Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases.

ABSTRACT: Biocatalytic C-H activation has the potential to merge enzymatic and synthetic strategies for bond formation. Fe^II/αKG-dependent halogenases are particularly distinguished for their ability both to control selective C-H activation as well as to direct group transfer of a bound anion along a reaction axis separate from oxygen rebound, enabling the development of new transformations. In this context, we elucidate the basis for the selectivity of enzymes that perform selective halogenation to yield 4-Cl-lysine (BesD), 5-Cl-lysine (HalB), and 4-Cl-ornithine (HalD), allowing us to probe how site-selectivity and chain length selectivity are achieved. We now report the crystal structure of the HalB and HalD, revealing the key role of the substrate-binding lid in positioning the substra

SUBMITTER: Kissman EN 

PROVIDER: S-EPMC10041140 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature