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Structures and mechanism of the monoamine oxidase family

2011/08/13 by Helena Gaweska, Paul F. Fitzpatrick · 1 citation
Biochemistry, Genetics and Molecular Biology · #Polyamine Metabolism and Applications #Amino Acid Enzymes and Metabolism #Photosynthetic Processes and Mechanisms

paper · doi:10.1515/bmc.2011.030

openalex publication_date 2011/08/13 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/29

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 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.

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