G1924
L-Glutamate Oxidase from Streptomyces sp.
recombinant, expressed in E. coli
Synonym(s):
L-Glutamate:oxygen oxidoreductase (deaminating)
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About This Item
recombinant
expressed in E. coli
Quality Level
form
solid
specific activity
≥5 units/mg protein
mol wt
120 kDa
storage temp.
−20°C
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General description
L-Glutamate Oxidase (LGOX) from Streptomyces sp is secreted extracellularly in the wheat bran pre cultivation medium. It corresponds to a molecular weight of 120 kDa with monomer subunit of 61 kDa. The structure of LGOX comprises of hexamer and has flavin adenine dinucleotide prosthetic group.
This product has a 6xHistidine tag with a thrombin cleavage site.
Application
L-Glutamate Oxidase from Streptomyces sp may be used:
- as a reference enzyme in hydrogelpoly(carbamoylsulphonate) based immobilization for biosensor development
- as a component of pencil graphite electrode for biosensing L-glutamate
Biochem/physiol Actions
L-Glutamate Oxidase (LGOX) catalyzes the oxidative deamination of L-glutamate to α-ketoglutarate, ammonia and hydrogen peroxide. LGOX is industrially produced and is exploited majorly as a biosensor for L-glutamate detection and in the L-glutamate kits.
Unit Definition
One unit will form 1.0 micromole of alpha-ketoglutaric acid from L-glutamic acid per minute at pH 7.4 at 30 deg C.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Isolation, purification, and characterization of L-glutamate oxidase from Streptomyces sp. 18G
Electronic journal of Biotechnology, 7(3), 09-10 (2004)
L-Glutamate biosensor based on l-glutamate oxidase immobilized onto ZnO nanorods/polypyrrole modified pencil graphite electrode
Biochemical Engineering Journal, 105, 428-436 (2016)
Comparative study of hydrogel-immobilized L-glutamate oxidases for a novel thick-film biosensor and its application in food samples
Biotechnology Letters, 22(4), 267-272 (2000)
The FEBS journal, 276(14), 3894-3903 (2009-06-18)
L-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6, which catalyzes the oxidative deamination of L-glutamate, has attracted increasing attention as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry. The precursor of LGOX, which has a
Cell chemical biology, 26(11), 1501-1514 (2019-09-10)
Imidazole glycerol phosphate synthase (ImGPS) is an allosteric bienzyme complex in which substrate binding to the synthase subunit HisF stimulates the glutaminase subunit HisH. To control this stimulation with light, we have incorporated the photo-responsive unnatural amino acids phenylalanine-4'-azobenzene (AzoF)
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