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    Human Copper-Dependent Amine Oxidases

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    Finney_2014_HumanCopper.pdf (1.070Mb)
    Issue Date
    2014-03-15
    Author
    Finney, Joel
    Moon, Hee-Jung
    Ronnebaum, Trey
    Lantz, Mason
    Mure, Minae
    Publisher
    Elsevier
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
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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.
    URI
    http://hdl.handle.net/1808/26722
    DOI
    https://doi.org/10.1016/j.abb.2013.12.022
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    • Chemistry Scholarly Works [610]
    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

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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