1.4.3.11: L-glutamate oxidase
This is an abbreviated version!
For detailed information about L-glutamate oxidase, go to the full flat file.
Word Map on EC 1.4.3.11
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1.4.3.11
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electrode
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biosensors
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amperometric
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microelectrode
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permselective
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diglycidyl
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nafion
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electrodeposited
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chemiluminometric
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analysis
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microbiosensors
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polypyrrole
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biotechnology
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food industry
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medicine
- 1.4.3.11
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electrode
-
biosensors
-
amperometric
-
microelectrode
-
permselective
-
diglycidyl
-
nafion
-
electrodeposited
-
chemiluminometric
- analysis
-
microbiosensors
-
polypyrrole
- biotechnology
- food industry
- medicine
Reaction
Synonyms
dehydrogenase, glutamate (acceptor), GLOD, GluOx, glutamate oxidase, glutamic acid oxidase, glutamic dehydrogenase (acceptor), GOX, L-GLOD, l-GlOx, L-glutamate oxidase, L-glutamic acid oxidase, LGOX
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1.4.3.11 L-glutamate oxidaseAdvanced search results
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Application on EC 1.4.3.11 - L-glutamate oxidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
biotechnology
diagnostics
the R305E mutant enzyme is suitable for the determination of L-arginine. L-Arginine can be a medical biomarker because patients with argininemia or cancer show unusual concentrations of L-arginine in the blood
food industry
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development of a polarographic biosensor for monosodium glutamate by immobilizing L-GLOD on polycarbonate membrane and attached with oxygen electrode with a push cap system, usage of the membrane for over 20 measurements, showing stability
industry
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displaying L-glutamate oxidase/L-amino acid oxidase on the Pichia pastoris surface generates a useful whole cell biocatalyst for 2-oxoglutarate production that can be applied in industry
medicine
synthesis
analysis
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immobilization of L-glutamate oxidase and peroxidase for glutamate determination in flow injection analysis system
analysis
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hydrogel-immobilization of L-glutamate oxidases for a novel thick-film biosensor and application in food samples
analysis
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the enzyme can be used for detectioon of glutamate and H2O2 in a biosensor
analysis
the enzyme is useful as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry
biotechnology
an amperometric microbiosensor for real time monitoring L-glutamate release in neural tissue, based on enzymatic oxidation catalyzed by the L-glutamate oxidase is developed. By means of a sol-gel coating method, L-glutamate oxidase is entrapped in a biocompatible gel layer that provides a benign environment and retains enzyme activity on the surface of Pt microelectrode. Prior to gel layer formation, a modification on the surface of Pt microelectrode with poly(phenylene diamine) enables the microbiosensor screen majority of common potential interfering substances existing in physiological samples. The resulting L-glutamate microbiosensors are characterized by a fast response, high sensitivity, favourable selectivity and excellent long-term stability
biotechnology
application of L-glutamate oxidase with catalase (KatE) to whole-cell systems for glutaric acid production in Escherichia coli. The 2-oxoglutarate regeneration system has potential for improving production in various aminotransferase systems
biotechnology
engineering of L-glutamate oxidase has great potentials to enhance the industrial production of 2-oxoglutarate. A whole-cell biocatalyst for 2-oxoglutarate production is developed by co-expression of both S280T/H533L mutant and KatE catalase. S280T/H533L mutant has high maximal velocity (Vmax: 0.2313 mM/mg/min) and the low Km-value of 2.7 mM. Randomized ribosome binding site (RBS) sequences are introduced to generate vectors with varying expression levels of S280T/H533L and KatE, and two optimized coexpression strains are obtained after screening. The 2-oxoglutarate production reaches a maximum titer of 181.9 g/l after 12 h conversation using the optimized whole-cell biocatalyst, with a molar conversion rate of substrate higher than 86.3% in the absence of exogenous catalase, while the molar conversion rate of substrate using the wild-type biocatalyst is less than 30%
biotechnology
to simplify technological processes and reduce production costs, cascade biocatalysis for 2-oxoglutarate production is constructed by simultaneously expressing L-glutamate oxidase (LGOX) from Streptomyces viridosporus and KatG from Escherichia coli W3110 in Escherichia coli BL21 (DE3). In vivo cascade biocatalysis is constructed and optimized by promoter engineering to finely control the coexpression of LGOX and KatG, thus resulting in a significant increase in 2-oxoglutarate concentration and its conversion rate with no catalase addition
biotechnology
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to simplify technological processes and reduce production costs, cascade biocatalysis for 2-oxoglutarate production is constructed by simultaneously expressing L-glutamate oxidase (LGOX) from Streptomyces viridosporus and KatG from Escherichia coli W3110 in Escherichia coli BL21 (DE3). In vivo cascade biocatalysis is constructed and optimized by promoter engineering to finely control the coexpression of LGOX and KatG, thus resulting in a significant increase in 2-oxoglutarate concentration and its conversion rate with no catalase addition
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medicine
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Pt/polyethyleneimine/GluOx/poly(o-phenylenediamine) biosensors of both cylinder and disk configurations display superb sensitivity in the linear glutamate calibration region, would provide excellent glutamate sensitivity and spatial resolution in neurochemical monitoring involving small brain areas or layered structures in vivo
medicine
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recombinant l-GlOx may be used for food analysis or in the monitoring of L-glutamate as a neurotransmitter, can be used to construct micro sensors and microanalysis systems, performs very similarly to the commercially available wild-type l-GlOx, the recombinant l-GlOx is suitable for mass production
synthesis
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development of glutaric acid production consortium system with 2-oxoglutarate regeneration by glutamate oxidase in Escherichia coli
synthesis
engineering of L-glutamate oxidase has great potentials to enhance the industrial production of 2-oxoglutarate. A whole-cell biocatalyst for 2-oxoglutarate production is developed by co-expression of both S280T/H533L mutant and KatE catalase
synthesis
to simplify technological processes and reduce production costs, cascade biocatalysis for 2-oxoglutarate production is constructed by simultaneously expressing L-glutamate oxidase (LGOX) from Streptomyces viridosporus and KatG from Escherichia coli W3110 in Escherichia coli BL21 (DE3). In vivo cascade biocatalysis is constructed and optimized by promoter engineering to finely control the coexpression of LGOX and KatG, thus resulting in a significant increase in 2-oxoglutarate concentration and its conversion rate with no catalase addition
synthesis
-
to simplify technological processes and reduce production costs, cascade biocatalysis for 2-oxoglutarate production is constructed by simultaneously expressing L-glutamate oxidase (LGOX) from Streptomyces viridosporus and KatG from Escherichia coli W3110 in Escherichia coli BL21 (DE3). In vivo cascade biocatalysis is constructed and optimized by promoter engineering to finely control the coexpression of LGOX and KatG, thus resulting in a significant increase in 2-oxoglutarate concentration and its conversion rate with no catalase addition
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