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Human Copper-Dependent Amine Oxidases
Finney, Joel Moon, Hee-Jung Ronnebaum, Trey Lantz, Mason Mure, Minae
Finney, Joel
Moon, Hee-Jung
Ronnebaum, Trey
Lantz, Mason
Mure, Minae
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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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Date
2014-03-15
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Elsevier
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Keywords
Cooper amine oxidase, Lysyl oxidase, Quinoprotein
Citation
Joel Finney, Hee-Jung Moon, Trey Ronnebaum, Mason Lantz, Minae Mure
Arch Biochem Biophys. 2014 Mar 15; 546: 19–32. Published online 2014 Jan 6. doi: 10.1016/j.abb.2013.12.022