Monoamine oxidase

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Monoamine oxidases (MAO) (EC 1.4.3.4) are a family of enzymes that catalyze the oxidation of monoamines.[2][3] They are found bound to the outer membrane of mitochondria in most cell types in the body. The enzyme was originally discovered by Mary Bernheim (maiden name: Hare) in the liver and was named tyramine oxidase.[4][5] They belong to the protein family of flavin-containing amine oxidoreductases.

Contents

Subtypes and tissue distribution

In humans there are two types of MAO: MAO-A and MAO-B.[6]

Function

Monoamine oxidases catalyze the oxidative deamination of monoamines. Oxygen is used to remove an amine group from a molecule, resulting in the corresponding aldehyde and ammonia. The general form of the catalyzed reaction (with R denoting an arbitrary group) is:

Monoamine oxidases contain the covalently-bound cofactor FAD and are, thus, classified as flavoproteins.

Substrate specificities

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