F
Filippo Fiorentini
Researcher at University of Pavia
Publications - 7
Citations - 188
Filippo Fiorentini is an academic researcher from University of Pavia. The author has contributed to research in topics: Flavin-containing monooxygenase & Monooxygenase. The author has an hindex of 6, co-authored 7 publications receiving 133 citations. Previous affiliations of Filippo Fiorentini include Graz University of Technology & University of Graz.
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Journal ArticleDOI
Biocatalytic Characterization of Human FMO5: Unearthing Baeyer–Villiger Reactions in Humans
Filippo Fiorentini,Martina Geier,Claudia Binda,Margit Winkler,Kurt Faber,Mélanie Hall,Andrea Mattevi +6 more
TL;DR: The atypical in vitro activity of human FMO5 as a Baeyer-Villiger mono-oxygenase on a broad range of substrates is demonstrated, revealing the first example to date of a human protein catalyzing such reactions and open new perspectives in human oxidative metabolism.
Journal ArticleDOI
Ancestral-sequence reconstruction unveils the structural basis of function in mammalian FMOs.
Callum R. Nicoll,Gautier Bailleul,Filippo Fiorentini,María Laura Mascotti,Marco W. Fraaije,Andrea Mattevi +5 more
TL;DR: Ancestral reconstruction leads to characterization and crystallization of three ancient mammalian flavin-containing monooxygenases, offering insights into their mechanisms of membrane binding, catalytic activity and substrate selection.
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Baeyer-Villiger Monooxygenase FMO5 as Entry Point in Drug Metabolism
Filippo Fiorentini,Filippo Fiorentini,Elvira Romero,Marco W. Fraaije,Kurt Faber,Mã©lanie Hall,Andrea Mattevi +6 more
TL;DR: Nabumetone and pentoxifylline, two widely used pharmaceuticals, were demonstrated to be efficiently oxidized in vitro by FMO5 to the corresponding acetate esters with high selectivity and the proposed pathways explain the formation of a predominant plasma metabolite of pentoxifyinglline.
Journal ArticleDOI
Beyond active site residues: overall structural dynamics control catalysis in flavin-containing and heme-containing monooxygenases.
TL;DR: To correctly choreograph the substrates spatially and temporally, MOs evolved a variety of strategies, which involve structural flexibility, including conformational changes of their flavin prosthetic group and their nicotinamide cofactor.
Journal ArticleDOI
The Extreme Structural Plasticity in the CYP153 Subfamily of P450s Directs Development of Designer Hydroxylases.
Filippo Fiorentini,Anna-Maria Hatzl,Sandy Schmidt,Simone Savino,Anton Glieder,Andrea Mattevi +5 more
TL;DR: An extensive characterization of CYP153 enzymes was performed, highlighting a conserved architecture and amino acid composition of the catalytic core close to the heme, while showing a huge degree of structural plasticity and flexibility in those regions hosting the substrate recognition sites.