Monoamine Oxidase Contains a Redox-active Disulfide

Mitochondrial monoamine oxidases A and B (MAO A and MAO B) are ubiquitous homodimeric FAD-containing oxidases that catalyze the oxidation of biogenic amines. Both enzymes play a vital role in the regulation of neurotransmitter levels in brain and are of interest as drug targets. However, little is k...

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Bibliographic Details
Published in:The Journal of biological chemistry 1998-06, Vol.273 (23), p.14074-14076
Main Authors: Sablin, Sergey O., Ramsay, Rona R.
Format: Article
Language:English
Subjects:
Animals
Binding Sites - physiology
Cattle
Dextroamphetamine - pharmacology
Disulfides - chemistry
Disulfides - metabolism
Dithionite - metabolism
Electron Transport - physiology
Enzyme Inhibitors - pharmacology
Flavoproteins - chemistry
Humans
Mercaptoethanol - metabolism
Mitochondria, Liver - enzymology
Monoamine Oxidase - chemistry
Oxidation-Reduction
Oxidoreductases - chemistry
Pyridines - metabolism
Spectrophotometry
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Summary:Mitochondrial monoamine oxidases A and B (MAO A and MAO B) are ubiquitous homodimeric FAD-containing oxidases that catalyze the oxidation of biogenic amines. Both enzymes play a vital role in the regulation of neurotransmitter levels in brain and are of interest as drug targets. However, little is known about the amino acid residues involved in the catalysis. The experiments reported here show that both MAO A and MAO B contain a redox-active disulfide at the catalytic center. The results imply that MAO may be a novel type of disulfide oxidoreductase and open the way to characterizing the catalytic and chemical mechanism of the enzyme.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.23.14074