florian Leisinger¹, Reto Burn¹, Marcel Meury¹

¹Department for Chemistry , University of Basel , Mattenstrasse 24a, BPR 1002 , 4056 , Basel , Switzerland.

Journal of the American Chemical Society

|April 4, 2019

概括

对于细胞氧化还原平衡至关重要的ergothioneine是由无氧细菌通过氧气独立途径合成的. 研究人员阐明了EanB酶的晶体结构,揭示了它创造不寻常的碳硫键的机制.

科学领域:

生物化学生物化学
微生物学微生物学
结构生物学结构生物学

背景情况:

欧戈氨酸以其在保护细胞免受活性氧物种的作用而闻名.
最近的发现表明,厌氧微生物利用无氧化学物质合成埃尔戈氨酸,这表明它们具有更广泛的生理作用.
这凸显了在不同条件下理解欧戈氨酸生物合成的必要性.

研究的目的:

为了确定无氧性ergothioneine生物合成酶EanB的晶体结构.
阐明EanB的催化机制,重点关注不寻常的C-S键形成.
研究EanB的进化保存及其功能.

主要方法:

进行X射线晶体学,以获得EanB.的晶体结构.
酶动力学研究以了解反应速率和机制.
生物信息分析以识别EanB同类物和保存的活性部位特征.

主要成果:

从Chlorobium limicola中确定了EanB的晶体结构.
这种酶被证明可以催化N-α-trimethyl histidine的氧化硫化.
结构和运动数据为CS债券形成的机制提供了洞察力.
在各种细菌EanB同类物体中确定了保存的活性部位残留物.

结论:

通过EanB揭示了无氧欧戈氨酸生物合成的结构和机制.
这种酶促进了一种不寻常的氧化硫化反应.
保存的特征表明这种途径在细菌中很普遍,可能会影响各种异环化合物代谢.

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