Description
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
Abbr
L-Glutamic Dehydrogenase, Native (Proteus sp.)
Applications
This enzyme is useful for enzymatic determination of NH3, α-ketoglutaric acid and L-glutamic acid, and for assay of leucine aminopeptidase and urease. This enzyme is also used for enzymatic determination of urea when coupled with urease (URH-201) in clinical analysis.
Form
buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide
Enzyme Commission Number
EC 1.4.1.4
Activity
> 400 units/mg protein (biuret)
Molecular Weight
mol wt ~300 kDa
pH Stability
pH 6.0-8.5 (25°C, 20hr)
Michaelis Constant
1.1 X 10-3M (NH3), 3.4 X 10-4M (α-Ketoglutarate) 1.2 X 10-3M (L-Glutamate), 1.4 X 10-5M (NADPH), 1.5 X 10-5M (NADP+) Structure : 6 subunits (M.W.50 kDa) per mol of enzyme
Unit Definition
One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 8.3 at 30°C in the presence of ammonium ions and NADPH.
Optimum pH
8.5 (α-KG→L-Glu) 9.8 (L-Glu→α-KG)
Optimum temperature
45°C (α-KG−L-Glu) 45-55°C (L-Glu→α-KG)
Thermal stability
below 50°C (pH 7.4, 10min)
Inhibitors
Hg++, Cd++, p-chloromercuribenzoate, pyridine, 4-4′-dithiopyridine, 2,2′-dithiopyridine
Warnings
Do not confuse with non-specific L-GLDH, EC 1.4.1.3.
Synonyms
L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP)
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