ArticleJournal of neural transmission (Vienna, Austria : 1996)2007
Do monomeric vs dimeric forms of MAO-A make a difference? A direct comparison of the catalytic properties of rat and human MAO-A's.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Exploring Disulfide Bridge as a Tool to Improve Pioglitazone's Neuroprotective Potential: Toward the Development of Prolonged-Acting MAO-B/PPARγ Modulators.ChemMedChem · 2026Article
- Advances in the Understanding of Protein-Protein Interactions in Drug Metabolizing Enzymes through the Use of Biophysical Techniques.Frontiers in pharmacology · 2017Review
- Computational modeling of the direct hydride transfer mechanism for the MAO catalyzed oxidation of phenethylamine and benzylamine: ONIOM (QM/QM) calculations.Journal of neural transmission (Vienna, Austria : 1996) · 2013Article
- Computational investigation on the structure-activity relationship of the biradical mechanism for monoamine oxidase.Journal of neural transmission (Vienna, Austria : 1996) · 2011Article
- Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.Biochemistry · 2009Review
- New insights into the structures and functions of human monoamine oxidases A and B.Journal of neural transmission (Vienna, Austria : 1996) · 2007Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The recent crystallographic structures of human MAO-A and rat MAO-A have shown that human MAO-A is monomeric whereas rat MAO-A is a dimer, even though they share approximately 90% sequence identity. The functional significance of this structural difference is unknown. Therefore, biochemical approaches in this paper were performed to investigate the influence of oligomeric state on functional properties of human and rat MAO-A's. The data show that 1) dimerization of MAO-A increases its structural stability; 2) the differences in kinetic properties may be caused by differences in active site structures as a result of differences in oligomeric states of the human and the rat enzymes; 3) QSAR studies show rat MAO-A as well as human MAO-A catalysis occur via proton abstraction mechanisms, and the binding of substrates is similar for both enzymes.
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