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Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase

  • W. S. McIntire
  • D. M. Dooley
  • M. A. McGuirl
  • C. E. Cote
  • J. L. Bates
Part of the Journal of Neural Transmission book series (NEURAL SUPPL, volume 32)

Summary

Methylamine oxidase (MAOX) from Gram-positive soil bacterium Arthrobacter PI catalyzes the oxidation of CH3NH2 to H2C=O and NH4 + via reduction of O2 to H2O2. Past work indicates that MAOx is similar to mammalian plasma amine oxidase (PAO) and diamine oxidase (DAO), plant DAO, and yeast peroxisomal amine oxidase (YAO). All have Mr ≃ 170,000 and are composed of 2 identical subunits, each of which contains 1 atom of Cu(II) and one molecule of quinonoid cofactor. Herein, we report further evidence as to the striking similarity of these enzymes, and describe properties of MAOX which offer insights into understanding the eukaryotic oxidases. It is our belief that the structure of the quinone cofactor, and the Cu(II) site in MAOX are identical to these sites in PAO and DAO.

Keywords

Amine Oxidase Veteran Affair Medical Diamine Oxidase Electron Spin Echo Envelope Modulation Resonance Raman Spectrum 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1990

Authors and Affiliations

  • W. S. McIntire
    • 1
  • D. M. Dooley
    • 2
  • M. A. McGuirl
    • 2
  • C. E. Cote
    • 2
  • J. L. Bates
    • 2
  1. 1.Molecular Biology Division, Department of Veterans Affairs Medical Center, San Francisco, Department of Biochemistry and Biophysics and Department of AnesthesiaUniversity of CaliforniaSan FranciscoUSA
  2. 2.Department of ChemistryAmherst CollegeAmherstUSA

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