Sandbox WWC2: Difference between revisions

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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 [https://books.google.com/books?id=6p_cBAAAQBAJ&pg=PA23&lpg=PA23&dq=h2o2+produced+by+mao+neutralized+by&source=bl&ots=xMja8jxpkk&sig=-o5KLxfPBe7m_selXCo9iVt8OuY&hl=en&sa=X&ved=0ahUKEwiDt_qYlJHMAhVIeD4KHcIDC3UQ6AEISzAF#v=onepage&q=h2o2%20produced%20by%20mao%20neutralized%20by&f=false]. 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 <scene name='69/696303/N_to_c_rainbow/3'>polypeptide chain</scene> .

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== 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,

Unlike dimers MAO-B and rat MAO-A, human MAO-A is a monomer composed 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 (this can clearly be seen in the provided crystal structure as the only α-helix that significantly sticks out away from the rest of the globular structure). Furthermore, amino acids 519—527 are present in the intermembrane of the mitochondria [http://www.uniprot.org/uniprot/P2139]. The active site of MAO-A is a single hydrophobic pocket with a volume of approximately 550 cubic Å [http://www.pnas.org/content/102/36/12684.full].

amino acids 519—527 are present in the intermembrane of the mitochondria [http://www.uniprot.org/uniprot/P2139].

== Function ==

== Function

== Disease ==

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@@ Line 11: / Line 11: @@
 in which the H<sub>2</sub>O<sub>2</sub> is enzymatically removed by glutathione reductase and glutathione peroxidase to produce a reduced glutathione since heightened levels of H<sub>2</sub>O<sub>2</sub> promote apoptosis signalling within cells [https://books.google.com/books?id=6p_cBAAAQBAJ&pg=PA23&lpg=PA23&dq=h2o2+produced+by+mao+neutralized+by&source=bl&ots=xMja8jxpkk&sig=-o5KLxfPBe7m_selXCo9iVt8OuY&hl=en&sa=X&ved=0ahUKEwiDt_qYlJHMAhVIeD4KHcIDC3UQ6AEISzAF#v=onepage&q=h2o2%20produced%20by%20mao%20neutralized%20by&f=false]. 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 <scene name='69/696303/N_to_c_rainbow/3'>polypeptide chain</scene> .
@@ Line 18: / Line 16: @@
 == 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,
+Unlike dimers MAO-B and rat MAO-A, human MAO-A is a monomer composed 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 (this can clearly be seen in the provided crystal structure as the only α-helix that significantly sticks out away from the rest of the globular structure). Furthermore, amino acids 519—527 are present in the intermembrane of the mitochondria [http://www.uniprot.org/uniprot/P2139]. The active site of MAO-A is a single hydrophobic pocket with a volume of approximately 550 cubic Å [http://www.pnas.org/content/102/36/12684.full].
-amino acids 519—527 are present in the intermembrane of the mitochondria [http://www.uniprot.org/uniprot/P2139].
-== Function ==
+== Function
 == Disease ==