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Enzymes for Research, Diagnostic and Industrial Use

Glutamate Dehydrogenase from Thermophilic Bacterium, recombinant

Cat No.
NATE-1701
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)
Source
E. coli
Species
Thermophilic Bacterium
Form
Lyophilized powder
Enzyme Commission Number
EC 1.4.1.2
Activity
> 90 U/mg protein
CAS No.
9001-46-1
Molecular Weight
270 kDa; Homohexameric ( 45 kDa per subunit)
Concentration
Protein concentration: > 13% (w/w)
pH Stability
7-8.5
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
Optimum pH
8
Optimum temperature
50°C
Thermal stability
20-70°C, Maintains over 85% of its activity for 8 hours at 50°C.
Storage
at -20 °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
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