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

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

Engineering Microbiology (Mar 2022)

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

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

Affiliations

Linlin Pang: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Weijing Niu: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Yuwei Duan: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Liujie Huo: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Aiying Li: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Jiequn Wu: Collaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, College of Pharmaceutical Sciences, Zhejiang University of Technology, Hangzhou 310014, China
Youming Zhang: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China
Xiaoying Bian: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China; Corresponding authors.
Guannan Zhong: Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China; Suzhou Institute of Shandong University, Suzhou 215123, China; Corresponding authors.

Journal volume & issue: Vol. 2, no. 1
p. 100007

Abstract

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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.

Published in Engineering Microbiology

ISSN: 2667-3703 (Online)
Publisher: Elsevier
Country of publisher: Netherlands
LCC subjects: Technology: Chemical technology: Biotechnology; Science: Microbiology
Website: https://www.sciencedirect.com/journal/engineering-microbiology

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