galactose oxidase

Copper ion is required as a cofactor for galactose oxidase.

Galactose oxidase is a fungal enzyme of unknown biological function.

Galactose oxidase belongs to the family of oxidoreductases.

A remarkable feature of galactose oxidase is that it is a free radical enzyme.

Galactose oxidase is a type II copper protein.

The free radical in galactose oxidase is unusually stable compared to many other protein free radicals.

Oxidation of asialoerythropoietin with galactose oxidase completely restored in vivo biological activity.

The copper in the active site of galactose oxidase is described as having a "distorted square pyramidal" coordination geometry.

In fact, galactose oxidase catalyzes dihydroxyacetone three times faster than it does to galactose.

Galactose oxidase contains 639 amino acids.

In yeasts, galactose oxidase catalyzes the following reaction:

It has been shown that galactose oxidase is also able to catalyze various primary alcohols other than galactose.

Galactose oxidase has been utilized as a biocatalyst in the synthesis of aldehyde and carboxylic acid from primary alcohol.

For example galactose oxidase will oxidise fructose poorly but is still used in biosensors for fructose.

Supporting evidence comes from that mutation of this tryptophan residue leads to a lower stability of the active form of galactose oxidase.

The catalytic cycle of galactose oxidase (GOase) illustrates the involvement of non-innocent ligands.

Growing cells oxidized lactose to a product that was identical with lactobionate except that it did not serve as a substrate for galactose oxidase.

In the catalytic cycle of galactose oxidase, the enzyme shuttles between the fully oxidized form and the fully reduced form.

Because carbohydrates can normally have primary hydroxyl groups, galactose oxidase can be used to modify cell surface glycoproteins to achieve cell labelling.

Redox non-innocent ligands play a crucial role in the mechanism of catalytic processes mediated by several metalloenzymes, including galactose oxidase and cytochrome P450.

Fig. 8 Oxidation of galactose by galactose oxidase The oxidised polysaccharide has a much higher viscosity and can also form gels.

SCOP also indicated that the beta-propeller in MEGF8 is a member of the galactose oxidase super family.

In the fully oxidized form of galactose oxidase, the free radical couples to the copper(II) center antiferromagnetically, supported by EPR spectroscopic studies.

The hypotonic shock treatment also led to enhanced galactose oxidase catalyzed Na3B3H4 labelling of the membranes and to increased K+-activated ouabain-sensitive p-nitrophenyl phosphatase activity.

Although the oxidation reaction of D-galactose gives galactose oxidase its name, the coupled reduction of dioxygen to hydrogen peroxide is believed to have greater physiological significance in yeasts.