Pang Linlin, Niu Weijing, Duan Yuwei, Huo Liujie, Li Aiying, Wu Jiequn, Zhang Youming, Bian Xiaoying, Zhong Guannan
Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.
Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014, China.
Eng Microbiol. 2021 Nov 25;2(1):100007. doi: 10.1016/j.engmic.2021.100007. eCollection 2022 Mar.
characterization experiments revealed the formations of 3-(-2'-aminocyclopropyl)alanine ((3-Acp)Ala) and 3-(-2'-nitrocyclopropyl)alanine ((3-Ncp)Ala) are originated via two homologous proteins, BelK and HrmI, which regioselectively catalyze the Nε-oxygenation of l-lysine. The two enzymes belong to the emerging heme-oxygenase-like diiron oxidase and oxygenase (HDO) superfamily and the catalytic center of BelK is validated by homology modeling and site-directed mutations. Based on the characterization, the biosynthetic pathways of (3-Acp)Ala and (3-Ncp)Ala are proposed.
表征实验表明，3-（-2'-氨基环丙基）丙氨酸（（3-Acp）Ala）和3-（-2'-硝基环丙基）丙氨酸（（3-Ncp）Ala）的形成是通过两种同源蛋白BelK和HrmI实现的，这两种蛋白区域选择性地催化L-赖氨酸的Nε-氧化。这两种酶属于新兴的类血红素加氧酶双铁氧化酶和加氧酶（HDO）超家族，BelK的催化中心通过同源建模和定点突变得到验证。基于表征结果，提出了（3-Acp）Ala和（3-Ncp）Ala的生物合成途径。
