ArticleACS catalysis2024
Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit.
Article in ACS catalysis, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Site-Specific Features Guiding Effective Reversible Photocontrol of Tryptophan Synthase With the Unnatural Amino Acid AzoF.Chembiochem : a European journal of chemical biology · 2026Article
- The Discovery ofACS catalysis · 2026Article
- Inactive but Essential: The Role of the Inactive State of E49 in the Mechanism of the Alpha Subunit of Tryptophan Synthase and Its Stand-Alone BlueprintACS catalysis · 2026Article
- Clustering and Analyzing Ensembles of Residue Interaction Networks from Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Of Revolutions and Roadblocks: The Emerging Role of Machine Learning in Biocatalysis.ACS central science · 2025Review
- Distal mutations enhance catalysis in designed enzymes by facilitating substrate binding and product release.Nature communications · 2025Article
- A naturally occurring standalone TrpB enzyme provides insights into allosteric communication within tryptophan synthase.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The α-subunit (TrpA) of the allosterically regulated bifunctional tryptophan synthase αββα enzyme catalyzes the retro-aldol cleavage of indole-glycerol phosphate (IGP) to d-glyceraldehyde 3-phosphate (G3P) and indole. The activity of the enzyme is highly dependent on the β-subunit (TrpB), which allosterically regulates and activates TrpA for enhanced function. This contrasts with the homologous BX1 enzyme from
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.