Laccase
From Proteopedia
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EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen | EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen | ||
oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen | oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen | ||
| - | oxidoreductase, EC 1.16.3.1). Similar to the other laccases the three dimensional struture of CotA [[ | + | oxidoreductase, EC 1.16.3.1). Similar to the other laccases the three dimensional struture of CotA [[1w6l]] comprises three cupredoxin domain and four copper ions organised in <scene name='CotA_laccase/Copper_centers/3'>two copper centers</scene>: |
a mononuclear blue type 1 copper centre and a trinuclear centre. | a mononuclear blue type 1 copper centre and a trinuclear centre. | ||
Revision as of 11:16, 6 October 2010
CotA laccase
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CotA laccase belong to the multi-copper oxidase family. The multi-copper oxidases constitute a family of enzymes whose principal members are laccase (benzenediol oxygen oxidoreductase, EC 1.10.3.2), ascorbate oxidase (L-ascorbate oxygen oxidoreductase, EC 1.10.3.3) and ceruloplasmin (Fe(II) oxygen oxidoreductase, EC 1.16.3.1). Similar to the other laccases the three dimensional struture of CotA 1w6l comprises three cupredoxin domain and four copper ions organised in : a mononuclear blue type 1 copper centre and a trinuclear centre.
The trinuclear centre has two type 3 copper ions, that can be anti-ferromagnetically coupled through an hydroxyl moiety in between them, and one type 2 copper ion.‡ The mononuclear copper is able to accept an electron froma variety of phenolic substrates and then transmits it to the trinuclear centre.
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Michal Harel, Isabel Bento, Alexander Berchansky, David Canner, Jaime Prilusky
