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Structure and Reactivity of Copper-Containing Amine Oxidases

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Bioinorganic Chemistry of Copper

Abstract

In recent years, considerable progress has been made toward understanding the active site structures and mechanisms of copper-containing amine oxidases. Copper-containing amine oxidases are one of the most widely distributed classes of “Type-2” copper enzyme. Copper amine oxidases have been highly purified from bacteria, yeasts, plants, and mammals.1 Recently an inducible phenethylamine oxidase was purified from the K-12 strain of E. coli and shown to contain copper, the first example of a copper-containing amine oxidase in gram-negative bacteria.2 Amine oxidases (hereafter this phrase will refer exclusively to the copper-containing enzymes, unless otherwise indicated) catalyze the oxidative examination of primary amines:

$$ RCH_2 NH_2 + O_2 + H_2 O \to RCHO + H_2 O_2 + NH_3 $$

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© 1993 Chapman & Hall, Inc.

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Dooley, D.M. et al. (1993). Structure and Reactivity of Copper-Containing Amine Oxidases. In: Karlin, K.D., Tyeklár, Z. (eds) Bioinorganic Chemistry of Copper. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6875-5_37

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  • DOI: https://doi.org/10.1007/978-94-011-6875-5_37

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-011-6877-9

  • Online ISBN: 978-94-011-6875-5

  • eBook Packages: Springer Book Archive

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