Sandbox Reserved 697

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This Sandbox is Reserved from 30/01/2013, through 30/12/2013 for use in the course "Biochemistry II" taught by Hannah Tims at the Messiah College. This reservation includes Sandbox Reserved 686 through Sandbox Reserved 700.

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spinqualitylabelsall models Monoamine Oxidase Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Monoamine Oxidases

Monoamine oxidases (MAOs) are a class of enzyme that are localized to the outer membrane of the mitochondria and catalyzes the oxidative deamination of different monoamines. There are two subtypes of MAOs: and , which are closely related in stucture, but each has different substrate and inhibitor specificities. The two subtypes of MAO shown were those of humans, which can vary between different species of mammals. Note that human MAO-A is monomeric while human MAO-B forms a dimer.

Substrates for MAO-A include dopamine, serotonin and norepinephrine. The is located in the center of the protein shown in green. Additionally, MAO-A (and MAO-B) bind flavin adenine dinucleotide (FAD) at an shown in cyan which also is involved with the activity of the enzyme. This site of FAD covalent attachment is very conserved among MAOs. MAOs are anchored into the outer membrane of the mitochondria by a shown in yellow. All of these domains are highly conserved among MAO-As of different species.

MAO-B also binds similar monoamines to MAO-A, but preferentially binds beta-phenylethylamines and benzylamine. The is shown in green with the domain predicted to form the shown in red. The located in the center of the protein binds the inhibitor to it covalently. The inhibitor shown is pargyline.