Products Cited in Publications Worldwide A self‐sufficient β‐Methylarginine Biosynthetic Pathway in Planctomyces

A self‐sufficient β‐Methylarginine Biosynthetic Pathway in Planctomyces

Lara, Darwin Daniel; Zeng, Bryan Tianzuo; Hai, Yang

DOI:

Abstract

β-Methylamino acids (β-MAAs) enhance the bioactivity of natural products and possess intrinsic pharmacological properties as free amino acids. While the biosynthetic capacity for this class of noncanonical amino acids has been established in certain bacterial lineages such as Gammaproteobacteria and Actinomycetes, other bacterial phyla remain largely unexplored. Here we report the genome-mining guided discovery of a novel biosynthetic gene cluster capable of producing β-methylarginine, from the phylum Planctomycetes. We provide both in vivo and in vitro evidence that Planctomycetes employ a transaminase (PlaA) and a methyltransferase (PlaB) to synthesize this β-MAA. Unlike previously described β-methylarginine biosynthetic pathways, PlaA and PlaB function as a self-sufficient enzyme cascade that operates without the need for additional keto acid and amino acid partners. These findings expand the catalytic repertoire for β-MAAs biosynthesis and establish Planctomycetes as a new source of secondary metabolites discovery.

Keywords

β-methyl-arginine ; PLP-dependent enzyme ; genome mining

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