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.
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.
