Deng Zhiwei, Yuan Zhenbo, Luo Zhengshan, Rao Yijian
Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, China.
Eng Microbiol. 2025 Jan 1;5(1):100188. doi: 10.1016/j.engmic.2024.100188. eCollection 2025 Mar.
Owing to their diverse coordination patterns and catalytic mechanisms, non-heme iron-dependent dioxygenases catalyze a variety of biochemical reactions involved in the synthesis of numerous natural products and valuable compounds. Recently, we discovered a novel and atypical non-heme iron-dependent dioxygenase, BTG13, that features a unique coordination center consisting of four histidines and a carboxylated lysine (Kcx). This enzyme catalyzes the C-C bond cleavage of anthraquinone through two unconventional steps, with modified Kcx playing a key role in facilitating these processes, as revealed by molecular dynamics simulations and quantum chemical calculations. Phylogenetic analyses and other studies suggest that BTG13-related metalloenzymes are widespread in various organisms. Here, we highlight the significance of this new class of non-heme iron-dependent oxygenases and their potential as novel tools for practical applications in synthetic biology.
由于其多样的配位模式和催化机制，非血红素铁依赖性双加氧酶催化多种参与众多天然产物和有价值化合物合成的生化反应。最近，我们发现了一种新型非典型非血红素铁依赖性双加氧酶BTG13，其具有由四个组氨酸和一个羧化赖氨酸（Kcx）组成的独特配位中心。该酶通过两个非常规步骤催化蒽醌的碳 - 碳键裂解，分子动力学模拟和量子化学计算表明，修饰后的Kcx在促进这些过程中起关键作用。系统发育分析和其他研究表明，与BTG13相关的金属酶广泛存在于各种生物体中。在此，我们强调这类新型非血红素铁依赖性加氧酶的重要性及其作为合成生物学实际应用新工具的潜力。
