ArticleProceedings of the National Academy of Sciences of the United States of America2015
Panoramic view of a superfamily of phosphatases through substrate profiling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 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
76 citing papers in PubMed.
- Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026Review
- Graph-based representations in modern protein science.The Biochemical journal · 2026Review
- Robots and Minimal, Physics-Informed Features: A Hybrid Framework for Enzyme Catalysis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Systematic discovery of enzyme promiscuity in Escherichia coli using in vitro metabolomics.Communications biology · 2026Article
- Review
- SynRXN: An Open Benchmark and Curated Dataset for Computational Reaction Modeling.Scientific data · 2026Article
- Toward the Chemoenzymatic Synthesis of DNA-Encoded Libraries.ACS central science · 2026Review
- Article
- Mutations Elevate an Underground Pathway to a Physiologically Relevant Protopathway.Molecular biology and evolution · 2025Article
- Glucoselipid Biosurfactant Biosynthesis Operon ofMicroorganisms · 2025Article
- A substrate-multiplexed platform for profiling enzymatic potential of plant family 1 glycosyltransferases.Nature communications · 2025Article
- Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of the phosphatase essential for riboflavin biosynthesis in Aquifex aeolicus.The Journal of biological chemistry · 2025Article
- CPI-Pred: A deep learning framework for predicting functional parameters of compound-protein interactions.bioRxiv : the preprint server for biology · 2025Article
- Self-supervised domain adaptation of protein language model based solely on positive enzyme-reaction pairs.Computational and structural biotechnology journal · 2025Article
- Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024Review
- Microbial synthesis of sedoheptulose from glucose by metabolically engineered Corynebacterium glutamicum.Microbial cell factories · 2024Article
- Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products.Natural product reports · 2024Review
- Article
- Enhancing Machine-Learning Prediction of Enzyme Catalytic Temperature Optima through Amino Acid Conservation Analysis.International journal of molecular sciences · 2024Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors.
Funding
Abstract
Large-scale activity profiling of enzyme superfamilies provides information about cellular functions as well as the intrinsic binding capabilities of conserved folds. Herein, the functional space of the ubiquitous haloalkanoate dehalogenase superfamily (HADSF) was revealed by screening a customized substrate library against >200 enzymes from representative prokaryotic species, enabling inferred annotation of ∼35% of the HADSF. An extremely high level of substrate ambiguity was revealed, with the majority of HADSF enzymes using more than five substrates. Substrate profiling allowed assignment of function to previously unannotated enzymes with known structure, uncovered potential new pathways, and identified iso-functional orthologs from evolutionarily distant taxonomic groups. Intriguingly, the HADSF subfamily having the least structural elaboration of the Rossmann fold catalytic domain was the most specific, consistent with the concept that domain insertions drive the evolution of new functions and that the broad specificity observed in HADSF may be a relic of this process.
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.