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4-benzyl-L-glutamate + O2 + H2O
4-benzyl-2-oxoglutarate + NH3 + H2O2
-
13% of the activity with L-glutamate
-
-
?
L-alanine + O2 + H2O
?
-
slight catalytic activity with the micro L-glutamate sensor with recombinant l-GlOx
-
-
?
L-Asp + O2 + H2O
2-oxosuccinamic acid + NH3 + H2O2
-
at 0.6% of the activity with L-glutamate, at pH 7.4, no measurable activity at pH 6.0
-
-
?
L-aspartate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
L-Gln + O2 + H2O
2-oxoglutaric acid 5-amide + NH3 + H2O2
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
L-glutamine + O2 + H2O
2-oxoglutaramate + NH3 + H2O2
L-glutamine + O2 + H2O
? + NH3 + H2O2
-
-
-
-
?
L-His + O2 + H2O
2-oxo-3-(1H-imidazol-4yl)-propionic acid + NH3 + H2O2
L-Tyr + O2 + H2O
3-(4-hydroxyphenyl)-2-oxopropionic acid + NH3 + H2O2
additional information
?
-
L-aspartate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
slight catalytic activity with the micro L-glutamate sensor with recombinant l-GlOx
-
-
?
L-aspartate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
0.6% activity compared to L-glutamate
-
-
?
L-Gln + O2 + H2O
2-oxoglutaric acid 5-amide + NH3 + H2O2
-
2.5% of the activity with L-glutamate at pH 5.0, 32.1% of the activity with L-glutamate at pH 6.8
-
-
?
L-Gln + O2 + H2O
2-oxoglutaric acid 5-amide + NH3 + H2O2
-
2.5% of the activity with L-glutamate at pH 5.0, 32.1% of the activity with L-glutamate at pH 6.8
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
the enzyme exhibits strict specificity for L-glutamate
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
high specificity for L-glutamate
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
100% activity
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
specific substrate
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
wild-type enzyme shows strict substrate specificity for L-glutamate. The R305E mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
no activity with NADP+, methylene blue, thionine and ferricyanide as electron acceptor
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
no activity with NADP+, methylene blue, thionine and ferricyanide as electron acceptor
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
?
L-glutamate + O2 + H2O
2-oxoglutarate + NH3 + H2O2
-
-
-
-
?
L-glutamine + O2 + H2O
2-oxoglutaramate + NH3 + H2O2
0.63% activity compared to L-glutamate
-
-
?
L-glutamine + O2 + H2O
2-oxoglutaramate + NH3 + H2O2
3.6% activity compared to L-glutamate
-
-
?
L-His + O2 + H2O
2-oxo-3-(1H-imidazol-4yl)-propionic acid + NH3 + H2O2
-
2.4% of the activity with L-glutamate, 13.1% of the activity with L-glutamate at pH 6.8
-
-
?
L-His + O2 + H2O
2-oxo-3-(1H-imidazol-4yl)-propionic acid + NH3 + H2O2
-
2.4% of the activity with L-glutamate, 13.1% of the activity with L-glutamate at pH 6.8
-
-
?
L-Tyr + O2 + H2O
3-(4-hydroxyphenyl)-2-oxopropionic acid + NH3 + H2O2
-
2.7% of the activity with L-glutamate
-
-
?
L-Tyr + O2 + H2O
3-(4-hydroxyphenyl)-2-oxopropionic acid + NH3 + H2O2
-
2.7% of the activity with L-glutamate
-
-
?
additional information
?
-
-
no activity with amino acids other than L-glutamate and L-aspartate
-
-
?
additional information
?
-
LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site
-
-
?
additional information
?
-
no activity with L-Leu, L-Phe, L-Asn, L-His, and L-Arg
-
-
?
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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
-
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
-
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
analysis
-
specific and sensitive determination of L-glutamate
analysis
-
immobilization of L-glutamate oxidase and peroxidase for glutamate determination in flow injection analysis system
analysis
-
hydrogel-immobilization of L-glutamate oxidases for a novel thick-film biosensor and application in food samples
analysis
-
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
analysis
-
specific and sensitive determination of L-glutamate
-
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
-
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
-
medicine
-
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
-
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
-
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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Boehmer, A.; Mueller, A.; Passarge, M.; Liebs, P.; Honeck, H.; Mueller, H.G.
A novel L-glutamate oxidase from Streptomyces endus. Purification and properties
Eur. J. Biochem.
182
327-332
1989
Streptomyces hygroscopicus subsp. hygroscopicus
brenda
Kamei, T.; Asano, K.; Kondo, H.; Matsuzaki, M.; Nakamura, S.
L-Glutamate oxidase from Streptomyces violascens. II. Properties
Chem. Pharm. Bull.
31
3609-3616
1983
Streptomyces violascens, Streptomyces violascens H82-N-SY7
-
brenda
Kusakabe, H.; Midorikawa, Y.; Kuninaka, A.; Yoshino, H.
