Autor: |
Linlin Pang, Weijing Niu, Yuwei Duan, Liujie Huo, Aiying Li, Jiequn Wu, Youming Zhang, Xiaoying Bian, Guannan Zhong |
Jazyk: |
angličtina |
Rok vydání: |
2022 |
Předmět: |
|
Zdroj: |
Engineering Microbiology, Vol 2, Iss 1, Pp 100007- (2022) |
Druh dokumentu: |
article |
ISSN: |
2667-3703 |
DOI: |
10.1016/j.engmic.2021.100007 |
Popis: |
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 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 in vitro characterization, the biosynthetic pathways of (3-Acp)Ala and (3-Ncp)Ala are proposed. |
Databáze: |
Directory of Open Access Journals |
Externí odkaz: |
|