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- W3136123324 abstract "Aspartic proteases use a pair of carboxylic acids to activate water molecules for nucleophilic attack. Here we report a nanoparticle catalyst with a similar catalytic motif capable of generating a hydroxide ion in its active site even under acidic reaction conditions. The synthetic enzyme accelerated the hydrolysis of para-nitrophenyl acetate (PNPA) by 91,000 times and could also hydrolyze nonactivated aryl esters at pH 7. The distance between the two acids and, in particular, the flexibility of the catalytic groups in the active site controlled the catalytic efficiency. The synthetic enzyme readily detected the addition of a single methyl on the acyl group of the substrate, as well as the substitution pattern on the phenyl ring." @default.
- W3136123324 created "2021-03-29" @default.
- W3136123324 creator A5023367767 @default.
- W3136123324 creator A5070084402 @default.
- W3136123324 date "2021-03-16" @default.
- W3136123324 modified "2023-10-18" @default.
- W3136123324 title "Selective Hydrolysis of Aryl Esters under Acidic and Neutral Conditions by a Synthetic Aspartic Protease Mimic" @default.
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- W3136123324 doi "https://doi.org/10.1021/acscatal.1c00371" @default.
- W3136123324 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8378761" @default.
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