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Literature summary extracted from

  • Semashko, T.; Mikhailova, R.; Ramanaviciene, A.; Ramanavicius, A.
    Specificity of glucose oxidase from Penicillium funiculosum 46.1 towards some redox mediators (2013), Appl. Biochem. Biotechnol., 171, 1739-1749 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.3.4 9,10-phenanthrenequinone highly activating redox mediator Talaromyces funiculosus
1.1.3.4 9,10-phenanthroline-5,6-dione highly activating redox mediator Talaromyces funiculosus
1.1.3.4 alpha-methylferrocenemethanol
-
 Talaromyces funiculosus
1.1.3.4 Ferrocene
-
 Talaromyces funiculosus
1.1.3.4 ferrocenecarboxaldehyde
-
 Talaromyces funiculosus
1.1.3.4 ferrocenecarboxylic acid
-
 Talaromyces funiculosus
1.1.3.4 additional information the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation Talaromyces funiculosus
1.1.3.4 N-methylphenazonium methyl sulfate
-
 Talaromyces funiculosus

Application

EC Number Application Comment Organism
1.1.3.4 analysis the enzyme GOx is applied in biosensor technologies Talaromyces funiculosus
1.1.3.4 biofuel production the enzyme used for biofuel cells Talaromyces funiculosus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.3.4 additional information construction of a Penicillium funiculosum highly active strain 46.1 from parental strain BIM F-15 as a producer of extracellular GOx by induced mutagenesis technique. The GOx from Penicillium funiculosum strain 46.1 differs from GOx purified from the parent strain BIM F-15 by reduced Michaelis constant, higher efficiency of glucose oxidation, pH dependence, and thermal stability, but it has similar thermal optimum. The enzyme-encoding gene has no special mutation Talaromyces funiculosus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.4 extracellular
-
 Talaromyces funiculosus
-
-

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 Talaromyces funiculosus
-
 D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 beta-D-glucose + O2 Talaromyces funiculosus 46.1
-
 D-glucono-1,5-lactone + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Talaromyces funiculosus
-
-
-
1.1.3.4 Talaromyces funiculosus 46.1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4 native extracellular enzyme by step-by-step ultrafiltration Talaromyces funiculosus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.4 85.4
-
 purified native extracellular enzyme, pH 7.0, 25°C Talaromyces funiculosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + 1,4-benzoquinone
-
 Talaromyces funiculosus D-glucono-1,5-lactone + hydroquinone
-
 ?
1.1.3.4 beta-D-glucose + 1,4-benzoquinone
-
 Talaromyces funiculosus 46.1 D-glucono-1,5-lactone + hydroquinone
-
 ?
1.1.3.4 beta-D-glucose + O2
-
 Talaromyces funiculosus D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 beta-D-glucose + O2 the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2 Talaromyces funiculosus D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 beta-D-glucose + O2
-
 Talaromyces funiculosus 46.1 D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 beta-D-glucose + O2 the beta-D-glucose serves as a donor of electrons and hydrogen ions, on other side of this complex reaction, oxygen dissolved in water-based reaction media is as an acceptor. Coenzyme FAD acts as electron shuttle during catalytic action of the enzyme, FAD is converted to FADH2 Talaromyces funiculosus 46.1 D-glucono-1,5-lactone + H2O2
-
 ?
1.1.3.4 additional information the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation Talaromyces funiculosus ?
-
 ?
1.1.3.4 additional information the enzyme interacts with redox mediators, e.g. 9,10-phenantroline-5,6-dione, 9,10-phenanthrenequinone, N-methylphenazonium methyl sulfate, ferrocene, ferrocenecarboxylic acid, alpha-methylferrocenemethanol, ferrocenecarboxaldehyde. 9,10-phenantroline-5,6-dione and 9,10-phenanthrenequinone are the best redox mediators or electron acceptors for this type of GOx. The redox mediators in a reaction mixture containing glucose, GOx and 1,4-benzoquinone lead to a 1.4-7.9fold rise of the 1,4-benzoquinone reduction rate, method evaluation Talaromyces funiculosus 46.1 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.3.4 beta-D-glucose/oxygen 1-oxidoreductase
-
 Talaromyces funiculosus
1.1.3.4 GOX
-
 Talaromyces funiculosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.4 25
-
 assay at Talaromyces funiculosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 7
-
 in phosphate buffer Talaromyces funiculosus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.3.4 additional information
-
 the pH correlation of enzyme activity and catalytic characteristics in various buffer systems (phosphate (pH 5.0–9.0), citrate (pH 3.0–5.0), citrate-phosphate (pH 3.0–9.0), and universal (pH 3.0-9.0)) are determined. The GOx is the most efficiently interacting with substrate (glucose) in phosphate buffer at pH 7.0 Talaromyces funiculosus
1.1.3.4 3 9 low activity at pH 3.0 and pH 9.0, high activity at pH 4.0-7.0 depending on the buffer system used Talaromyces funiculosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD coenzyme FAD acts as electron shuttle during catalytic action of the enzyme. The FAD extinction is used for enzyme quantification Talaromyces funiculosus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.3.4 21.825
-
 beta-D-glucose purified native enzyme, pH 7.0, 25°C Talaromyces funiculosus