characterization of a nitro-forming oxygenase involved in 3-(-2'-aminocyclopropyl)alanine biosynthesis.

Eng Microbiol

Helmholtz International Lab for AntiInfectives, Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China.

Published: March 2022

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11611017PMC
http://dx.doi.org/10.1016/j.engmic.2021.100007DOI Listing

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