Monoamine oxidase: Difference between revisions

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|description='''Monoamine oxdiases'''  are a family of enzymes that catalyze the oxidation of monoamines and they are bound to the outer membrane of mitochondria .
|description='''Monoamine oxdiases'''  are enzymes bound to the outer membrane of mitochondria and they catalyze the oxidative deamination of monoamines.
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|type=Enzyme
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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. Monoamine oxidases contain the covalently bound cofactor FAD and are, thus, classified as flavoproteins.
 
Oxygen is used to remove an amine group from a molecule, resulting in the corresponding aldehyde and ammonia. Monoamine oxidases contain the covalently bound cofactor FAD and are, thus, classified as flavoproteins.

Revision as of 11:25, 21 May 2012


high-resolution terminology - matching measurements at high-resolution


Monoamine oxidase

Description

Monoamine oxdiases are enzymes bound to the outer membrane of mitochondria and they catalyze the oxidative deamination of monoamines.

Abbreviation: MAO


MitoPedia topics: Enzyme 


Oxygen is used to remove an amine group from a molecule, resulting in the corresponding aldehyde and ammonia. Monoamine oxidases contain the covalently bound cofactor FAD and are, thus, classified as flavoproteins.

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