ArticleJACS Au2025
Photocontrolling the Enantioselectivity of a Phosphotriesterase via Incorporation of a Light-Responsive Unnatural Amino Acid.
Article in JACS Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Catalytic pBiochemistry · 2026Article
- Expanding the Repertoire of Photoswitchable Unnatural Amino Acids for Enzyme Engineering.Angewandte Chemie (International ed. in English) · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The external control of catalytic activity and substrate specificity of enzymes by light has aroused great interest in the fields of biocatalysis and pharmacology. Going beyond, we have attempted to photocontrol enzyme stereoselectivity on the example of phosphotriesterase (PTE), which is capable of hydrolyzing a wide variety of racemic organophosphorus substrates where one of two enantiomers is often highly toxic. To pursue this goal, the photocaged unnatural amino acid
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Registered trials
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