Description
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. 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.
Abbr
L-GLDH, Native (Bovine)
Form
Type I, ammonium sulfate suspension, Suspension in 2.0 M (NH4)2SO4 solution; Type II, lyophilized powder, Contains primarily Citrate buffer salt; Type III, aqueous glycerol solution, Solution in 50% glycerol, pH 7.3.
Enzyme Commission Number
EC 1.4.1.3
Activity
Type I, > 40 units/mg protein; Type II, > 20 units/mg protein; Type III, > 35 units/mg protein.
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.
Warnings
Protein determined by biuret
Pathway
Alanine, aspartate and glutamate metabolism, organism-specific biosystem; Alanine, aspartate and glutamate metabolism, conserved biosystem; D-Glutamine and D-glutamate metabolism, organism-specific biosystem
Function
ATP binding; GTP binding; glutamate dehydrogenase (NAD+) activity
Synonyms
glutamic dehydrogenase; glutamate dehydrogenase [NAD (P)]; 9029-12-3; glutamate dehydrogenase [NAD (P)+]; EC 1.4.1.3; L-GLDH; L-Glutamate:NAD[P]+ Oxidoreductase (deaminating)
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