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==Introduction==
==Introduction==


Monoamine oxidase A (MAO-A) is an flavoenzyme, encoded in the MAOA gene on the X chromosome, that is present throughout the brain, central nervous system, and stomach. Two isoforms of this enzyme are expressed on the outer surface of the mitochondrial membrane, MAO-A and MAO-B, and both are responsible for the oxidative deamination of various neurotransmitters and dietary amines. Each isoform is characterized by its unique substrate specificity and inhibitor sensitivity (Kaludercic et al.). For example, MAO-A preferentially oxidizes 5-hydroxytryptamine (5-HT), epinephrine, and norepinephrine; while MAO-B prefers phenylethylamine and benzylamine. Both of these enzymes oxidize dopamine, tyramine, and N,N-dimethyltryptamine.  
Monoamine oxidase A (MAO-A) is an oxidoreductase flavoenzyme, encoded in the MAOA gene on the X chromosome; the enzyme is present throughout the brain, central nervous system, and stomach. Two isoforms of this enzyme (MAO-A and MAO-B) are expressed on the outer surface of the mitochondrial membrane, and both are responsible for the oxidative deamination of various neurotransmitters and dietary amines. Each isoform is characterized by its unique substrate specificity and inhibitor sensitivity (Kaludercic et al.). For example, MAO-A preferentially oxidizes 5-hydroxytryptamine (5-HT), epinephrine, and norepinephrine; while MAO-B prefers phenylethylamine and benzylamine. Both of these enzymes oxidize dopamine, tyramine, and N,N-dimethyltryptamine as well as their respective unique substrates according to the following reaction:
 
                                                        RCH2NHR' + H2O + O2 --> RCHO + R'NH2 + H2O2
 
in which the H2O2 is enzymatically removed by glutathione reductase and glutathione peroxidase to produce a reduced glutathione.  
 


<Structure load='2Z5X' size='500' frame='top' align='right' caption='Crystal Structure of Human Monoamine Oxidase A with Harmine' scene='Insert optional scene name here' />
<Structure load='2Z5X' size='500' frame='top' align='right' caption='Crystal Structure of Human Monoamine Oxidase A with Harmine' scene='Insert optional scene name here' />

Revision as of 20:25, 15 April 2016

IntroductionIntroduction

Monoamine oxidase A (MAO-A) is an oxidoreductase flavoenzyme, encoded in the MAOA gene on the X chromosome; the enzyme is present throughout the brain, central nervous system, and stomach. Two isoforms of this enzyme (MAO-A and MAO-B) are expressed on the outer surface of the mitochondrial membrane, and both are responsible for the oxidative deamination of various neurotransmitters and dietary amines. Each isoform is characterized by its unique substrate specificity and inhibitor sensitivity (Kaludercic et al.). For example, MAO-A preferentially oxidizes 5-hydroxytryptamine (5-HT), epinephrine, and norepinephrine; while MAO-B prefers phenylethylamine and benzylamine. Both of these enzymes oxidize dopamine, tyramine, and N,N-dimethyltryptamine as well as their respective unique substrates according to the following reaction:

                                                        RCH2NHR' + H2O + O2 --> RCHO + R'NH2 + H2O2

in which the H2O2 is enzymatically removed by glutathione reductase and glutathione peroxidase to produce a reduced glutathione.


Crystal Structure of Human Monoamine Oxidase A with Harmine

Drag the structure with the mouse to rotate

The , illustrated in the protein image to the right, in conjunction with the color key, below, indicates the directionality of the polypeptide chain.

 Amino Terminus                 Carboxy Terminus 

How many alpha helices are in this structure?

None
One
Four.



FunctionFunction

DiseaseDisease

RelevanceRelevance

Structural highlightsStructural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Dana Emmert, Evan Muir