ArticleACS chemical biology2022
Substrate Recognition by the Peptidyl-(
Article in ACS chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Biosynthesis of Peptidic Thiooxazole Metallophores Installed by Multinuclear Nonheme Iron Enzymes.ACS chemical biology · 2026Article
- 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
- Discovery of a Two-Step Enzyme Cascade Converting Aspartate to Aminomalonate in Peptide Natural Product Biosynthesis.Journal of the American Chemical Society · 2025Article
- Substrate recognition by a peptide-aminoacyl-tRNA ligase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Total Synthesis of (±)-3-Thiaglutamate.Tetrahedron letters · 2024Article
- Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme.ACS central science · 2024Article
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC.Biochemistry · 2024Article
- Genome Mining for New Enzyme Chemistry.ACS catalysis · 2024Review
- N-Cα Bond Cleavage Catalyzed by a Multinuclear Iron Oxygenase from a Divergent Methanobactin-like RiPP Gene Cluster.Journal of the American Chemical Society · 2024Article
- Structures of the holoenzyme TglHI required for 3-thiaglutamate biosynthesis.Structure (London, England : 1993) · 2023Article
- How nature incorporates sulfur and selenium into bioactive natural products.Current opinion in chemical biology · 2023Review
- Macrocyclization and Backbone Rearrangement During RiPP Biosynthesis by a SAM-Dependent Domain-of-Unknown-Function 692.ACS central science · 2023Article
- Mechanistic Studies on Dehydration in Class V Lanthipeptides.ACS chemical biology · 2022Article
- Biosynthesis of 3-thia-α-amino acids on a carrier peptide.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
3-Thiaglutamate is a recently identified amino acid analog originating from cysteine. During its biosynthesis, cysteinyl-tRNA is first enzymatically appended to the C-terminus of TglA, a 50-residue ribosomally translated peptide scaffold. After hydrolytic removal of the tRNA, this cysteine residue undergoes modification on the scaffold before eventual proteolysis of the nascent 3-thiaglutamyl residue to release 3-thiaglutamate and regenerate TglA. One of the modifications of TglACys requires a complex of two polypeptides, TglH and TglI, which uses nonheme iron and O
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.