Work

Structures and mechanism of the monoamine oxidase family

Year: 2011

Type: article

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.

Source: BioMolecular Concepts

DOI: 10.1515/bmc.2011.030

Authors: Helena Gaweska, Paul F. Fitzpatrick

Institution: The University of Texas at San Antonio Health Science Center

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $1,808

Funder: National Institute of General Medical Sciences