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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