Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies.

ABSTRACT: Iterative enzymes, which catalyze sequential reactions, have the potential to improve the atom economy and diversity of industrial enzymatic processes. Redesigning one-step enzymes to be iterative biocatalysts could further enhance these processes. Carbamoyltransferases (CTases) catalyze carbamoylation, an important modification for the bioactivity of many secondary metabolites with pharmaceutical applications. To generate an iterative CTase, we determine the X-ray structure of GdmN, a one-step CTase involved in ansamycin biosynthesis. GdmN forms a face-to-face homodimer through unusual C-terminal domains, a previously unknown functional form for CTases. Structural determination of GdmN complexed with multiple intermediates elucidates the carbamoylation process and identifies key binding r

SUBMITTER: Wei J 

PROVIDER: S-EPMC9633730 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature