酶催化氧化降解的ergothioneine的氧化降解
Egor Y Nalivaiko1, Camille M Vasseur1, Florian P Seebeck1
1Department of Chemistry, University of Basel, Mattenstrasse 22, 4002, Basel, Switzerland.
Angewandte Chemie (International ed. in English)
|December 14, 2023
概括
这项研究确定了actinobacteria中的两种酶,这些酶降解了保护氧化应激的化合物ergothioneine. 这一发现表明,这些细菌积极调节它们的ergothioneine水平.
科学领域:
- 生物化学 生物化学
- 微生物学 微生物学
- 酶学 是一种酶学.
背景情况:
- 欧戈氨酸是一种含硫的代谢物,具有抗氧化特性,被植物和动物作为微量营养素吸收.
- 它通过与有害氧化剂 (如单氧氧和过氧化) 反应来保护细胞免受氧化应激.
研究的目的:
- 为了识别和描述负责氧化降解ergothioneine的actinobacteria中的酶.
- 为了阐明涉及到ergothioneine分解的生化途径和酶机制.
主要方法:
- 从actinobacteria进行酶净化和表征.
- 来自Thermocatellispora tengchongensis的欧戈氨酸二氧化酶的结晶学.
- 生物化学测试以确定酶活性和产品.
主要成果:
- 确定了两种合作的酶:一种依赖铁的二二氧化酶产生厄戈氨酸硫酸,一种依赖金属的脱硫酶产生Nα-trimethylhistidine和SO2.
- 埃尔戈氨酸二氧化酶的晶体结构与氨酸二氧化酶有相似之处,这表明一种保存的催化机制.
- 动因细菌拥有O2依赖的欧戈氨酸生物合成和降解的酶机制.
结论:
- 动氨基细菌可以通过专门的氧化降解途径积极管理其欧戈氨酸含量.
- 鉴定的酶提供了对微生物代谢和欧戈氨酸的生物学作用的见解.
- 这项研究突出了actinobacteria关于ergothioneine平衡的复杂生化能力.
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