glutamate dehydrogenase การใช้

• Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase, as follows:
• Glutamate dehydrogenase ( pGluDH ) separated by Counterimmunoelectrophoresis
• Glutamate dehydrogenase 2 is localized to the mitochondrion and acts as a homohexamer to recycle alpha-ketoglutarate.
• The other pathway for incorporating nitrogen onto the ?-carbon of amino acids involves the enzyme glutamate dehydrogenase ( GDH ).
• SIRT4 is a mitochondrial ADP-ribosyltransferase that inhibits mitochondrial glutamate dehydrogenase 1 activity, thereby downregulating insulin secretion in response to amino acids.
• Glutaminase is expressed and active in periportal hepatocytes, where it generates NH 3 ( ammonia ) for urea synthesis, as does glutamate dehydrogenase.
• First of all, glutamate can be converted to 2-oxoglutarate with expense of NAD + and H 2 O with help of glutamate dehydrogenase.
• Typically, the ?-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and ?-ketoglutarate.
• The key enzymes in these processes are : NADP-linked malic enzyme, NADP-linked isocitrate dehydrogenase, NADP-linked glutamate dehydrogenase and nicotinamide nucleotide transhydrogenase.
• Additionally, SGCs contain the glutamate related enzymes glutamate dehydrogenase and pyruvate carboxylase, and thus can supply the neurons not only with glutamine, but also with lactate.
• In addition this approach detected " gdhA " as direct target of Spot42 . " gdhA " codes for the glutamate dehydrogenase and links citrate cycle and nitrogen metabolism.
• He obtained the first direct evidence for the " one gene-one enzyme " hypothesis, using mutants of " Neurospora crassa " deficient in a specific enzyme called glutamate dehydrogenase.
• While the enzyme glutamate dehydrogenase ( GDH ) does not play a direct role in the assimilation, it protects the mitochondrial functions during periods of high nitrogen metabolism and takes part in nitrogen remobilization.
• The regulation of the synthesis of glutamate from ?-ketoglutarate is subject to regulatory control of the Citric Acid Cycle as well as mass action dependent on the concentrations of reactants involved due to the reversible nature of the transamination and glutamate dehydrogenase reactions.
• The enzyme represents a key link between catabolic and GLUD1 ( glutamate dehydrogenase 1 ) and GLUD2 ( glutamate dehydrogenase 2 ), and there are also at least 8 GLDH pseudogenes in the human genome as well, probably reflecting microbial influences on eukaryote evolution.
• The enzyme represents a key link between catabolic and GLUD1 ( glutamate dehydrogenase 1 ) and GLUD2 ( glutamate dehydrogenase 2 ), and there are also at least 8 GLDH pseudogenes in the human genome as well, probably reflecting microbial influences on eukaryote evolution.
• "' 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 ?-ketoglutarate, and vice versa.
• 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, ?-ketoglutarate and ammonia to glutamate and NAD ( P ) + ).