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Literature summary extracted from

  • Takegawa, K.; Fujiwara, K.; Iwahara, S.; Yamamoto, K.; Tochikura, T.
    Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger (1989), Biochem. Cell Biol., 67, 460-464.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.1.3.4 freezing/thawing, stable Aspergillus niger
1.1.3.4 SDS, 5%, stable to Aspergillus niger

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.4 4 5.4 beta-D-glucose immobilized enzyme Aspergillus niger
1.1.3.4 37
-
beta-D-glucose native enzyme Aspergillus niger
1.1.3.4 37 38 beta-D-glucose
-
Aspergillus niger
1.1.3.4 38
-
beta-D-glucose carbohydrate-depleted enzyme Aspergillus niger

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.4 87100
-
x * 87100, SDS-PAGE Aspergillus niger

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.3.4 glycoprotein N- and O-linked sugar chains, the enzyme contains 15.2% carbohydrates Aspergillus niger
1.1.3.4 additional information endo-beta-N-acetylglucosaminidase from Flavobacterium sp. releases about 30% of the N-linked sugar chains from the enzyme Aspergillus niger

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4 purchased and further purified by DEAE-Toyopearl 650M column chromatography Aspergillus niger

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
1.1.3.4 ? x * 87100, SDS-PAGE Aspergillus niger

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.4 additional information
-
native and carbohydrate-depleted enzyme, no decrease of activity after 100 freeze-thaw cycles Aspergillus niger
1.1.3.4 50
-
both native and carbonhydrate-depleted enzyme retain full activity below Aspergillus niger
1.1.3.4 55
-
native and carbohydrate-depleted enzyme, inactivation above Aspergillus niger

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 5 6 native and deglycosylated enzyme Aspergillus niger

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.3.4 5 8 native and deglycosylated form Aspergillus niger