Occurrence of a new enzyme, L-glutamate oxidase in a wheat bran culture extract of Streptomyces sp. X-119-6
Agric. Biol. Chem.
47
179-182
1983
Streptomyces sp.
-
brenda
Kusakabe, H.; Midorikawa, Y.; Fujishima, T.; Kuninaka, A.; Yoshino, H.
Purification and properties of a new enzyme, L-glutamate oxidase, from Streptomyces sp. X-119-6 grown on wheat bran
Agric. Biol. Chem.
47
1323-1328
1983
Streptomyces sp.
-
brenda
Kwong, A.W.K.; Grundig, B.; Hu, J.; Renneberg, R.
Comparative study of hydrogel-immobilized L-glutamate oxidases for a novel thick-film biosensor and its application in food samples
Biotechnol. Lett.
22
267-272
2000
Streptomyces sp.
-
brenda
Li, G.; Zhang, S.; Yu, J.
Immobilization of L-glutamate oxidase and peroxidase for glutamate determination in flow injection analysis system
Appl. Biochem. Biotechnol.
59
53-61
1996
Streptomyces sp.
-
brenda
Sukhacheva, M.V.; Netrusov, A.I.
Extracellular L-glutamate oxidase of Streptomyces sp. Z-11-6: obtainment and properties
Microbiology
69
17-20
2000
Streptomyces sp.
-
brenda
Sukhacheva, M.V.; Zhuravleva, N.I.
Properties of and prospects for practical use of extracellular L-glutamate oxidase of Streptomyces sp. Z-11-6
Appl. Biochem. Microbiol.
40
146-150
2004
Streptomyces sp., Streptomyces sp. Z-11-6
-
brenda
Toshio, K.; Kazuko, A.; Hajime, S.; meiki, M.; Shoshiro, N.
L-Glutamate oxidase from Streptomyces violascens
Chem. Pharm. Bull.
31
1307-1314
1983
Streptomyces violascens
-
brenda
Arima, J.; Tamura, T.; Kusakabe, H.; Ashiuchi, M.; Yagi, T.; Tanaka, H.; Inagaki, K.
Recombinant expression, biochemical characterization and stabilization through proteolysis of an L-glutamate oxidase from Streptomyces sp. X-119-6
J. Biochem.
134
805-812
2003
Streptomyces sp. X-119-6
brenda
Katsos, N.E.; Labrou, N.E.; Clonis, Y.D.
Interaction of L-glutamate oxidase with triazine dyes: selection of ligands for affinity chromatography
J. Chromatogr. B
807
277-285
2004
Streptomyces sp.
brenda
McMahon, C.P.; Rocchitta, G.; Serra, P.A.; Kirwan, S.M.; Lowry, J.P.; ONeill, R.D.
The efficiency of immobilised glutamate oxidase decreases with surface enzyme loading: an electrostatic effect, and reversal by a polycation significantly enhances biosensor sensitivity
Analyst
131
68-72
2006
Streptomyces sp.
brenda
Basu, A.K.; Chattopadhyay, P.; Roychudhuri, U.; Chakraborty, R.
Development of biosensor based on immobilized L-glutamate oxidase for determination of monosodium glutamate in food
Indian J. Exp. Biol.
44
392-398
2006
Streptomyces sp.
brenda
Upadhyay, S.; Ohgami, N.; Kusakabe, H.; Mizuno, H.; Arima, J.; Tamura, T.; Inagaki, K.; Suzuki, H.
Performance characterization of recombinant L-glutamate oxidase in a micro GOT/GPT sensing system
Sens. Actuators B Chem.
B119
570-576
2006
Streptomyces sp.
-
brenda
Zakir Hossain, S.M.; Shinohara, H.; Wang, F.; Kitano, H.
Real-time detection of L-glutamate released from C6 glioma cells using a modified enzyme-luminescence method
Anal. Bioanal. Chem.
389
1961-1966
2007
Streptomyces sp.
brenda
Tian, F.; Gourine, A.V.; Huckstepp, R.T.; Dale, N.
A microelectrode biosensor for real time monitoring of L-glutamate release
Anal. Chim. Acta
645
86-91
2009
Streptomyces sp. X-119-6 (Q8L3C7)
brenda
Arima, J.; Sasaki, C.; Sakaguchi, C.; Mizuno, H.; Tamura, T.; Kashima, A.; Kusakabe, H.; Sugio, S.; Inagaki, K.
Structural characterization of L-glutamate oxidase from Streptomyces sp. X-119-6
FEBS J.
276
3894-3903
2009
Streptomyces sp. X-119-6
brenda
Ammam, M.; Fransaer, J.
Highly sensitive and selective glutamate microbiosensor based on cast polyurethane/AC-electrophoresis deposited multiwalled carbon nanotubes and then glutamate oxidase/electrosynthesized polypyrrole/Pt electrode
Biosens. Bioelectron.
25
1597-1602
2010
Streptomyces sp.
brenda
Arima, J.; Sasaki, C.; Sakaguchi, C.; Mizuno, H.; Tamura, T.; Kashima, A.; Kusakabe, H.; Sugio, S.; Inagaki, K.
Structural characterization of l-glutamate oxidase from Streptomyces sp. X-119-6
FEBS J.
276
4318-4327
2009
Streptomyces sp. (Q8L3C7)
brenda
Utsumi, T.; Arima, J.; Sakaguchi, C.; Tamura, T.; Sasaki, C.; Kusakabe, H.; Sugio, S.; Inagaki, K.
Arg305 of Streptomyces L-glutamate oxidase plays a crucial role for substrate recognition
Biochem. Biophys. Res. Commun.
417
951-955
2012
Streptomyces sp. (Q8L3C7)
brenda
Wang, L.; Peng, R.; Tian, Y.; Liu, M.; Yao, Q.
Isolation and characterization of a novel L-glutamate oxidase with strict substrate specificity from Streptomyces diastatochromogenes
Biotechnol. Lett.
39
523-528
2017
Streptomyces diastatochromogenes (A0A1B1PF34), Streptomyces diastatochromogenes
brenda
Liu, Q.; Ma, X.; Cheng, H.; Xu, N.; Liu, J.; Ma, Y.
Co-expression of L-glutamate oxidase and catalase in Escherichia coli to produce alpha-ketoglutaric acid by whole-cell biocatalyst
Biotechnol. Lett.
39
913-919
2017
Streptomyces mobaraensis (A0A1S6XWY4), Streptomyces mobaraensis
brenda
Niu, P.; Dong, X.; Wang, Y.; Liu, L.
Enzymatic production of alpha-ketoglutaric acid from L-glutamic acid via L-glutamate oxidase
J. Biotechnol.
179
56-62
2014
Streptomyces viridosporus (D6A5I3), Streptomyces viridosporus ATCC14672 (D6A5I3)
brenda
Eynur, F.; Karakus, E.
L-glutamate oxidase enzyme from Hypocrea jecorina Production and biochemical characterization
J. Chem. Soc. Pak.
36
736-743
2014
Trichoderma reesei
-
brenda
YaPing, W.; Ben, R.; Hong, Y.; Rui, H.; Li, L.; Pingan, L.; Lixin, M.
High-level expression of L-glutamate oxidase in Pichia pastoris using multi-copy expression strains and high cell density cultivation
Protein Expr. Purif.
129
108-114
2017
Streptomyces viridosporus (D6A5I3), Streptomyces viridosporus ATCC 14672 (D6A5I3)
brenda
Wu, J.; Fan, X.; Liu, J.; Luo, Q.; Xu, J.; Chen, X.
Promoter engineering of cascade biocatalysis for alpha-ketoglutaric acid production by coexpressing L-glutamate oxidase and catalase
Appl. Microbiol. Biotechnol.
102
4755-4764
2018
Streptomyces viridosporus (D6A5I3), Streptomyces viridosporus, Streptomyces viridosporus ATCC 14672 (D6A5I3)
brenda
Rao, B.; Zhou, R.; Dong, Q.; Liao, X.; Liu, F.; Chen, W.; Liu, X.; Min, Y.; Wang, Y.
Efficient surface display of L-glutamate oxidase and L-amino acid oxidase on Pichia pastoris using multi-copy expression strains
Biotechnol. Bioprocess Eng.
25
571-579
2020
Saccharomyces cerevisiae
-
brenda
Yang, S.Y.; Choi, T.R.; Jung, H.R.; Park, Y.L.; Han, Y.H.; Song, H.S.; Gurav, R.; Bhatia, S.K.; Park, K.; Ahn, J.O.; Yang, Y.H.
Development of glutaric acid production consortium system with alpha-ketoglutaric acid regeneration by glutamate oxidase in Escherichia coli
Enzyme Microb. Technol.
133
109446
2020
Streptomyces mobaraensis
brenda
Zhang, X.; Xu, N.; Li, J.; Ma, Z.; Wei, L.; Liu, Q.; Liu, J.
Engineering of L-glutamate oxidase as the whole-cell biocatalyst for the improvement of alpha-ketoglutarate production
Enzyme Microb. Technol.
136
109530
2020
Streptomyces mobaraensis (A0A1S6XWY4), Streptomyces mobaraensis
brenda
Ham, S.; Han, Y.; Kim, S.; Suh, M.; Cho, J.; Lee, H.; Park, S.; Park, K.; Ahn, J.; Joo, J.; Bhatia, S.; Yang, Y.
Application of l-glutamate oxidase from Streptomyces sp. X119-6 with catalase (KatE) to whole-cell systems for glutaric acid production in Escherichia coli
Korean J. Chem. Engin.
38
2106-2112
2021
Streptomyces sp. X-119-6 (Q8L3C7)
-
brenda
Yano, Y.; Matsuo, S.; Ito, N.; Tamura, T.; Kusakabe, H.; Inagaki, K.; Imada, K.
A new L-arginine oxidase engineered from L-glutamate oxidase
Protein Sci.
30
1044-1055
2021
Streptomyces sp. X-119-6 (Q8L3C7)
brenda