Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation
AbstractProteases have evolved to mediate the hydrolysis of peptide bonds but may perform transpeptidation in the presence of a proper nucleophilic molecule that can effectively compete with water to react with the acyl-enzyme intermediate. There have been several examples of protease-mediated transpeptidation, but they are generally inefficient, and little effort has been made to systematically control the transpeptidation activity of other proteases with good nucleophiles. Here, we developed an on-bead screening approach to find a probe that functions efficiently as a nucleophile in the protease-mediated transpeptidation reaction, and we identified good probes for a model protease DegP. These probes were covalently linked to the C-termini of the cleaved peptides in a mild condition and made the selective enrichment of ligated peptides possible. We suggest that good nucleophilic probes can be found for many other proteases that act via acyl-enzyme intermediates, and these probes will help characterize their substrates. View Full-Text
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Eom, G.-E.; Kim, S. Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation. Molecules 2018, 23, 2109.
Eom G-E, Kim S. Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation. Molecules. 2018; 23(9):2109.Chicago/Turabian Style
Eom, Ga-eul; Kim, Seokhee. 2018. "Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation." Molecules 23, no. 9: 2109.
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