Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca (Articolo in rivista)

Type
Label
  • Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.tetasy.2005.08.004 (literal)
Alternative label
  • de Gonzalo G., Pazmino D.E.T., Ottolina G., Fraaije M.W., Carrea G. (2005)
    Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca
    in Tetrahedron: asymmetry (Print); ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, AMSTERDAM (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • de Gonzalo G., Pazmino D.E.T., Ottolina G., Fraaije M.W., Carrea G. (literal)
Pagina inizio
  • 3077 (literal)
Pagina fine
  • 3083 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.sciencedirect.com/science/article/pii/S0957416605005902 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 16 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 18 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131 Milano, Italy Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (literal)
Titolo
  • Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca (literal)
Abstract
  • Several organic sulfides, ketones and other organic systems have been tested as substrates in oxidation reactions catalyzed by the recently discovered phenylacetone monooxygenase from Thermobifida fusca. The biocatalytic properties of this Baeyer-Villiger monooxygenase have been studied, revealing reactivity with a large range of sulfides and ketones. Oxidations of several sulfoxides, an amine and an organoboron compound were also observed. The enzyme is able to oxidize a number of sulfides with excellent enantioselectivity, demonstrating the catalytic potential of this novel biocatalyst. (literal)
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