The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.

ABSTRACT: Flavin-dependent monooxygenases (FMOs) constitute a diverse enzyme family that catalyzes crucial hydroxylation, epoxidation, and Baeyer-Villiger reactions across various metabolic pathways in all domains of life. Due to the intricate nature of this enzyme family's mechanisms, some aspects of their functioning remain unknown. Here, we present the results of molecular dynamics computations, supplemented by a bioinformatics analysis, that clarify the early stages of their catalytic cycle. We have elucidated the intricate binding mechanism of NADPH and L-Orn to a class B monooxygenase, the ornithine hydroxylase from Aspergillus$$ Aspergillus $$ fumigatus$$ fumigatus $$ known as SidA. Our investigation involved a comprehensive characterization of the conformational changes associated with the F

SUBMITTER: Pierdominici-Sottile G 

PROVIDER: S-EPMC10962481 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature