ArticleFrontiers in microbiology2015
The Pseudomonas aeruginosa antimetabolite L -2-amino-4-methoxy-trans-3-butenoic acid (AMB) is made from glutamate and two alanine residues via a thiotemplate-linked tripeptide precursor.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed.
- An extragenic fix for a broken enzyme.Microbiology (Reading, England) · 2026Article
- Deciphering microbial biofilm: mechanism, infection, and advanced approaches for control.Folia microbiologica · 2026Review
- Review
- Systems-level exploitation of OxyR regulon unravels a potential antibacterial target in Pseudomonas aeruginosa.Communications biology · 2025Article
- In-depth genome and comparative genome analysis of a metal-resistant environmental isolateFrontiers in cellular and infection microbiology · 2025Article
- Analysing theFrontiers in cellular and infection microbiology · 2025Review
- Molecular Aspects of the Functioning of Pathogenic Bacteria Biofilm Based onInternational journal of molecular sciences · 2024Review
- The phage-encoded protein PIT2 impactsiScience · 2023Article
- Structural insights into the substrate-bound condensation domains of non-ribosomal peptide synthetase AmbB.Scientific reports · 2022Article
- Nonribosomal Peptide Synthesis Definitely Working Out of the Rules.Microorganisms · 2022Review
- Antifungal strains and gene mapping of secondary metabolites in mangrove sediments from Semarang city and Karimunjawa islands, Indonesia.AIMS microbiology · 2021Article
- We Are One: Multispecies Metabolism of a Biofilm Consortium and Their Treatment Strategies.Frontiers in microbiology · 2021Review
- Review
- Bacteria Belonging toInsects · 2020Article
- Draft Genome Sequence of Pseudomonas aeruginosa Strain LMG 1272, an Atypical White Line Reaction Producer.Microbiology resource announcements · 2020Article
- Putting an end to the Pseudomonas aeruginosa IQS controversy.MicrobiologyOpen · 2020Article
- Article
- Traditional Chinese Medicine Tanreqing Inhibits Quorum Sensing Systems inFrontiers in microbiology · 2020Article
- The plant pathogeneLife · 2018Article
- In Vitro Biosynthesis of the Nonproteinogenic Amino Acid Methoxyvinylglycine.Angewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Pseudomonas aeruginosa toxin L-2-amino-4-methoxy-trans-3-butenoic acid (AMB) is a non-proteinogenic amino acid which is toxic for prokaryotes and eukaryotes. Production of AMB requires a five-gene cluster encoding a putative LysE-type transporter (AmbA), two non-ribosomal peptide synthetases (AmbB and AmbE), and two iron(II)/α-ketoglutarate-dependent oxygenases (AmbC and AmbD). Bioinformatics analysis predicts one thiolation (T) domain for AmbB and two T domains (T1 and T2) for AmbE, suggesting that AMB is generated by a processing step from a precursor tripeptide assembled on a thiotemplate. Using a combination of ATP-PPi exchange assays, aminoacylation assays, and mass spectrometry-based analysis of enzyme-bound substrates and pathway intermediates, the AmbB substrate was identified to be L-alanine (L-Ala), while the T1 and T2 domains of AmbE were loaded with L-glutamate (L-Glu) and L-Ala, respectively. Loading of L-Ala at T2 of AmbE occurred only in the presence of AmbB, indicative of a trans loading mechanism. In vitro assays performed with AmbB and AmbE revealed the dipeptide L-Glu-L-Ala at T1 and the tripeptide L-Ala-L-Glu-L-Ala attached at T2. When AmbC and AmbD were included in the assay, these peptides were no longer detected. Instead, an L-Ala-AMB-L-Ala tripeptide was found at T2. These data are in agreement with a biosynthetic model in which L-Glu is converted into AMB by the action of AmbC, AmbD, and tailoring domains of AmbE. The importance of the flanking L-Ala residues in the precursor tripeptide is discussed.
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.