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Literature summary for 1.4.3.11 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.
    View publication on PubMed
Search for more literature for 1.4.3.11

Application

Application Comment Organism
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)

Cloned (Comment) Organism
expression in Escherichia coli strain JM109 Streptomyces sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
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]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
10000
-
 alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry Streptomyces sp.
17000
-
 alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry Streptomyces sp.
75000
-
 pre-mature enzyme, SDS-PAGE and MALDI-TOF mass spectrometry Streptomyces sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamate + O2 + H2O Streptomyces sp.
-
 2-oxoglutarate + NH3 + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces sp. Q8L3C7
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain JM109 Streptomyces sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + O2 + H2O
-
 Streptomyces sp. 2-oxoglutarate + NH3 + H2O2
-
 ?
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

Subunits Comment Organism
hexamer alpha2beta2gamma2, 2 * 40000-42000, alpha-subunit, 2 * 17000, beta-subunit, + 2 * 10000, gamma-subunit, SDS-PAGE and MALDI-TOF mass spectrometry Streptomyces sp.
monomer 1 * 75000, pre-mature enzyme, SDS-PAGE and MALDI-TOF mass spectrometry Streptomyces sp.
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

Synonyms Comment Organism
LGOX
-
 Streptomyces sp.

Cofactor

Cofactor Comment Organism Structure
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

General Information Comment Organism
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.