The dynamics of the flavin, NADPH, and active site loops determine the mechanism of activation of class B flavin-dependent monooxygenases.
NADPH binding
NADPH dynamics
flavin dynamics
flavin-dependent monooxygenases
ornithine binding
uncoupling
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
Apr 2024
Apr 2024
Historique:
revised:
02
02
2024
received:
11
10
2023
accepted:
06
02
2024
medline:
19
3
2024
pubmed:
19
3
2024
entrez:
19
3
2024
Statut:
ppublish
Résumé
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
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e4935Subventions
Organisme : CONICET
ID : 11220130100260CO
Organisme : Fulbright
Organisme : ANPCyT
ID : PICT 2020-SerieA-00192
Organisme : National Science Foundation
ID : CHE-2003658
Organisme : Universidad Nacional de Quilmes (UNQ)
ID : 1292/19
Informations de copyright
© 2024 The Protein Society.
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