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spinqualitylabelsall models Crystal Structure of Human Monoamine Oxidase A with Harmine Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Hey Austen! I figure it out! (Actually Savannah did last year...) In the section above you can include your scene where it says "Insert iotional scene name here". See Savannah's example below.

spinqualitylabelsall models ABCB1: 3.4 Å resolution Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Contents 1 Introduction 2 Structure 3 Function 4 Disease 5 Relevance 6 Structural highlights 7 References

Introduction

(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 [1]. Each isoform is characterized by its unique substrate specificity and inhibitor sensitivity. For example, MAO-A (found primarily in catecholaminergic neurons) preferentially oxidizes 5-hydroxytryptamine (5-HT), epinephrine, and norepinephrine; while MAO-B (found primarily in sertonergic neurons) 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 since heightened levels of H₂O₂ promote apoptosis signalling within cells [2]. Due to the important role MAOs play in controlling the prevalence of various neurotransmitters in the body as well as producing reactive oxygen species (ROS), an imbalance of these enzymes may be detrimental to human health.

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

Amino Terminus

Carboxy Terminus

Structure

MAO-A is a monomer composeare present in the d of 527 amino acids, with a molecular weight of 60,512±6 Da. The first 497 amino acids in the polypeptide exist in the cytoplasm of the cell; while amino acids 498—518 are involved in an α-helix that anchors the enzyme to the mitochondrial membrane. Furthermore, amino acids 519—527 are present in the intermembrane of the mitochondria [3].

Function

Disease

Relevance

Structural highlights

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References