Human copper-dependent amine oxidases

J Finney, HJ Moon, T Ronnebaum, M Lantz… - Archives of biochemistry …, 2014 - Elsevier
J Finney, HJ Moon, T Ronnebaum, M Lantz, M Mure
Archives of biochemistry and biophysics, 2014Elsevier
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 …
Abstract
Copper amine oxidases (CAOs) are a class of enzymes that contain Cu2+ 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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