Literature summary extracted from
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 (2009), FEBS J., 276, 4318-4327.
Application
EC Number |
Application |
Comment |
Organism |
---|
1.4.3.11 |
analysis |
the enzyme is useful as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemistry |
Streptomyces sp. |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.4.3.11 |
expression in Escherichia coli strain JM109 |
Streptomyces sp. |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.4.3.11 |
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 |
Streptomyces sp. |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
1.4.3.11 |
10000 |
- |
alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry |
Streptomyces sp. |
1.4.3.11 |
17000 |
- |
alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry |
Streptomyces sp. |
1.4.3.11 |
75000 |
- |
pre-mature enzyme, SDS-PAGE and MALDI-TOF mass spectrometry |
Streptomyces sp. |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.4.3.11 |
L-glutamate + O2 + H2O |
Streptomyces sp. |
- |
2-oxoglutarate + NH3 + H2O2 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.4.3.11 |
Streptomyces sp. |
Q8L3C7 |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
1.4.3.11 |
proteolytic modification |
LGOX is expressed as a single polypeptide precursor in an incompletely active form. It forms a mature enzyme with a hexameric alpha2beta2gamma2 structure formed through protease modification |
Streptomyces sp. |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.4.3.11 |
recombinant enzyme from Escherichia coli strain JM109 |
Streptomyces sp. |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.4.3.11 |
L-glutamate + O2 + H2O |
- |
Streptomyces sp. |
2-oxoglutarate + NH3 + H2O2 |
- |
? |
|
1.4.3.11 |
additional information |
LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site |
Streptomyces sp. |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.4.3.11 |
hexamer |
alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry |
Streptomyces sp. |
1.4.3.11 |
monomer |
1 * 75000, pre-mature enzyme, SDS-PAGE and MALDI-TOF mass spectrometry |
Streptomyces sp. |
1.4.3.11 |
More |
the precursor of LGOX has a homodimeric structure and is less active than the mature enzyme with an alpha2beta2gamma2 structure, structure determination, overview. LGOX has a deeply buried active site and two entrances from the surface of the protein into the active site, amino acid sequence/primary structure analysis, overview |
Streptomyces sp. |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.4.3.11 |
LGOX |
- |
Streptomyces sp. |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.4.3.11 |
FAD |
the enzyme contains one FAD per trimer. The FAD prosthetic group is buried deeply within the enzyme, the isoalloxazine ring of FAD is positioned at the interface between the FAD-binding domain and the substrate-binding domain. It undergoes extensive interactions with the protein residues, overview |
Streptomyces sp. |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.4.3.11 |
additional information |
the precursor of LGOX has a homodimeric structure and is less active than the mature enzyme with an alpha2beta2gamma2 structure, overview |
Streptomyces sp. |