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Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico

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CiteScore 2017: 2.50

SCImago Journal Rank (SJR) 2017: 0.861
Source Normalized Impact per Paper (SNIP) 2017: 0.722

ICV 2017: 131.30

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Volume 2, Issue 5


Structures and mechanism of the monoamine oxidase family

Helena Gaweska
  • Department of Biochemistry, University of Texas Health Science Center, San Antonio, TX 78229, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Paul F. Fitzpatrick
Published Online: 2011-08-13 | DOI: https://doi.org/10.1515/BMC.2011.030


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.

Keywords: enzyme mechanism; flavoproteins; L-amino acid oxidase; lysine-specific demethylase; monoamine oxidase; polyamine oxidase; protein structure; spermine oxidase

About the article

Corresponding author

Received: 2011-03-17

Accepted: 2011-06-17

Published Online: 2011-08-13

Published in Print: 2011-10-01

Citation Information: BioMolecular Concepts, Volume 2, Issue 5, Pages 365–377, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/BMC.2011.030.

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