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Author Notes:

Correspondence: Dr. Dale E. Edmondson, Department of Biochemistry, Emory University 1510 Clifton Rd. Atlanta, GA 30322; Ph. No.:404-727-5972; Fax: 404-727-2738; Email: deedmon@emory.edu

Acknowledgments: The following former and present graduate and postdoctoral students are acknowledged for their contributions to the work described her include: Paige Newton Vinson, Richard Miller, Min Li, Franta Hubalek, Luigi DeColibus, Milagros Aldeco, and Jin Wang.

Subjects:

Research Funding:

The work described in this review was supported by NIH grant GM-29433, by Ministry of Science and Education Grants (Italy) FIRB and COFIN04, and by Fondazione MINTAS.

C.B. is supported by an Investigator Fellowship from Collegio Ghislieri, Pavia, Italy.

Keywords:

  • Monoamine oxidases
  • MAO A
  • MAO B
  • flavin coenzymes
  • amine neurotransmitter
  • QSAR
  • proton abstraction
  • expression in Pichia pastoris
  • x-ray structures

Structural insights into the mechanism of amine oxidation by monoamine oxidases A and B

Tools:

Journal Title:

Archives of Biochemistry and Biophysics

Volume:

Volume 464, Number 2

Publisher:

, Pages 269-276

Type of Work:

Article | Post-print: After Peer Review

Abstract:

Due to their pharmacological importance in the oxidation of amine neurotransmitters, the membrane-bound flavoenzymes monoamine oxidase A and monoamine oxidase B have attracted numerous investigations and, as a result, two different mechanisms; the single electron transfer and the polar nucleophilic mechanisms, have been proposed to describe their catalytic mechanisms. This review compiles the recently available structural data on both enzymes with available mechanistic data as well as current NMR data on flavin systems to provide an integration of the approaches. These conclusions support the proposal that a polar nucleophilic mechanism for amine oxidation is the most consistent mechanistic scheme as compared with the single electron transfer mechanism mechanism.

Copyright information:

© 2007 Esevier

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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