Skip to content
BY-NC-ND 3.0 license Open Access Published by De Gruyter August 13, 2011

Structures and mechanism of the monoamine oxidase family

  • Helena Gaweska and Paul F. Fitzpatrick EMAIL logo
From the journal Biomolecular Concepts

Abstract

Members of the monoamine oxidase family of flavoproteins catalyze the oxidation of primary and secondary amines, polyamines, amino acids, and methylated lysine side chains in proteins. The enzymes have similar overall structures, with conserved flavin adenine dinucleotide (FAD)-binding domains and varied substrate-binding sites. Multiple mechanisms have been proposed for the catalytic reactions of these enzymes. The present review compares the structures of different members of the family and the various mechanistic proposals.


Corresponding author

Received: 2011-3-17
Accepted: 2011-6-17
Published Online: 2011-08-13
Published in Print: 2011-10-01

©2011 by Walter de Gruyter Berlin Boston

This article is distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Downloaded on 29.3.2024 from https://www.degruyter.com/document/doi/10.1515/BMC.2011.030/html
Scroll to top button