ArticleMicrobial genomics2025
Multinuclear non-haem iron-dependent oxidative enzymes: landscape of their substrates, partner proteins and biosynthetic gene clusters.
Article in Microbial genomics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026Article
- Biosynthesis of Peptidic Thiooxazole Metallophores Installed by Multinuclear Nonheme Iron Enzymes.ACS chemical biology · 2026Article
- Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- CrpH ofFrontiers in microbiology · 2026Article
- Article
- Biosynthesis of peptidic thiooxazole metallophores installed by multinuclear nonheme iron enzymes.bioRxiv : the preprint server for biology · 2025Article
- Co-opting the bacterial lipoprotein pathway in the biosynthesis of a lipidated macrocyclic peptide.bioRxiv : the preprint server for biology · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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Abstract
Proteins of the multinuclear non-haem iron-dependent oxidative (MNIO) enzyme superfamily catalyse various modification reactions on the precursors of ribosomally synthesized post-translationally modified peptides (RiPPs). We recently identified two large families of MNIO-modified RiPPs called bufferins, which enhance bacterial growth under copper stress by chelating the excess metal ions. Here, we explored the diversity of potential MNIO substrates by performing extensive
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