Abstract
AbstractHormaomycins and belactosins are peptide natural products that contain unusual cyclopropane moieties. Bioinformatics analysis of the corresponding biosynthetic gene clusters showed that two conserved genes, hrmI/belK and hrmJ/belL, were potential candidates for catalyzing cyclopropanation. Using in vivo and in vitro assays, the functions of HrmI/BelK and HrmJ/BelL were established. HrmI and BelK, which are heme oxygenase‐like dinuclear iron enzymes, catalyze oxidation of the ϵ‐amino group of l‐lysine to afford l‐6‐nitronorleucine. Subsequently, HrmJ and BelL, which are iron‐ and α‐ketoglutarate‐dependent oxygenases, effectively convert l‐6‐nitronorleucine into 3‐(trans‐2‐nitrocyclopropyl)‐alanine through C4−C6 bond installation. These observations disclose a novel pathway of cyclopropane ring construction and exemplify the new chemistry involving metalloenzymes in natural product biosynthesis.
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