ArticleNature communications2021
Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Parallel Pathways and Alternative Macrocyclizations in the Biosynthesis of Largimycins by Cytochrome P450 Minus Mutants ofJournal of natural products · 2026Article
- Biosynthesis of 6-thioguanine: characterizing two intermediates involved in its thioamide formation reaction.ACS catalysis · 2026Article
- Discovery of acylsulfenic acid-featuring natural product sulfenicin and characterization of its biosynthesis.Nature chemistry · 2025Article
- Molecular basis for the diversification of lincosamide biosynthesis by pyridoxal phosphate-dependent enzymes.Nature chemistry · 2025Article
- Divergent Tandem Acyl Carrier Proteins Necessitate In-Series Polyketide Processing in the Leinamycin Family.Angewandte Chemie (International ed. in English) · 2025Article
- Evolution-guided engineering ofScience (New York, N.Y.) · 2024Article
- How nature incorporates sulfur and selenium into bioactive natural products.Current opinion in chemical biology · 2023Review
- The many facets of sulfur incorporation in natural product biosynthesis.Current opinion in chemical biology · 2023Review
- Biosynthesis of DNA-Alkylating Antitumor Natural Products.Molecules (Basel, Switzerland) · 2022Review
- Understanding and Circumventing the Requirement for Native Thioester Substrates for α-Oxoamine Synthase Reactions.ACS chemical biology · 2022Article
- Decatungstate-catalyzed radical disulfuration through direct C-H functionalization for the preparation of unsymmetrical disulfides.Nature communications · 2022Article
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8 authors.
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Abstract
Nature forms S-S bonds by oxidizing two sulfhydryl groups, and no enzyme installing an intact hydropersulfide (-SSH) group into a natural product has been identified to date. The leinamycin (LNM) family of natural products features intact S-S bonds, and previously we reported an SH domain (LnmJ-SH) within the LNM hybrid nonribosomal peptide synthetase (NRPS)-polyketide synthase (PKS) assembly line as a cysteine lyase that plays a role in sulfur incorporation. Here we report the characterization of an S-adenosyl methionine (SAM)-dependent hydropersulfide methyltransferase (GnmP) for guangnanmycin (GNM) biosynthesis, discovery of hydropersulfides as the nascent products of the GNM and LNM hybrid NRPS-PKS assembly lines, and revelation of three SH domains (GnmT-SH, LnmJ-SH, and WsmR-SH) within the GNM, LNM, and weishanmycin (WSM) hybrid NRPS-PKS assembly lines as thiocysteine lyases. Based on these findings, we propose a biosynthetic model for the LNM family of natural products, featuring thiocysteine lyases as PKS domains that directly install a -SSH group into the GNM, LNM, or WSM polyketide scaffold. Genome mining reveals that SH domains are widespread in Nature, extending beyond the LNM family of natural products. The SH domains could also be leveraged as biocatalysts to install an -SSH group into other biologically relevant scaffolds.
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