Abstract
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 Nε-nitration 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 first proposed.
Supplementary materials
Title
Supporting Information
Description
Full experimental details, in silico analysis, SDS-PAGE, homology modeling, MS data, NMR spectra and sequence alignments.
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