Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

Copper Amine Oxidase

Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_335

Synonyms

Definition

Copper amine oxidase refers to a ubiquitous family of enzymes that catalyze the oxidative deamination of primary amines, concomitant with the two-electron reduction of molecular oxygen to hydrogen peroxide. To accomplish this reaction, these enzymes utilize the redox-active cofactor 2,4,5-trihydroxyphenylalanine quinone (TOPA quinone or TPQ).

Classification

Up until recently, copper amine oxidases (CAOs) were classified within the Enzyme Commission classification EC 1.4.3.6, distinct from the flavin-containing amine oxidases (monoamine oxidase, EC 1.4.3.4) (Boyce et al. 2009). This distinction was based on cofactor content rather than reaction catalyzed, however, leading to some confusion in the literature. For clarification, EC 1.4.3.6 has now been deleted and replaced with two distinct entries: EC 1.4.3.21 and EC 1.4.3.22 (Boyce et al. 2009). EC 1.4.3.21...

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References

  1. Boyce S, Tipton KF, O’Sullivan MI, Davey GP, Gildea MM, McDonald AG, Olivieri A, O’Sullivan J (2009) Nomenclature and potential functions of copper amine oxidases. In: Floris G, Mondovì B (eds) Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology. CRC Press, Boca RatonGoogle Scholar
  2. Brazeau BJ, Johnson BJ, Wilmot CM (2004) Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective. Arch Biochem Biophys 428:22–31CrossRefPubMedGoogle Scholar
  3. Chen ZW, Datta S, DuBois JL, Klinman JP, Mathews FS (2010) Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity. Biochemistry 49:7393–7402CrossRefPubMedGoogle Scholar
  4. Davidson VL (2007) Protein-derived cofactors. Expanding the scope of post-translational modifications. Biochemistry 46:5283–5292CrossRefPubMedGoogle Scholar
  5. DuBois JL, Klinman JP (2005) Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover. Arch Biochem Biophys 433:255–265CrossRefPubMedGoogle Scholar
  6. DuBois JL, Klinman JP (2006) Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha. Biochemistry 45:3178–3188CrossRefPubMedGoogle Scholar
  7. Guss JM, Zanotti G, Salminen TA (2009) Copper amine oxidase crystal structures. In: Floris G, Mondovì B (eds) Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology. CRC Press, Boca RatonGoogle Scholar
  8. Janes SM, Mu D, Wemmer D, Smith AJ, Kaur S, Maltby D, Burlingame AL, Klinman JP (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 25:981–987CrossRefGoogle Scholar
  9. Kim M, Okajima T, Kishishita S, Yoshimura M, Kawamori A, Tanizawa K, Yamaguchi H (2002) X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase. Nat Struct Biol 9:591–596PubMedGoogle Scholar
  10. Mure M, Mills SA, Klinman JP (2002) Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry 41:9269–9278CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Departments of Chemistry and Molecular and Cell BiologyCalifornia Institute for Quantitative Biosciences, University of California, BerkeleyBerkeleyUSA
  2. 2.Department of Molecular and Cell BiologyCalifornia Institute for Quantitative Biosciences, University of California, BerkeleyBerkeleyUSA