ArticleNature chemical biology2012
A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 119 citations in OpenAlex.
- A heme-dependent enzyme forms the hydrazine in the antibiotic negamycin.Nature chemical biology · 2025Article
- The Intricate Nonribosomal Assembly of a Potent Antifungal Lipopeptide from theJournal of the American Chemical Society · 2025Article
- Article
- Structure, Function and Engineering of the Nonribosomal Peptide Synthetase Condensation Domain.International journal of molecular sciences · 2024Review
- Ultrasensitive Electrochemical Immunosensor for Multiplex Sandwich Bioassaying Based on the Functional Antibodies.ACS omega · 2024Article
- History of the streptothricin antibiotics and evidence for the neglect of the streptothricin resistome.npj antimicrobials and resistance · 2024Review
- Evaluation ofFrontiers in microbiology · 2024Article
- Separation of an ε-poly-L-lysine derivative by solvent extraction under a controlled interfacial potential difference.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Structural and functional insights into δ-poly-L-ornithine polymer biosynthesis from Acinetobacter baumannii.Communications biology · 2023Article
- Elucidating the molecular programming of a nonlinear non-ribosomal peptide synthetase responsible for fungal siderophore biosynthesis.Nature communications · 2023Article
- N-Formimidoylation/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry.Nature communications · 2023Article
- Nonribosomal antibacterial peptides isolated from Streptomyces agglomeratus 5-1-3 in the Qinghai-Tibet Plateau.Microbial cell factories · 2023Article
- The Assembly-Line Enzymology of Nonribosomal Peptide Biosynthesis.Methods in molecular biology (Clifton, N.J.) · 2023Article
- First direct evidence for direct cell-membrane penetrations of polycationic homopoly(amino acid)s produced by bacteria.Communications biology · 2022Article
- GNPS-Guided Discovery of Madurastatin Siderophores from the Termite-Associated Actinomadura sp. RB99.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Biotechnological production optimization of argyrins - a potent immunomodulatory natural product class.Microbial biotechnology · 2022Article
- Nonribosomal peptide synthetases and their biotechnological potential in Penicillium rubens.Journal of industrial microbiology & biotechnology · 2021Review
- Production of a broad spectrum streptothricin like antibiotic from halotolerant Streptomyces fimbriatus isolate G1 associated with marine sediments.Folia microbiologica · 2021Article
- Enzymatic Late-Stage Modifications: Better Late Than Never.Angewandte Chemie (International ed. in English) · 2021Review
- Enzymkatalysierte späte Modifizierungen: Besser spät als nie.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The streptothricin (ST) antibiotics, produced by Streptomyces bacteria, contain L-β-lysine ((3S)-3,6-diaminohexanoic acid) oligopeptides as pendant chains. Here we describe three unusual nonribosomal peptide synthetases (NRPSs) involved in ST biosynthesis: ORF 5 (a stand-alone adenylation (A) domain), ORF 18 (containing thiolation (T) and condensation (C) domains) and ORF 19 (a stand-alone A domain). We demonstrate that ST biosynthesis begins with adenylation of L-β-lysine by ORF 5, followed by transfer to the T domain of ORF 18. In contrast, L-β-lysine molecules adenylated by ORF 19 are used to elongate an L-β-lysine peptide chain on ORF 18, a reaction unexpectedly catalyzed by ORF 19 itself. Finally, the C domain of ORF 18 catalyzes the condensation of L-β-lysine oligopeptides covalently bound to ORF 18 with a freely diffusible intermediate to release the ST products. These results highlight an unusual activity for an A domain and unique mechanisms of crosstalk within NRPS machinery.
Indexed as
Identifiers
What OpenQuestion holds
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.