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Literature summary for 1.1.3.9 extracted from

  • Toftgaard Pedersen, A.; Birmingham, W.; Rehn, G.; Charnock, S.; Turner, N.; Woodley, J.
    Process requirements of galactose oxidase catalyzed oxidation of alcohols (2015), Org. Process Res. Dev., 19, 1580-1589 .
No PubMed abstract available
Search for more literature for 1.1.3.9

Activating Compound

Activating Compound Comment Organism Structure
K3[Fe(CN)6] the inactive form of GOase can be reactivated by further reduction to form the active copper(I) complex or reformation of the radical by single-electron oxidation. In practice, only reoxidation, and not further reduction, of the inactive state is performed to ensure a fully active enzyme, typically using mild chemical oxidants such as potassium ferricyanide Fusarium sp.
additional information protein based single-electron oxidants such as peroxidases can regenerate the active radical center of the enzyme Fusarium sp.
additional information the concentration and type of buffer is essential for the activity of GOase, which is significantly more active in sodium phosphate buffer than in other buffers investigated Fusarium sp.
phosphate
-
 Fusarium sp.

Application

Application Comment Organism
synthesis galactose oxidase is a promising biocatalyst for the oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones, respectively. For this purpose, GOase requires a number of additives to sustain its catalytic function, such as the enzyme catalase for degradation of the byproduct hydrogen peroxide as well as single-electron oxidants to reactivate the enzyme upon loss of the amino acid radical in its active site. GOase can be used to modify naturally occurring polysaccharides with terminal galactose moieties (or other saccharides through GOase mutants) by oxidizing the C6 hydroxyl groups and enabling further chemical or enzymatic modifications of the aldehyde such as amination. And GOase can be applied in the synthesis of a range of industrially relevant compounds containing ketones and aldehydes, such as diformylfuran obtained by selective oxidation of 5-hydroxymethylfurfural. GOase mutants able to enantioselectively oxidize secondary alcohols enable the use of the enzyme for kinetic resolution of racemic mixtures of secondary alcohols Fusarium sp.

Protein Variants

Protein Variants Comment Organism
W290H the mutant is highly activates by phosphate Fusarium sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Fusarium sp.
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a copper-dependent enzyme Fusarium sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Fusarium sp. the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide ?
-
 ?
additional information Fusarium sp. NRLL 2903 the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide ?
-
 ?

Organism

Organism UniProt Comment Textmining
Fusarium sp.
-
-
-
Fusarium sp. NRLL 2903
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification of commercially available GOase mutant M3-5 Fusarium sp.

Reaction

Reaction Comment Organism Reaction ID
D-galactose + O2 = D-galacto-hexodialdose + H2O2 the catalytic mechanism of enzyme GOase can be described by the ping-pong bi bi mechanism, where the alcohol substrate is oxidized in one catalytic halfreaction followed by reoxidation of the enzyme by reduction of oxygen to hydrogen peroxide in a second half-reaction Fusarium sp.
a

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation mutant M3-5 Fusarium sp.
-

Storage Stability

Storage Stability Organism
the enzyme is completely stable for 120 h in buffer with stirring at 25°C, and the activity even increases 30% if the enzyme solution is also aerated in a similar experiment Fusarium sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyl alcohol + O2
-
 Fusarium sp. ? + H2O2
-
 ?
benzyl alcohol + O2
-
 Fusarium sp. NRLL 2903 ? + H2O2
-
 ?
additional information the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide Fusarium sp. ?
-
 ?
additional information galactose oxidase catalyzes oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones, respectively. For this purpose, GOase requires a number of additives to sustain its catalytic function, such as the enzyme catalase for degradation of the byproduct hydrogen peroxide as well as single-electron oxidants to reactivate the enzyme upon loss of the amino acid radical in its active site. The substrate specificity of wild-type GOase is rather restricted, it accepts galactose-containing polysaccharides and also some primary alcohols such as dihydroxyacetone and benzyl alcohol Fusarium sp. ?
-
 ?
additional information the enzyme naturally catalyzes the oxidation of the C6 hydroxyl group of D-galactose to the corresponding aldehyde, while simultaneously reducing molecular oxygen to hydrogen peroxide Fusarium sp. NRLL 2903 ?
-
 ?
additional information galactose oxidase catalyzes oxidation of primary and secondary alcohols to their corresponding aldehydes and ketones, respectively. For this purpose, GOase requires a number of additives to sustain its catalytic function, such as the enzyme catalase for degradation of the byproduct hydrogen peroxide as well as single-electron oxidants to reactivate the enzyme upon loss of the amino acid radical in its active site. The substrate specificity of wild-type GOase is rather restricted, it accepts galactose-containing polysaccharides and also some primary alcohols such as dihydroxyacetone and benzyl alcohol Fusarium sp. NRLL 2903 ?
-
 ?

Synonyms

Synonyms Comment Organism
GOase
-
 Fusarium sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Fusarium sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 the enzyme is completely stable for 120 h in buffer with stirring at 25°C, and the activity even increases 30% if the enzyme solution is also aerated in a similar experiment Fusarium sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
 Fusarium sp.