Catalytic divergencies in the mechanism of L-arginine hydroxylating nonheme iron enzymes.

ABSTRACT: Many enzymes in nature utilize a free arginine (L-Arg) amino acid to initiate the biosynthesis of natural products. Examples include nitric oxide synthases, which generate NO from L-Arg for blood pressure control, and various arginine hydroxylases involved in antibiotic biosynthesis. Among the groups of arginine hydroxylases, several enzymes utilize a nonheme iron(II) active site and let L-Arg react with dioxygen and α-ketoglutarate to perform either C₃-hydroxylation, C₄-hydroxylation, C₅-hydroxylation, or C₄-C₅-desaturation. How these seemingly similar enzymes can react with high specificity and selectivity to form different products remains unknown. Over the past few years, our groups have investigated the mechanisms of L-Arg-

SUBMITTER: Ali HS 

PROVIDER: S-EPMC10884159 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature