Related Experiment Video
Updated: Sep 20, 2026

Chemical Triphosphorylation of Oligonucleotides
Published on: June 2, 2022
Enhancement of the catalytic activity of an artificial phosphotriesterase using a molecular imprinting technique
Zihui Meng1, Tomohiko Yamazaki, Koji Sode
1Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Nakamachi, Koganei, Tokyo 184-8588, Japan.
Abstract:
An artificial phosphotriesterase (PTE) was constructed by co-polymerization of 4(5)-vinylimidazole-Zn(2+)-methacrylic acid cluster with a divinylbenzene polymer. Compared with the spontaneous hydrolysis, the resulting polymer catalyst caused 105-fold rate acceleration towards the hydrolysis of diethyl p-nitrophenyl phosphate (Paraoxon). The catalytic activity of the polymer catalyst could be enhanced for 30% using molecular imprinting technique and the molecularly-imprinted catalyst (MIC) showed a turnover rate of 7.4 x 10(-2) s(-1) towards the hydrolysis of Paraoxon. The MIC also hydrolyzed thiophosphates and phosphorothiolate triester pesticides. Construction of an amperometric sensor employing the MIC as catalyst achieved a detection limit of 0.1 mM Paraoxon.
Related Concept Videos
Phosphodiester Linkages
Enzyme Inhibition
Catalytically Perfect Enzymes
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

