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galactose oxidase
Galactose oxidase (D-galactose:oxygen 6-oxidoreductase, D-galactose oxidase, beta-galactose oxidase; abbreviated GAO, GAOX, GOase; ) is an enzyme that catalyzes the oxidation of D-galactose in some species of fungi.
Galactose oxidase belongs to the family of oxidoreductases. Copper ion is required as a cofactor for galactose oxidase. A remarkable feature of galactose oxidase is that it is a free radical enzyme. Its catalytic site contains a free radical ligand coordinating to the copper center.〔 This free radical ligand is a covalently cross-linked cysteine and tyrosine side chains that is formed during post-translational modification.〔〔
==Background==
Found in several fungal species such as ''Fusarium graminearum'' NRRL 2903 (formerly misidentified as ''Dactylium dendroides''), and other species of Fusarium and Aspergillus genera,〔 galactose oxidase is first isolated in 1959. This enzyme is secreted by fungi to function in extracellular space.〔〔 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.〔〔 Hydrogen peroxide which can be produced by yeasts in this way is possibly a bacteriostatic agent.〔
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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