Identification of Nucleophilic Probes for Protease-Mediated Transpeptidation.

ABSTRACT: Proteases 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

SUBMITTER: Eom GE 

PROVIDER: S-EPMC6225416 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature