L-Glutamic Dehydrogenase from bovine liver Type I, ammonium sulfate suspension, ≥40 units/mg protein

Properties

Related Categories	1.4.x.x Acting on CH-NH₂, 1.x.x.x Oxidoreductases, Biochemicals and Reagents, Enzyme Class Index, Enzymes, Inhibitors, and Substrates, General Metabolic Enzymes, General Metabolic Enzymes A-H, Metabolomics More...
type	Type I
form	ammonium sulfate suspension
storage temp.	2-8°C
Gene Information	cow ... GLUD1(281785)

Description

Analysis Note

Protein determined by biuret

Unit Definition

One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.3 at 25 °C, in the presence of ammonium ions.

Physical form

Suspension in 2.0 M (NH₄)₂SO₄ solution, pH 7.0

Biochem/physiol Actions

L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate<<<24,25>>>.

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.