In vitro characterization of a nitro-forming oxygenase involved in 3-(trans-2’-aminocyclopropyl)alanine biosynthesis  

作　　者：Linlin Pang Weijing Niu Yuwei Duan Liujie Huo Aiying Li Jiequn Wu Youming Zhang Xiaoying Bian Guannan Zhong 

机构地区：[1]Helmholtz International Lab for AntiInfectives,Shandong University-Helmholtz Institute of Biotechnology,State Key Laboratory of Microbial Technology,Shandong University,Qingdao 266237,China [2]Suzhou Institute of Shandong University,Suzhou 215123,China [3]Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals,College of Pharmaceutical Sciences,Zhejiang University of Technology,Hangzhou 310014,China

出　　处：《Engineering Microbiology》2022年第1期35-38,共4页工程微生物学（英文）

基　　金：supported by the National Key R&D Program of China(2019YFA0905700);the National Natural Science Foundation of China(21907057,32070060);the Shan-dong Provincial Natural Science Foundation,China(ZR2019JQ11,ZR2019ZD18);the Natural Science Foundation of Jiangsu Province,China(BK20190201);the 111 project(B16030),the Youth Interdisci-plinary Innovative Research Group(2020QNQT009);the Future Plan for Young Scholars,and the Fundamental Research Funds(2019GN032)of Shandong University.

摘　　要：In vitro characterization experiments revealed the formations of 3-(trans-2’-aminocyclopropyl)alanine((3-Acp)Ala)and 3-(trans-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 emerg-ing 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 in vitro characterization,the biosyn-thetic pathways of(3-Acp)Ala and(3-Ncp)Ala are proposed.

关 键 词：Nitro-forming oxygenase HDO superfamily protein Belactosin A Hormaomycin Cyclopropyl ring 

分 类 号：Q93[生物学—微生物学]