9029-12-3

Found in enzyme mothers, higher plants, and animals. The commercial product is typically a crystal suspension extracted from bovine liver in a 2 mol·L-1 ammonium sulfate solution. Its pH is 7. Each ml contains 20 mg of enzyme, with an activity of 450,000 units per mg. The activity remains stable for 12 months, but the aqueous solution may become slightly turbid after a few months.

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.