Boron Designer Enzyme with a Hybrid Catalytic Dyad.

ABSTRACT: Genetically encoded noncanonical amino acids can introduce new-to-nature activation modes into enzymes. While these amino acids can act as catalysts on their own due to their inherent chemical properties, interactions with adjacent residues in an enzyme, such as those present in natural catalytic dyads or triads, unlock a higher potential for designer enzymes. We incorporated a boron-containing amino acid into the protein scaffold RamR to create an active enzyme for the kinetic resolution of α-hydroxythioesters. We found that a closely positioned lysine residue is crucial for the catalytic activity of the designer enzyme by forming a hybrid catalytic dyad with the boronic acid residue. The enzyme is capable of resolving differently substituted α-hydroxythioesters with good selectivities. H

SUBMITTER: Longwitz L 

PROVIDER: S-EPMC11667675 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature