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User:Christian Bukh/sandbox
From Proteopedia
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Multicopper oxidases contains three different types of copper sites (type 1, type 2 and type 3) defined by their spectroscopic properties. Several structures of multicopper oxidases have been published showing a protein containing high amounts of β-barrel and only low amounts of α-helix structures. | Multicopper oxidases contains three different types of copper sites (type 1, type 2 and type 3) defined by their spectroscopic properties. Several structures of multicopper oxidases have been published showing a protein containing high amounts of β-barrel and only low amounts of α-helix structures. | ||
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<scene name='User:Christian_Bukh/sandbox/1gyc_coppers/1'>TextToBeDisplayed</scene> | <scene name='User:Christian_Bukh/sandbox/1gyc_coppers/1'>TextToBeDisplayed</scene> | ||
Current revision
Test of sandbox
The blue, multicopper oxidase, laccase, (benzenediol oxygen oxidoreductase, E.C. 1.10.3.2) catalyzes single electron oxidation of a broad range of substrates coupled to the four-electron reduction of dioxygen to water. The group of multicopper oxidases contains also e.g. Fet3p from yeast, ascorbate oxidase, and human ceruloplasmin.
Multicopper oxidases contains three different types of copper sites (type 1, type 2 and type 3) defined by their spectroscopic properties. Several structures of multicopper oxidases have been published showing a protein containing high amounts of β-barrel and only low amounts of α-helix structures.
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