Sandbox Reserved 477: Difference between revisions

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NAD+ is the most common <scene name='Sandbox_Reserved_477/Ligand/1'>ligand</scene> for the binding of GAPDH. A ligand is a molecule that binds to a central atom to form a complex. NAD+ expresses negative cooperativity in relation to GAPDH; as NAD+ binds to the protein, the protein's affinity for the ligand decreases.

<scene name='Sandbox_Reserved_477/Hydrophobic_residues/1'>hydrophobic residues</scene>

Due this enzyme's high content of <scene name='Sandbox_Reserved_477/Hydrophobic_residues/1'>hydrophobic residues</scene>, GAPDH maintains efficient stability by numerous hydrophobic interactions within the molecule.

[[Image:DomainAlisha.png| NAD Binding Domain | left | thumb | 300px]]

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'''''Glyceraldehyde-3-Phosphate Dehydrogenase''''' deficiency is a rare genetic disorder in which an individual has a deficiency of GAPDH, which is heavily involved in breaking down carbohydrates consumed in the diet in order to produce energy. This condition is asymptomatic and affects less than 200,000 people in the United States. GAPDH deficiency also occurs in plants, known as plastidial GAPDH deficiency. In plants, glycolysis occurs in both the cytosol and plastids. In a chloroplast/plastid-localized GAPDH isoform, gapcp, these double mutants have produced drastic phenotypes of arrested root development, dwarfism, and sterility.

'''''Glyceraldehyde-3-Phosphate Dehydrogenase''''' deficiency is a rare genetic disorder in which an individual has a deficiency of GAPDH, which is heavily involved in breaking down carbohydrates consumed in the diet in order to produce energy. This condition is asymptomatic and affects less than 200,000 people in the United States. "GAPDH deficiency also occurs in plants, known as plastidial GAPDH deficiency. In plants, glycolysis occurs in both the cytosol and plastids. In a chloroplast/plastid-localized GAPDH isoform, gapcp, these double mutants have produced drastic phenotypes of arrested root development, dwarfism, and sterility." <ref>Muñoz-Bertomeu, J. (2009). Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in arabidosis. Plant Physiology, 151(2), 541-558. Retrieved from http://www.jstor.org/stable/40537793</ref> GAPDH is a critical enzyme for all organisms. Major '''''mutations''''' in this enzyme could lead to almost immediate death of the cell. Nevertheless, GAPDH is not just a glycolytic protein. It is a multidimensional protein with nuclear, cytoplasmic and membrane functions. GAPDH may be involved in apoptosis and age-related neuronal diseases, such as Alzheimers; a subcellular reduction in GAPDH glycolytic activity (ie intracellular differences) is found in Alzheimer's and Huntington's disease cells. GAPDH is involved in the molecular mechanisms that are responsible for pathogenesis in the CAG trinucleotide repeat diseases. Eight inherited neurodegenerative diseases are known to be caused by expansion of the CAG repeat. It is possible that GAPDH's interaction with mutant proteins may damage brain neurons.

GAPDH is a critical enzyme for all organisms. Major '''''mutations''''' in this enzyme could lead to almost immediate death of the cell. Nevertheless, GAPDH is not just a glycolytic protein. It is a multidimensional protein with nuclear, cytoplasmic and membrane functions. GAPDH may be involved in apoptosis and age-related neuronal diseases, such as Alzheimers; a subcellular reduction in GAPDH glycolytic activity (ie intracellular differences) is found in Alzheimer's and Huntington's disease cells. GAPDH is involved in the molecular mechanisms that are responsible for pathogenesis in the CAG trinucleotide repeat diseases. Eight inherited neurodegenerative diseases are known to be caused by expansion of the CAG repeat. It is possible that GAPDH's interaction with mutant proteins may damage brain neurons.

Sandbox Reserved 477: Difference between revisions

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@@ Line 21: / Line 21: @@
 NAD+ is the most common <scene name='Sandbox_Reserved_477/Ligand/1'>ligand</scene> for the binding of GAPDH. A ligand is a molecule that binds to a central atom to form a complex. NAD+ expresses negative cooperativity in relation to GAPDH; as NAD+ binds to the protein, the protein's affinity for the ligand decreases.
-<scene name='Sandbox_Reserved_477/Hydrophobic_residues/1'>hydrophobic residues</scene>
+Due this enzyme's high content of <scene name='Sandbox_Reserved_477/Hydrophobic_residues/1'>hydrophobic residues</scene>, GAPDH maintains efficient stability by numerous hydrophobic interactions within the molecule.
 [[Image:DomainAlisha.png| NAD Binding Domain | left | thumb | 300px]]
@@ Line 37: / Line 37: @@
 ----
-'''''Glyceraldehyde-3-Phosphate Dehydrogenase''''' deficiency is a rare genetic disorder in which an individual has a deficiency of GAPDH, which is heavily involved in breaking down carbohydrates consumed in the diet in order to produce energy. This condition is asymptomatic and affects less than 200,000 people in the United States. GAPDH deficiency also occurs in plants, known as plastidial GAPDH deficiency. In plants, glycolysis occurs in both the cytosol and plastids. In a chloroplast/plastid-localized GAPDH isoform, gapcp, these double mutants have produced drastic phenotypes of arrested root development, dwarfism, and sterility.
+'''''Glyceraldehyde-3-Phosphate Dehydrogenase''''' deficiency is a rare genetic disorder in which an individual has a deficiency of GAPDH, which is heavily involved in breaking down carbohydrates consumed in the diet in order to produce energy. This condition is asymptomatic and affects less than 200,000 people in the United States. "GAPDH deficiency also occurs in plants, known as plastidial GAPDH deficiency. In plants, glycolysis occurs in both the cytosol and plastids. In a chloroplast/plastid-localized GAPDH isoform, gapcp, these double mutants have produced drastic phenotypes of arrested root development, dwarfism, and sterility." <ref>Muñoz-Bertomeu, J. (2009). Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in arabidosis. Plant Physiology, 151(2), 541-558. Retrieved from http://www.jstor.org/stable/40537793</ref> GAPDH is a critical enzyme for all organisms. Major '''''mutations''''' in this enzyme could lead to almost immediate death of the cell. Nevertheless, GAPDH is not just a glycolytic protein. It is a multidimensional protein with nuclear, cytoplasmic and membrane functions. GAPDH may be involved in apoptosis and age-related neuronal diseases, such as Alzheimers; a subcellular reduction in GAPDH glycolytic activity (ie intracellular differences) is found in Alzheimer's and Huntington's disease cells. GAPDH is involved in the molecular mechanisms that are responsible for pathogenesis in the CAG trinucleotide repeat diseases. Eight inherited neurodegenerative diseases are known to be caused by expansion of the CAG repeat. It is possible that GAPDH's interaction with mutant proteins may damage brain neurons.
-GAPDH is a critical enzyme for all organisms. Major '''''mutations''''' in this enzyme could lead to almost immediate death of the cell. Nevertheless, GAPDH is not just a glycolytic protein. It is a multidimensional protein with nuclear, cytoplasmic and membrane functions. GAPDH may be involved in apoptosis and age-related neuronal diseases, such as Alzheimers; a subcellular reduction in GAPDH glycolytic activity (ie intracellular differences) is found in Alzheimer's and Huntington's disease cells. GAPDH is involved in the molecular mechanisms that are responsible for pathogenesis in the CAG trinucleotide repeat diseases. Eight inherited neurodegenerative diseases are known to be caused by expansion of the CAG repeat. It is possible that GAPDH's interaction with mutant proteins may damage brain neurons.