Amine oxidase (flavin-containing)

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Amine oxidase (flavin-containing) is a type of enzyme that catalyzes the oxidation of amines. This enzyme is part of the larger family of oxidoreductase enzymes, which are responsible for catalyzing oxidation-reduction reactions in various biological processes.

Function[edit | edit source]

The primary function of amine oxidase (flavin-containing) is to catalyze the oxidation of amines, a type of organic compound derived from ammonia. This process involves the removal of a hydrogen atom from the amine, resulting in the formation of an imine. The enzyme also plays a role in the metabolism of certain neurotransmitters, including serotonin and dopamine, which are essential for normal brain function.

Structure[edit | edit source]

Amine oxidase (flavin-containing) is a protein that consists of two identical subunits, each containing a flavin adenine dinucleotide (FAD) molecule. The FAD molecule is crucial for the enzyme's function, as it serves as a coenzyme that aids in the oxidation process. The structure of the enzyme allows it to bind to amines and facilitate their oxidation.

Clinical significance[edit | edit source]

Alterations in the activity of amine oxidase (flavin-containing) have been associated with various neurological disorders, including Parkinson's disease and depression. Inhibitors of this enzyme, such as monoamine oxidase inhibitors (MAOIs), are commonly used in the treatment of these conditions.

See also[edit | edit source]

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD