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
-
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
ECTree
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Crystallization
Crystallization on EC 1.4.3.11 - L-glutamate oxidase
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purified recombinant enzyme, sitting drop vapor diffusion method, mixing of protein solution containing 10 mg/mL protein in 20 mM KPB, pH 7.4, with 5 m; dithiothreitol, with a reservoir solution containing 1.2 M NaH2PO4, 0.8 M K2HPO4, 200 mM LiSO4, 100 mM CAPS, pH 6.2, in a 1:2 ratio, 5°C, 3-4 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution
crystals of mature LGOX are grown at 5°C using the sitting drop vapor diffusion method. The LGOX crystals are formed in the presence of alpha-ketoglutarate. LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site. Comparison of the LGOX structure with that of a structurally homologous model of L-amino acid oxidase (LAAO) from snake venom reveales that LGOX has three regions that are absent from the LAAO structure, one of which is involved in the formation of the entrance. The arrangement of the residues composing the active site differs between LGOX and LAAO, and the active site of LGOX is narrower than that of LAAO
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