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Literature summary for 1.1.3.4 extracted from

  • Nakamura, S.; Hayashi, S.; Koga, K.
    Effect of periodate oxidation on the structure and properties of glucose oxidase (1976), Biochim. Biophys. Acta, 445, 294-308.
    View publication on PubMed

General Stability

General Stability Organism
SDS, 1%, 30°C, pH 5.5, stable 30 h incubation Aspergillus niger
urea: 7 M, 5 min, activity fully restored Aspergillus niger

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
O2 periodate-oxidized enzyme Aspergillus niger
0.2
-
O2 native enzyme Aspergillus niger
26
-
D-glucose native enzyme Aspergillus niger
28
-
beta-D-glucose periodate-oxidized enzyme Aspergillus niger

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000 153000 periodate-oxidized enzyme Aspergillus niger
150000 153000 sedimentation and diffusion data Aspergillus niger

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Aspergillus niger
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein native enzyme contains 12% carbohydrate by weight, main component: mannose, the carbohydrate moiety plays a role in increasing the stability of the protein moiety, but does not directly participate in the catalytic activity, in the immunological reactivity, or in maintaining the conformation of the enzyme protein, periodate treatment decreases the carbohydrate content to about 40% of its original value Aspergillus niger

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
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
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
72.4
-
denaturation point of native enzyme Aspergillus niger
72.8
-
denaturation point of periodate-oxidized enzyme Aspergillus niger

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
323
-
beta-D-glucose periodate-oxidized enzyme Aspergillus niger
337
-
beta-D-glucose native enzyme Aspergillus niger