Chemical Properties
It is found in enzyme mother, higher plants and animals. The commercial product is usually crystallized from bovine liver, suspended in a suspension of 2 mol-L-1 ammonium sulfate solution. ph is 7. 20mg of enzyme per ml, viability is 450,000 units of enzyme per mg. no decrease in activity within 12 months, its aqueous solution may appear slightly turbid after a few months.
Uses
L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-ketoglutarate and carbon dioxide.
Biochem/physiol Actions
Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species. The bovine enzyme is characterized by three sets of properties: It has a reversible concentration-dependent association, producing higher molecular weight forms.Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
