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.

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 the fields of food production and clinical biochemistry.

Storage and Stability

Lyophilized powder may be stored desiccated at 4°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Prepare fresh before use.