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・ Glutamate 5-kinase
・ Glutamate aspartate transporter
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Glutamate dehydrogenase
・ Glutamate dehydrogenase 1
・ Glutamate flavoring
・ Glutamate formimidoyltransferase
・ Glutamate hypothesis of schizophrenia
・ Glutamate N-acetyltransferase
・ Glutamate permease
・ Glutamate racemase
・ Glutamate receptor
・ Glutamate receptor-interacting protein
・ Glutamate synthase (ferredoxin)
・ Glutamate synthase (NADH)
・ Glutamate synthase (NADPH)
・ Glutamate-1-semialdehyde
・ Glutamate-1-semialdehyde 2,1-aminomutase


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Glutamate dehydrogenase : ウィキペディア英語版
Glutamate dehydrogenase

Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Glutamate dehydrogenase also has a very low affinity for ammonia (high Michaelis constant K_m of about 1 mM), and therefore toxic levels of ammonia would have to be present in the body for the reverse reaction to proceed (that is, α-ketoglutarate and ammonia to glutamate and NAD(P)+). In bacteria, the ammonia is assimilated to amino acids via glutamate and aminotransferases. In plants, the enzyme can work in either direction depending on environment and stress.〔 Transgenic plants expressing microbial GLDHs are improved in tolerance to herbicide, water deficit, and pathogen infections. They are more nutritionally valuable.

Image:Glutaminsäure - Glutamic acid.svg|Glutamate
Image:Alpha-ketoglutaric acid.png |α-Ketoglutarate

The enzyme represents a key link between catabolic and metabolic pathways, and is, therefore, ubiquitous in eukaryotes.
==Clinical application==

GLDH can be measured in a medical laboratory to evaluate the liver function. Elevated blood serum GLDH levels indicate liver damage and GLDH plays an important role in the differential diagnosis of liver disease, especially in combination with aminotransferases. GLDH is localised in mitochondria, therefore practically none is liberated in generalised inflammatory diseases of the liver such as viral hepatitides. Liver diseases in which necrosis of hepatocytes is the predominant event, such as toxic liver damage or hypoxic liver disease, are characterised by high serum GLDH levels. GLDH is important for distinguishing between acute viral hepatitis and acute toxic liver necrosis or acute hypoxic liver disease, particularly in the case of liver damage with very high aminotransferases. In clinical trials, GLDH can serve as a measurement for the safety of a drug.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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