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Copper amine oxidase: cunning cofactor and controversial copper.
Dawkes, H C; Phillips, S E.
Afiliación
  • Dawkes HC; Astbury Centre for Structural Molecular Biology, School of Biochemistry and Molecular Biology, University of Leeds, LS29JT, Leeds, UK.
Curr Opin Struct Biol ; 11(6): 666-73, 2001 Dec.
Article en En | MEDLINE | ID: mdl-11751046
ABSTRACT
Copper amine oxidases have a complex reaction cycle that converts a primary amine and molecular oxygen into the aldehyde, ammonia and hydrogen peroxide. Coupling structural studies of freeze-trapped reaction intermediates in crystals with kinetic and spectroscopic experiments in solution has generated a detailed molecular picture of catalysis. Although dioxygen has been directly observed bound to the copper at a late stage in the reaction cycle, whether copper is the initial binding site remains controversial.
Asunto(s)
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Banco de datos: MEDLINE Asunto principal: Dihidroxifenilalanina / Amina Oxidasa (conteniendo Cobre) Límite: Animals Idioma: En Año: 2001 Tipo del documento: Article
Buscar en Google
Banco de datos: MEDLINE Asunto principal: Dihidroxifenilalanina / Amina Oxidasa (conteniendo Cobre) Límite: Animals Idioma: En Año: 2001 Tipo del documento: Article