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Cited by 247Enzyme Structure and FunctionMetal-Catalyzed Oxygenation MechanismsAmino Acid Enzymes and Metabolism

Structures and mechanism of the monoamine oxidase family

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Gaweska, Helena, Fitzpatrick, Paul F.·2011·bmc
DOI 10.1515/bmc.2011.030PMC PMC3197729
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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.

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  • LDX reduces monoamine degradation by MAO inhibition.

    “The inhibition of DAT1, targeted by both drugs, leads to no reuptake of the DA to the cytosol [166]; LDX also reduces monoamine degradation by MAO inhibition [167, 168].”

    From Molecular Characterisation of the Mechanism of Action of Stimulant Drugs Lisdexamfetamine and Methylphenidate on ADHD Neurobiology: A Review (2022) · cites this paper as [167]

    The “Monoamine Oxidases A and B” section (page unavailable) says MAOs metabolize dopamine and other monoamines and discusses MAO inhibitors. It does not say that LDX inhibits MAO or reduces monoamine degradation, so the drug-specific claim is unsupported. (LLM, conf=0.84)

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Authors
Gaweska, H., & Fitzpatrick, P. F.
Affiliations
The University of Texas at San Antonio Health Science Center (US)
Corresponding author
Fitzpatrick, Paul F.
ORCID
Fitzpatrick, Paul F.
Venue
bmc
Publisher
Walter de Gruyter GmbH
Published
2011-08-13
Volume
2
Issue
5
Pages
365-377
ISSN
  • 1868-5021 (ISSN-L)
  • 1868-503X
DOI
10.1515/bmc.2011.030
PMC
PMC3197729
OpenAlex
W2058494541
Cited by
247
References
120
Citations by year
2026: 25 · 2025: 21 · 2024: 26 · 2023: 35 · 2022: 22 · 2021: 29 · 2020: 25 · 2019: 20 · 2018: 10 · 2017: 7 · 2016: 9 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 1
FWCI
2.04
Type
journal article
Language
en
Open access
Licence
Locations
  • BioMolecular Concepts (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institute of General Medical Sciences (F32GM097762, R01GM058698)
Topics
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords
monoamine oxidase, flavoprotein, FAD-binding domain, enzyme structure, catalytic mechanism, polyamine oxidation, amino acid oxidation, substrate binding site

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