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From Proteopedia
Glutamate Dehydrogenase
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Glutamate dehydrogenase (GDH)is an enzyme found in the mitochondria of most organisms. GDH is used to remove the ketone group and replace it with an α-amine group on the α-carbon, which forms glutamate. Glutamate is one of the 20 essential amino acids. This is done in reverse to supply α-ketoglutarate to the tricarboxylic acid (TCA) cycle. GDH is an oxidoreductase, which is an enzyme that transfers electrons from one molecule (reductant/electron donor) to another molecule (oxidant/electron acceptor).
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. [1]
