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Human copper-dependent amine oxidases.
Finney, Joel; Moon, Hee-Jung; Ronnebaum, Trey; Lantz, Mason; Mure, Minae.
Afiliación
  • Finney J; Department of Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
  • Moon HJ; Department of Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
  • Ronnebaum T; Department of Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
  • Lantz M; Department of Chemistry, The University of Kansas, Lawrence, KS 66045, USA.
  • Mure M; Department of Chemistry, The University of Kansas, Lawrence, KS 66045, USA. Electronic address: mmure@ku.edu.
Arch Biochem Biophys ; 546: 19-32, 2014 Mar 15.
Article en En | MEDLINE | ID: mdl-24407025
ABSTRACT
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu(2+) and a tyrosine-derived quinone cofactor, catalyze the conversion of a primary amine functional group to an aldehyde, and generate hydrogen peroxide and ammonia as byproducts. These enzymes can be classified into two non-homologous families 2,4,5-trihydroxyphenylalanine quinone (TPQ)-dependent CAOs and the lysine tyrosylquinone (LTQ)-dependent lysyl oxidase (LOX) family of proteins. In this review, we will focus on recent developments in the field of research concerning human CAOs and the LOX family of proteins. The aberrant expression of these enzymes is linked to inflammation, fibrosis, tumor metastasis/invasion and other diseases. Consequently, there is a critical need to understand the functions of these proteins at the molecular level, so that strategies targeting these enzymes can be developed to combat human diseases.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Amina Oxidasa (conteniendo Cobre) Límite: Animals / Humans Idioma: En Revista: Arch Biochem Biophys Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Amina Oxidasa (conteniendo Cobre) Límite: Animals / Humans Idioma: En Revista: Arch Biochem Biophys Año: 2014 Tipo del documento: Article País de afiliación: Estados Unidos