ArticleProceedings of the National Academy of Sciences of the United States of America2012
Catalytic control of enzymatic fluorine specificity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 30 citations in OpenAlex.
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini.Nature chemistry · 2025Article
- Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein C termini.bioRxiv : the preprint server for biology · 2024Article
- Enzymatic synthesis of fluorinated compounds.Applied microbiology and biotechnology · 2021Review
- Steric-Free Bioorthogonal Labeling of Acetylation Substrates Based on a Fluorine-Thiol Displacement Reaction.Journal of the American Chemical Society · 2021Article
- Enhancing glycan stabilityChemical science · 2020Article
- Inverting Small Molecule-Protein Recognition by the Fluorine Gauche Effect: Selectivity Regulated by Multiple H→F Bioisosterism.Angewandte Chemie (International ed. in English) · 2019Article
- Entropy drives selective fluorine recognition in the fluoroacetyl-CoA thioesterase fromProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural insights into GDP-mediated regulation of a bacterial acyl-CoA thioesterase.The Journal of biological chemistry · 2017Article
- Fluorothreonyl-tRNA deacylase prevents mistranslation in the organofluorine producerProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Engineered Fluorine Metabolism and Fluoropolymer Production in Living Cells.Angewandte Chemie (International ed. in English) · 2017Article
- Synthetic biology approaches to fluorinated polyketides.Accounts of chemical research · 2015Article
- Divergence of substrate specificity and function in the Escherichia coli hotdog-fold thioesterase paralogs YdiI and YbdB.Biochemistry · 2014Article
- Molecular recognition of fluorine impacts substrate selectivity in the fluoroacetyl-CoA thioesterase FlK.Biochemistry · 2014Article
- Characterization of a SAM-dependent fluorinase from a latent biosynthetic pathway for fluoroacetate and 4-fluorothreonine formation in Nocardia brasiliensis.F1000Research · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The investigation of unique chemical phenotypes has led to the discovery of enzymes with interesting behaviors that allow us to explore unusual function. The organofluorine-producing microbe Streptomyces cattleya has evolved a fluoroacetyl-CoA thioesterase (FlK) that demonstrates a surprisingly high level of discrimination for a single fluorine substituent on its substrate compared with the cellularly abundant hydrogen analog, acetyl-CoA. In this report, we show that the high selectivity of FlK is achieved through catalysis rather than molecular recognition, where deprotonation at the C(α) position to form a putative ketene intermediate only occurs on the fluorinated substrate, thereby accelerating the rate of hydrolysis 10(4)-fold compared with the nonfluorinated congener. These studies provide insight into mechanisms of catalytic selectivity in a native system where the existence of two reaction pathways determines substrate rather than product selection.
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.