Description
GDH is an oxidoreductase enzyme which relates carbon and nitrogen metabolism. It catalyzes the reduction of α-ketoglutarate and ammonia to L-glutamate and vice versa. This enzyme is a robust and ideal candidate for research use, and industrial applications in the diagnostics and food industries.
Abbr
GLDH, Recombinant (Microbial)
Species
Thermophilic Bacterium
Enzyme Commission Number
EC 1.4.1.2
Activity
> 90 U/mg protein
Molecular Weight
270 kDa; Homohexameric ( 45 kDa per subunit)
Concentration
Protein concentration: > 13% (w/w)
Unit Definition
One unit is defined as the conversion of 1umol of α-ketoglutarate into glutamate, in 1 minute at 50°C at pH 8.0
Thermal stability
20-70°C, Maintains over 85% of its activity for 8 hours at 50°C.
Synonyms
glutamate dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD+); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD+-dependent glutamate dehydrogenase; NAD+-dependent glutamic dehydrogenase; NAD+-glutamate dehydrogenase; NAD+-linked glutamate dehydrogenase; NAD+-linked glutamic dehydrogenase; NAD+-specific glutamic dehydrogenase; NAD+-specific glutamate dehydrogenase; NAD+:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase; GLDH; EC 1.4.1.2