Description
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 α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate.
Appearance
White/off white powder
Enzyme Commission Number
EC 1.4.1.3
Activity
> 500U /mg protein
Molecular Weight
260 kDa (gel)
Michaelis Constant
9.5×10-3M (NH3); 5.0×10-3M (α-Ketoglutarate); 8.4×10-5M (NADH)
Unit Definition
One unit will convert one micromole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30°C.
Optimum pH
8.5(α-KG→L-Glu)
Thermal stability
< 60°C (pH8.3, 10min)
Inhibitors
Ag+, Hg2+, Cu2+, Zn2+ .
Preparation Instructions
The enzyme is reconstituted in 100mM Tris-HCl buffer, pH 8.3 for activity assay.
Pathway
Arginine and proline metabolism; D-Glutamine and D-glutamate metabolism; Glutamate metabolism; Nitrogen metabolism; Metabolism of amino acids.
Function
ATP binding; GTP binding; glutamate dehydrogenase [NAD(P)+] activity; glutamate dehydrogenase activity; nucleotide binding; oxidoreductase activity.
Synonyms
glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase
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