ArticleACS chemical biology2019
Directed Evolution Reveals the Functional Sequence Space of an Adenylation Domain Specificity Code.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Biosynthesis ofSynthetic and systems biotechnology · 2026Article
- Mapping the nonribosomal specificity code through promiscuity-guided A-domain engineering.Chemical science · 2026Article
- A broad-spectrum antibiotic targets multiple-drug-resistant bacteria with dual binding targets and no detectable resistance.Nature communications · 2025Article
- Viral escape-inspired framework for structure-guided dual bait protein biosensor design.PLoS computational biology · 2025Article
- Functional Diversity and Engineering of the Adenylation Domains in Nonribosomal Peptide Synthetases.Marine drugs · 2024Review
- Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.Natural product reports · 2024Review
- Current status and emerging frontiers in enzyme engineering: An industrial perspective.Heliyon · 2024Review
- Advances in the adenylation domain: discovery of diverse non-ribosomal peptides.Applied microbiology and biotechnology · 2023Review
- BioCAT: Search for biosynthetic gene clusters producing nonribosomal peptides with known structure.Computational and structural biotechnology journal · 2022Article
- Protein engineering for natural product biosynthesis and synthetic biology applications.Protein engineering, design & selection : PEDS · 2021Review
- HAMA: a multiplexed LC-MS/MS assay for specificity profiling of adenylate-forming enzymes.Chemical science · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Nonribosomal peptides are important natural products biosynthesized by nonribosomal peptide synthetases (NRPSs). Adenylation (A) domains of NRPSs are highly specific for the substrate they recognize. This recognition is determined by 10 residues in the substrate-binding pocket, termed the specificity code. This finding led to the proposal that nonribosomal peptides could be altered by specificity code swapping. Unfortunately, this approach has proven, with few exceptions, to be unproductive; changing the specificity code typically results in broadened specificity or poor function. To enhance our understanding of A domain substrate selectivity, we carried out a detailed analysis of the specificity code from the A domain of EntF, an NRPS involved in enterobactin biosynthesis in
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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.