{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lara DD"],"funding":["NIH HHS","NIGMS NIH HHS"],"pagination":["e202500331"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12283067"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(16)"],"pubmed_abstract":["β-Methyl amino 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. A genome-mining-guided discovery of a novel biosynthetic gene cluster capable of producing β-methylarginine, from the phylum Planctomycetes is reported. Both in vivo and in vitro evidence indicates 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 tha"],"journal":["Chembiochem : a European journal of chemical biology"],"pubmed_title":["A Self-Sufficient β-Methylarginine Biosynthetic Pathway in Planctomycetes."],"pmcid":["PMC12283067"],"funding_grant_id":["R35GM151205","R35 GM151205"],"pubmed_authors":["Zeng BT","Hai Y","Lara DD"],"additional_accession":[]},"is_claimable":false,"name":"A Self-Sufficient β-Methylarginine Biosynthetic Pathway in Planctomycetes.","description":"β-Methyl amino 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. A genome-mining-guided discovery of a novel biosynthetic gene cluster capable of producing β-methylarginine, from the phylum Planctomycetes is reported. Both in vivo and in vitro evidence indicates 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 tha","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-06T09:07:57.631Z","creation":"2026-05-28T03:11:47.721Z"},"accession":"S-EPMC12283067","cross_references":{"pubmed":["40523148"],"doi":["10.1002/cbic.202500331"]}}