Sandbox Reserved 641: Difference between revisions
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Glutamate dehydrogenase is a hexamer that contains two domains that have three subunits. GHD contains approximately 18 alpha helices and thirteen beta sheets. There is a large cleft that separates the two domains and allows for a substrate to enter and bind. The protein then closes around the substrate. For mammals only there is a structure that extends outward of the protein called the "antennae." | Glutamate dehydrogenase is a hexamer that contains two domains that have three subunits. GHD contains approximately 18 alpha helices and thirteen beta sheets. There is a large cleft that separates the two domains and allows for a substrate to enter and bind. The protein then closes around the substrate. For mammals only there is a structure that extends outward of the protein called the "antennae." | ||
Today, one of the primary research uses for glutamate dehydrogenase is to determine how well the human liver is functioning. If the level of GDH is too high that could indicate necrosis of the liver. | Today, one of the primary research uses for glutamate dehydrogenase is to determine how well the human liver is functioning. If the level of GDH is too high that could indicate necrosis of the liver. | ||
== '''Structure''' == | == '''Structure''' == | ||
