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Literature summary for 1.1.3.4 extracted from

  • Seymour, S.L.; Klinman, J.P.
    Comparison of rates and kinetic isotope effects using PEG-modified variants and glycoforms of glucose oxidase: the relationship of modification of the protein envelope to C-H activation and tunneling (2002), Biochemistry, 41, 8747-8758.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information preparation of surface variants that contain artificial polymer poylethylene glycol. All surface modifications of glucose oxidase beyond that of the wild-type enzyme give rise to altered behavior for hydrogen transfer in the active site such that the kinetic isotope effect becomes more temperature-dependent upon perturbation Aspergillus niger

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
136000
-
x * 136000 deglycosylated recombinant enzyme, SDS-PAGE Aspergillus niger
146000
-
x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE Aspergillus niger
155000
-
x * 155000, wild-type enzyme, SDS-PAGE Aspergillus niger
211000
-
x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE Aspergillus niger
320000
-
x * 320000, recombinant enzyme expressed in yeast, SDS-PAGE Aspergillus niger

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-D-glucose + O2 + H2O
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?

Subunits

Subunits Comment Organism
? x * 136000 deglycosylated recombinant enzyme, SDS-PAGE Aspergillus niger
? x * 146000, deglycosylated recombinant enzyme with PEG-350 reagent, SDS-PAGE Aspergillus niger
? x * 155000, wild-type enzyme, SDS-PAGE Aspergillus niger
? x * 211000, deglycosylated recombinant enzyme with PEG-5000 reagent, SDS-PAGE Aspergillus niger
? x * 320000, recombinant enzyme expressed in yeast, SDS-PAGE Aspergillus niger

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.2
-
beta-D-glucose pH 9.0, 33°C, deglycosylated recombinant enzyme with PEG-5000 reagent Aspergillus niger
5.5
-
beta-D-glucose pH 9.0, 33°C, deglycosylated recombinant enzyme with PEG-350 reagent Aspergillus niger
5.9
-
beta-D-glucose pH 9.0, 33°C, recombinant enzyme expressed in yeast Aspergillus niger
6.1
-
beta-D-glucose pH 9.0, 33°C, wild-type enzyme Aspergillus niger
6.3
-
beta-D-glucose pH 9.0, 33°C, deglycosylated recombinant enzyme Aspergillus niger