ArticleBiochemistry and biophysics reports2020
New luciferin-based probe substrates for human CYP26A1.
Article in Biochemistry and biophysics reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Design and engineering of logic genetic-enzymatic gates based on the activity of the human CYP2C9 enzyme in permeabilizedSynthetic and systems biotechnology · 2024Article
- Identification of New Substrates and Inhibitors of Human CYP2A7.Molecules (Basel, Switzerland) · 2024Article
- A convenient test system for the identification of CYP4V2 inhibitors.Molecular vision · 2021Article
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Authors and funding
6 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Activity of human CYP26A1 towards six proluciferin probe substrates and their ester derivatives was monitored. These included three monofluorobenzyl ether isomers and three five-membered heterocycles. Overall, luciferin substrates with a free acid group gave higher activities than the ester compounds. Also, luciferin derivatives with six-ring structures were better metabolized than those with five-rings. The best substrates identified in this study are Luciferin 6' 3-fluorobenzyl ether (Luciferin-3FBE) and its methyl ester (Luciferin-3FBEME). Taken together, we describe eleven new probe substrates for CYP26A1 and demonstrate for the first time that CYP26A1 does not only accept acid substrates but can also metabolize esters.
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