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L-Glutamate Oxidase, E. coli Recombinant

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:glutamate oxidase, GluOx, GLOD, L-GLOD, L-glutamic acid oxidase, l-GlOx
  • Species:Streptomyces
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Cat. No. Size Price


New 80049 25 U
Product Details
Technical Data

Type

Recombinant protein

Description

Recombinantly produced in E. coli, L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes oxidative deamination of the α-amino group of L-glutamate to 2-ketoglutarate, with concomitant reduction of molecular oxygen and water to ammonia and hydrogen peroxide.

Source

E. coli

Biological Activity

One unit equals the amount of enzyme that liberates 1 micromole 2-ketoglutarate per minute with 3-methyl-2-benzothiazolone hydrazone hydrochloride as substrate at 30°C, pH 7.4 (Soda K, et al. 1968).

Applications

Biologically active protein

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store below -15°C

Physical Appearance

White lyophilized (freeze-dried) powder.

Note

This product is furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Summary

Research topic

Neural tissue markers, Neurodegenerative disease

Summary

In 1983, during research on soy sauce, YAMASA CORPORATION discovered that some Streptomyces species produce glutamate oxidase, which specifically acts on L-glutamate.

L-glutamate oxidase (EC 1.4.3.11) is an enzyme that catalyzes oxidative deamination of the α-amino group of L-glutamate to 2-ketoglutarate, with concomitant reduction of molecular oxygen and water to ammonia and hydrogen peroxide. L-glutamate oxidase is a member of the general oxidoreductase family, which catalyzes the CH-OH group of the substrate and uses NAD+ or NADP+ as the cofactor. The systematic name of this enzyme class is L-glutamate:oxygen oxidoreductase (deaminating), which is also called glutamate (acceptor) dehydrogenase, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor) or L-glutamic acid oxidase.

L-glutamate, the substrate of the reaction catalyzed by L-glutamate oxidase, has a flavor-enhancing property that creates the sensation of “umami”, and the monosodium salt of L-glutamate is widely used as a seasoning for cooking and as a food additive. Since the L-glutamic acid content of foods can be readily determined by means of a kit or a sensor employing L-glutamate oxidase, this enzyme is now indispensable in the field of compositional analysis of foods.

Moreover, L-glutamate is also the principal excitatory neurotransmitter in the brain. Furthermore, the excessive release of this amino acid may play a pivotal role in the neuronal death associated with different neurological disorders. Therefore, L-glutamate and L-glutamate oxidase play important roles in clinical biochemistry. In the field of cerebral nerve science, attempts to analyze L-glutamic acid have been energetically pursued by use of a microdialysis and a microsensor in combination. Most enzymes employed in the sensor are L-glutamate oxidases.

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