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Literature summary for 1.1.3.4 extracted from

  • Suraniti, E.; Courjean, O.; Gounel, S.; Tremey, E.; Mano, N.
    Uncovering and redesigning a key amino acid of glucose oxidase for improved biotechnological applications (2013), Electroanalysis, 25, 606-611 .
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
ferrocenemethanol a redox mediator Penicillium amagasakiense
Os-(tpy)(MeCOOH-bpy)Cl2 a redox mediator Penicillium amagasakiense

Application

Application Comment Organism
analysis te enzyme is used on electrode surfaces of biosensors Penicillium amagasakiense

Protein Variants

Protein Variants Comment Organism
G423D site-directed mutagenesis, the mutant shows no activity compared to the wild-type enzyme Penicillium amagasakiense
G423D site-directed mutagenesis, the mutants containing the mutation G423D leads to quadruple mutants that are not able to reconstitute. The mutant enzymes displays a dramatic decrease in activity compared to thré wild-type enzyme Penicillium amagasakiense
K19E site-directed mutagenesis Penicillium amagasakiense
K23E site-directed mutagenesis Penicillium amagasakiense
K260E. site-directed mutagenesis Penicillium amagasakiense
K424E site-directed mutagenesis, the single mutation results in a significant increase in the current density which becomes 2.4 fold higher than the current obtained for the wild-type Penicillium amagasakiense
K424I site-directed mutagenesis, the mutation does not significantly affect the enzyme activity Penicillium amagasakiense
K48/50E site-directed mutagenesis Penicillium amagasakiense
additional information for use on electrode surfaces, the key amino acid at the entrance of the active site of glucose oxidase from Penicilium amagasakiense, Lys424, Gln75, Gln184, and Gly423, are redesign by nonactive site mutations, leading to enzymatic anodes with 2.4fold higher current densities, making the biosensor more effective. 424 is the key position Penicillium amagasakiense
Q184E site-directed mutagenesis Penicillium amagasakiense
Q75E site-directed mutagenesis Penicillium amagasakiense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
2.6
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
3.2
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
3.4
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
3.8
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
22
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Penicillium amagasakiense
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
GOX
-
Penicillium amagasakiense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Penicillium amagasakiense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
238
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
245
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
250
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
433
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
458
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
464
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1 7 assay at Penicillium amagasakiense

Cofactor

Cofactor Comment Organism Structure
FAD
-
Penicillium amagasakiense

General Information

General Information Comment Organism
additional information 424 is a key position for enzyme activity of the immobilized enzyme on electrode surfaces, overview Penicillium amagasakiense

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
95.2
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
96
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
115
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C Penicillium amagasakiense
120
-
beta-D-glucose recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
122
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme Penicillium amagasakiense
127
-
beta-D-glucose recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense
145
-
beta-D-glucose recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme Penicillium amagasakiense